NCBI Conserved Domain Search
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RPS-BLAST 2.2.9 [May-01-2004]
Query= local sequence: htrA 
         (486 letters)

Database: cdd.v2.01
gnl|CDD|27590 cd00987, PDZ_serine_protease, PDZ domain of tryspin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteinsgnl|CDD|27590 cd00987, PDZ_serine_protease, PDZ domain of tryspin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteinsgnl|CDD|27592 cd00989, PDZ_metalloprotease, PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteinsgnl|CDD|27592 cd00989, PDZ_metalloprotease, PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteinsgnl|CDD|27588 cd00136, PDZ, PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domains versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction proteingnl|CDD|27588 cd00136, PDZ, PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domains versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction proteingnl|CDD|27595 cd00992, PDZ_signaling, PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteasesgnl|CDD|27594 cd00991, PDZ_archaeal_metalloprotease, PDZ domain of archaeal zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteinsgnl|CDD|27591 cd00988, PDZ_CTP_protease, PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteinsgnl|CDD|25297 smart00228, PDZ, Domain present in PSD-95, Dlg, and ZO-1/2. Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificitiesgnl|CDD|25297 smart00228, PDZ, Domain present in PSD-95, Dlg, and ZO-1/2. Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificitiesgnl|CDD|25389 pfam00089, Trypsin, Trypsingnl|CDD|25565 pfam00595, PDZ, PDZ domain (Also known as DHR or GLGF). PDZ domains are found in diverse signaling proteinsgnl|CDD|10140 COG0265, DegQ, Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]gnl|CDD|10140 COG0265, DegQ, Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]gnl|CDD|10661 COG0793, Prc, Periplasmic protease [Cell envelope biogenesis, outer membrane]gnl|CDD|13280 COG3975, Predicted protease with the C-terminal PDZ domain [General function prediction only]gnl|CDD|10618 COG0750, Predicted membrane-associated Zn-dependent proteases 1 [Cell envelope biogenesis, outer membrane]
 Domain Relatives
    .. This CD alignment includes 3D structure. To display structure, download Cn3D!
  PSSMs producing significant alignments: Score
(bits)		 E
value
 
gnl|CDD|27590 cd00987, PDZ_serine_protease, PDZ domain of tryspin-like serin... 73.8 4e-14
gnl|CDD|27590 cd00987, PDZ_serine_protease, PDZ domain of tryspin-like serin... 57.6 3e-09
gnl|CDD|27592 cd00989, PDZ_metalloprotease, PDZ domain of bacterial and plan... 48.3 2e-06
gnl|CDD|27592 cd00989, PDZ_metalloprotease, PDZ domain of bacterial and plan... 47.5 3e-06
  gnl|CDD|27588 cd00136, PDZ, PDZ domain, also called DHR (Dlg homologous regi... 46.0 9e-06
  gnl|CDD|27588 cd00136, PDZ, PDZ domain, also called DHR (Dlg homologous regi... 39.1 0.001
gnl|CDD|27595 cd00992, PDZ_signaling, PDZ domain found in a variety of Eumet... 45.6 1e-05
gnl|CDD|27594 cd00991, PDZ_archaeal_metalloprotease, PDZ domain of archaeal ... 44.1 3e-05
gnl|CDD|27591 cd00988, PDZ_CTP_protease, PDZ domain of C-terminal processing... 42.9 8e-05
gnl|CDD|25297 smart00228, PDZ, Domain present in PSD-95, Dlg, and ZO-1/2. Al... 48.1 2e-06
gnl|CDD|25297 smart00228, PDZ, Domain present in PSD-95, Dlg, and ZO-1/2. Al... 39.6 8e-04
gnl|CDD|25389 pfam00089, Trypsin, Trypsin 54.3 3e-08
gnl|CDD|25565 pfam00595, PDZ, PDZ domain (Also known as DHR or GLGF). PDZ do... 43.0 7e-05
  gnl|CDD|10140 COG0265, DegQ, Trypsin-like serine proteases, typically peripl... 198 1e-51
  gnl|CDD|10140 COG0265, DegQ, Trypsin-like serine proteases, typically peripl... 43.7 5e-05
gnl|CDD|10661 COG0793, Prc, Periplasmic protease [Cell envelope biogenesis, ... 44.6 2e-05
  gnl|CDD|13280 COG3975, Predicted protease with the C-terminal PDZ domain [Ge... 40.3 4e-04
  gnl|CDD|10618 COG0750, Predicted membrane-associated Zn-dependent proteases ... 39.8 7e-04

gnl|CDD|27590, cd00987, PDZ_serine_protease, PDZ domain of tryspin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. 
             CD-Length = 90 residues,  96.7% aligned
             Score = 73.8 bits (181), Expect = 4e-14

Query:  293  GEVGILTQDLTPGLAKAFGIDEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGAS  352
Sbjct:  1    PWLGVTVQDLTPDLAEELGLKDTKGVLVASVDPGSPAAKAGLKPGDVILAVNGKPVKSVA  60

Query:  353  DVRRLVGSLPLQSKPSFQIDRASRRIE  379
Sbjct:  61   DLRRALAELKPGDKVTLTVLRGGKELT  87
gnl|CDD|27590, cd00987, PDZ_serine_protease, PDZ domain of tryspin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. 
             CD-Length = 90 residues,  85.6% aligned
             Score = 57.6 bits (139), Expect = 3e-09

Query:  406  ADAEMANSPDGPGARVVVVAEGSVAAQAGLQPDDVIVALDQQPVTDVGQLLSIL--VKEH  463
Sbjct:  13   DLAEELGLKDTKGVLVASVDPGSPAAKAGLKPGDVILAVNGKPVKSVADLRRALAELKPG  72

Query:  464  ARALITVVRNGHRLFVA  480
Sbjct:  73   DKVTLTVLRGGKELTVT  89
gnl|CDD|27592, cd00989, PDZ_metalloprotease, PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. 
             CD-Length = 79 residues,  79.7% aligned
             Score = 48.3 bits (115), Expect = 2e-06

Query:  316  AGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASDVRRLVGSLPLQSKPSFQIDRAS  375
Sbjct:  12   IEPVIGEVVPGSPAAKAGLKAGDRILAINGQKIKSWEDLVDAVQENP-GKPLTLTVERNG  70

Query:  376  RRIE  379
Sbjct:  71   ETIT  74
gnl|CDD|27592, cd00989, PDZ_metalloprotease, PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. 
             CD-Length = 79 residues,  91.1% aligned
             Score = 47.5 bits (113), Expect = 3e-06

Query:  413  SPDGPGARVVV--VAEGSVAAQAGLQPDDVIVALDQQPVTDVGQLLSILVKEHARAL-IT  469
Sbjct:  6    VPGGPPIEPVIGEVVPGSPAAKAGLKAGDRILAINGQKIKSWEDLVDAVQENPGKPLTLT  65

Query:  470  VVRNGHRLFVAA  481
Sbjct:  66   VERNGETITLTL  77
gnl|CDD|27588, cd00136, PDZ, PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein. 
             CD-Length = 70 residues, only  58.6% aligned
             Score = 46.0 bits (109), Expect = 9e-06

Query:  313  DEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASD  353
Sbjct:  10   GTEGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTL  50
gnl|CDD|27588, cd00136, PDZ, PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein. 
             CD-Length = 70 residues,  82.9% aligned
             Score = 39.1 bits (91), Expect = 0.001

Query:  415  DGPGARVVVVAEGSVAAQAGLQPDDVIVALDQQPVTDVGQLLSI-LVKEHARALITVV  471
Sbjct:  11   TEGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEKVTLT  68
gnl|CDD|27595, cd00992, PDZ_signaling, PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases. 
             CD-Length = 82 residues, only  51.2% aligned
             Score = 45.6 bits (108), Expect = 1e-05

Query:  311  GIDEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGAS  352
Sbjct:  21   GKDSGGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLT  62
gnl|CDD|27594, cd00991, PDZ_archaeal_metalloprotease, PDZ domain of archaeal zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. 
             CD-Length = 79 residues, only  53.2% aligned
             Score = 44.1 bits (104), Expect = 3e-05

Query:  316  AGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASDVRRL  357
Sbjct:  10   AGVVIVGVIVGSPAENAVLHTGDVIYSINGTPITTLEDFMEA  51
gnl|CDD|27591, cd00988, PDZ_CTP_protease, PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. 
             CD-Length = 85 residues, only  45.9% aligned
             Score = 42.9 bits (101), Expect = 8e-05

Query:  314  EGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGAS  352
Sbjct:  11   DDGGLVITSVLPGSPAAKAGIKAGDIIVAIDGEPVDGLS  49
gnl|CDD|25297, smart00228, PDZ, Domain present in PSD-95, Dlg, and ZO-1/2. Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. 
             CD-Length = 86 residues, only  70.9% aligned
             Score = 48.1 bits (114), Expect = 2e-06

Query:  313  DEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASDVRRLVGSLPLQSKPSFQID  372
Sbjct:  24   SGDGGVVVSSVVPGSPAAKAGLKPGDVILEVNGTSVEGLTHLEAVDLLKEAGDKVTLTVL  83

Query:  373  R  373
Sbjct:  84   R  84
gnl|CDD|25297, smart00228, PDZ, Domain present in PSD-95, Dlg, and ZO-1/2. Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. 
             CD-Length = 86 residues, only  75.6% aligned
             Score = 39.6 bits (92), Expect = 8e-04

Query:  412  NSPDGPGARVVVVAEGSVAAQAGLQPDDVIVALDQQPVTDVG--QLLSILVKEHARALIT  469
Sbjct:  22   KDSGDGGVVVSSVVPGSPAAKAGLKPGDVILEVNGTSVEGLTHLEAVDLLKEAGDKVTLT  81

Query:  470  VVRNG  474
Sbjct:  82   VLRGG  86
gnl|CDD|25389, pfam00089, Trypsin, Trypsin. 
             CD-Length = 217 residues,  75.1% aligned
             Score = 54.3 bits (130), Expect = 3e-08

Query:  120  SGVVIDEVHGYIVTNQHVIASASKIEVAL-------SDGRRFQAKLVGA------DPET-  165
Sbjct:  27   GGSLISE--NWVLTAAHCVSGASSVRVVLGEHNLGLTEGTEQKFDVKKIIVHPNYNPDTN  84

Query:  166  DVAVVQIPPDH--------LVQAEFGSASSLHVGDVVVAIGNPFGLG-----QTATMGIV  212
Sbjct:  85   DIALLKLKSPVTLGDTVRPICLPSASSSLPVGTTCSVSGWGRTKNLGRSDTLQEVVVPVV  144

Query:  213  S-ALGRRAVGSEGYEGFIQTDA----STNPGNSGGALVSEDGVVV  252
Sbjct:  145  SRETCRSSYGGTVTDTMLCAGALGGKDACQGDSGGPLVCSDGELV  189
gnl|CDD|25565, pfam00595, PDZ, PDZ domain (Also known as DHR or GLGF). PDZ domains are found in diverse signaling proteins. 
             CD-Length = 81 residues, only  48.1% aligned
             Score = 43.0 bits (101), Expect = 7e-05

Query:  317  GALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASDVR  355
Sbjct:  26   GIVVSEVLPGGAAERGGLKEGDRILEINGQDVENVTHER  64
gnl|CDD|10140, COG0265, DegQ, Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones] 
             CD-Length = 347 residues,  93.9% aligned
             Score =  198 bits (504), Expect = 1e-51

Query:  40   LLALAALFIAGESLLSAPAVADS--LSLAPMLQRVVPSVVSISVQGRELDDADATLADPF  97
Sbjct:  8    DLAVGLLLIAAIAGGRALTSAAGQRLSFATAVEKVAPAVVSIATGLTAKLRSFFP-----  62

Query:  98   YRKFFGLPDDAAPAEHSFQSAGSGVVIDEVHGYIVTNQHVIASASKIEVALSDGRRFQAK  157
Sbjct:  63   ----------SDPPLRSAEGLGSGFIISSD-GYIVTNNHVIAGAEEITVTLADGREVPAK  111

Query:  158  LVGADPETDVAVVQIPPDHLVQA-EFGSASSLHVGDVVVAIGNPFGLGQTATMGIVSALG  216
Sbjct:  112  LVGKDPISDLAVLKIDGAGGLPVIALGDSDKLRVGDVVVAIGNPFGLGQTVTSGIVSALG  171

Query:  217  RRAVGSEG-YEGFIQTDASTNPGNSGGALVSEDGVVVGINSAIIGPAGGSIGIGFAVPAE  275
Sbjct:  172  RTGVGSAGGYVNFIQTDAAINPGNSGGPLVNIDGEVVGINTAIIAPSGGSSGIGFAIPVN  231

Query:  276  TVGIVMRQLILTGKLVRGEVGILTQDLTPGLAKAFGIDEGAGALVSEVLPGSPAANAGIQ  335
Sbjct:  232  LVAPVLDELISKGKVVRGYLGVIGEPLTADI--ALGLPVAAGAVVLGVLPGSPAAKAGIK  289

Query:  336  PGDVIRMVDGRTVRGASDVRRLVGSLPLQSKPSFQIDRASRRIE  379
Sbjct:  290  AGDIITAVNGKPVASLSDLVAAVASNRPGDEVALKLLRGGKERE  333
gnl|CDD|10140, COG0265, DegQ, Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones] 
             CD-Length = 347 residues, only  30.8% aligned
             Score = 43.7 bits (102), Expect = 5e-05

Query:  380  AFPVVSDAPVAEPAAPRTIHIGRGPLADAEMANSPDGPGARVVVVAEGSVAAQAGLQPDD  439
Sbjct:  233  VAPVLDELISKGKVVRGYLGVIGEPLTADIALGLPVAAGAVVLGVLPGSPAAKAGIKAGD  292

Query:  440  VIVALDQQPVTDVGQLLSILVKEH--ARALITVVRNGHRLFVAADVQ  484
Sbjct:  293  IITAVNGKPVASLSDLVAAVASNRPGDEVALKLLRGGKERELAVTLG  339
gnl|CDD|10661, COG0793, Prc, Periplasmic protease [Cell envelope biogenesis, outer membrane] 
             CD-Length = 406 residues, only  11.8% aligned
             Score = 44.6 bits (105), Expect = 2e-05

Query:  305  GLAKAFGIDEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGAS  352
Sbjct:  101  GIGIELQMEDIGGVKVVSPIDGSPAAKAGIKPGDVIIKIDGKSVGGVS  148
gnl|CDD|13280, COG3975, COG3975, Predicted protease with the C-terminal PDZ domain [General function prediction only] 
             CD-Length = 558 residues, only  18.6% aligned
             Score = 40.3 bits (94), Expect = 4e-04

Query:  303  TPGLAKAFGIDEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASDVRRLVGSLP  362
Sbjct:  450  AYYLGLKVK-SEGGHEKITFVFPGGPAYKAGLSPGDKIVAINGISDQ--------LDRYK  500

Query:  363  LQSKPSFQIDRASRRIEAFPVVSDAPVAEPAAPRTIHIGRGPLADAEMANSPDGPGAR  420
Sbjct:  501  VNDKIQVHVFREGRLRE-FLVKLGG----DPTAQYIILPIGDRNPAQLANAAAWLGEI  553
gnl|CDD|10618, COG0750, COG0750, Predicted membrane-associated Zn-dependent proteases 1 [Cell envelope biogenesis, outer membrane] 
             CD-Length = 375 residues, only  26.1% aligned
             Score = 39.8 bits (92), Expect = 7e-04

Query:  306  LAKAFGIDEGAGALVSEVLPGSPAANAGIQPGDVIRMVDGRTVRGASDVRRLVGSLPLQS  365
Sbjct:  119  LFFVIGLVPVASPVVGEVAPKSAAALAGLRPGDRIVAVDGEKVASWDDVRRLLVAAAGDV  178

Query:  366  KPSFQIDRASRRIEAFPVVSDAPVAEPAAPRTIHIGRG  403
Sbjct:  179  FNLLTILVIRLDGEAHAVAAEIIKSLGLTPVVIPLKPG  216


Citing 
      CD-Search: Marchler-Bauer A, Anderson JB, DeWeese-Scott C, 
      Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR, Lanczycki 
      CJ, Liebert CA, Liu C, Madej T, Marchler GH, Mazumder R, Nikolskaya AN, 
      Panchenko AR, Rao BS, Shoemaker BA, Simonyan V, Song JS, Thiessen PA, 
      Vasudevan S, Wang Y, Yamashita RA, Yin JJ, and Bryant SH (2003), "CDD: 
      a curated Entrez database of conserved domain alignments", Nucleic 
      Acids Res. 31:383-387. 

  

    

      

      
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