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Conserved domains on  [gi|215713514|dbj|BAG94651|]
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unnamed protein product [Oryza sativa Japonica Group]

Protein Classification

S8 family peptidase( domain architecture ID 15916511)

S8 family peptidase is a subtilisin-like serine protease containing an Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to Arabidopsis thaliana subtilisin-like proteases

CATH:  3.40.50.200
EC:  3.4.-.-
Gene Ontology:  GO:0004252|GO:0006508
MEROPS:  S8
PubMed:  8439290|9070434
SCOP:  3000226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
 124-591 6.95e-118

Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


:

Pssm-ID: 173795 [Multi-domain]  Cd Length: 307  Bit Score: 358.06  E-value: 6.95e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 124 YKLMTTYTPKMVGLTGApaaYHGGLWNRSNMGEGMIIGVLDDGIAAGHPSFDAAGMGPPPARWKGRC----DFNSSVCNN 199
Cdd:cd04852    1 YQLHTTRSPDFLGLPGA---WGGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCvtgeDFNPFSCNN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 200 KLIGARSFFES--AKWKWRGVDDPVLPVYELAHGTHTSSTAGGNFVPGANVMGNGFGTAAGMAPRAHLALYQVCSEDRGC 277
Cdd:cd04852   78 KLIGARYFSDGydAYGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 278 DRDDILAAMDDAVDEGVDVLSISLGDDeAGDFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSNEAPWLLTVAASTt 357
Cdd:cd04852  158 FGSDILAAIDQAIADGVDVISYSIGGG-SPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 358 grkfvatvklgtgvefdgealyqppnfpstqwpliadtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdag 437
Cdd:cd04852      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 438 aagmvligpefmgsmvqpkshilpvaqivylsgeelkaymkstksptaaliykgtvfgdrktpevapfssrgpsrqnqgi 517
Cdd:cd04852      --------------------------------------------------------------------------------

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215713514 518 LKPDITGPGVNIIAGVPVTSGLATPPNPlaAKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTAD 591
Cdd:cd04852  236 LKPDIAAPGVDILAAWTPEGADPGDARG--EDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
 673-773 2.11e-36

Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins.


:

Pssm-ID: 465493  Cd Length: 98  Bit Score: 132.32  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  673 DLNYPSITVFLDREPYVVSVSRAVTNVGPrGKAVYAAKVDMPATVLVTVTPDTLRFKKVNQVRKFTVTFRGANGGpmKGG 752
Cdd:pfam17766   1 DLNYPSIAVSFENLNGSVTVTRTVTNVGD-GPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAP--SGE 77

                          90       100
                  ....*....|....*....|.
gi 215713514  753 VAEGQLRWVSPDHVVRSPIVV 773
Cdd:pfam17766  78 YVFGSLTWSDGKHTVRSPIVV 98
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 364-485 6.82e-27

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


:

Pssm-ID: 239035 [Multi-domain]  Cd Length: 126  Bit Score: 105.96  E-value: 6.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 364 TVKLGTGVEFDGEALYQPPN--FPSTQWPLIADTRGDGTCSDEHLMKEHVAGKLVVCNQGGNLTGLRKGSYLHDAGAAGM 441
Cdd:cd02120    1 VVTLGNGKTIVGQSLYPGNLktYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNTSRVAKGDAVKAAGGAGM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 215713514 442 VLIGPEFMGSMVQPKSHILPVAQIVYLSGEELKAYMKSTKSPTA 485
Cdd:cd02120   81 ILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTA 124
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 41-127 6.78e-10

Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'.


:

Pssm-ID: 428674  Cd Length: 82  Bit Score: 56.15  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514   41 IIVRKPYEYDHNVYKTVSSWHASLLASVcdtAKEELatdpGAETRLIYSYRNVVNGFCARVTREEVYEMAKKDWFVKAIP 120
Cdd:pfam05922   3 IVYLKEGAAAADSFSSHTEWHSSLLRSV---LSEES----SAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEP 75


                  ....*..
gi 215713514  121 EKTYKLM 127
Cdd:pfam05922  76 DQVVKLH 82
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
 124-591 6.95e-118

Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173795 [Multi-domain]  Cd Length: 307  Bit Score: 358.06  E-value: 6.95e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 124 YKLMTTYTPKMVGLTGApaaYHGGLWNRSNMGEGMIIGVLDDGIAAGHPSFDAAGMGPPPARWKGRC----DFNSSVCNN 199
Cdd:cd04852    1 YQLHTTRSPDFLGLPGA---WGGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCvtgeDFNPFSCNN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 200 KLIGARSFFES--AKWKWRGVDDPVLPVYELAHGTHTSSTAGGNFVPGANVMGNGFGTAAGMAPRAHLALYQVCSEDRGC 277
Cdd:cd04852   78 KLIGARYFSDGydAYGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 278 DRDDILAAMDDAVDEGVDVLSISLGDDeAGDFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSNEAPWLLTVAASTt 357
Cdd:cd04852  158 FGSDILAAIDQAIADGVDVISYSIGGG-SPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 358 grkfvatvklgtgvefdgealyqppnfpstqwpliadtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdag 437
Cdd:cd04852      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 438 aagmvligpefmgsmvqpkshilpvaqivylsgeelkaymkstksptaaliykgtvfgdrktpevapfssrgpsrqnqgi 517
Cdd:cd04852      --------------------------------------------------------------------------------

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215713514 518 LKPDITGPGVNIIAGVPVTSGLATPPNPlaAKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTAD 591
Cdd:cd04852  236 LKPDIAAPGVDILAAWTPEGADPGDARG--EDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
 673-773 2.11e-36

Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins.


Pssm-ID: 465493  Cd Length: 98  Bit Score: 132.32  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  673 DLNYPSITVFLDREPYVVSVSRAVTNVGPrGKAVYAAKVDMPATVLVTVTPDTLRFKKVNQVRKFTVTFRGANGGpmKGG 752
Cdd:pfam17766   1 DLNYPSIAVSFENLNGSVTVTRTVTNVGD-GPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAP--SGE 77

                          90       100
                  ....*....|....*....|.
gi 215713514  753 VAEGQLRWVSPDHVVRSPIVV 773
Cdd:pfam17766  78 YVFGSLTWSDGKHTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 140-594 3.96e-30

Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 124.44  E-value: 3.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 140 APAAYHGGLWNRSNMGEGMIIGVLDDGIAAGHPSFdaagmgppparwkgrcdfnssvcNNKLIGARSFfesakwkwrgVD 219
Cdd:COG1404   93 LLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDL-----------------------AGRVVGGYDF----------VD 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 220 DPVLPVYELAHGTHTSSTAGGNfvpganvmGNGFGTAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSI 299
Cdd:COG1404  140 GDGDPSDDNGHGTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNGADVINL 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 300 SLGDDeaGDFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSNEA--PWLLTVAASTtgrkfvatvklgtgvefdgea 377
Cdd:COG1404  212 SLGGP--ADGYSDALAAAVDYAVDKGVLVVAAAGNSGSDDATVSYPAayPNVIAVGAVD--------------------- 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 378 lyqppnfpstqwpliadtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdagaagmvligpefmgsmvqpks 457
Cdd:COG1404      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 458 hilpvaqivylsgeelkaymkstksptaaliykgtvfgdrKTPEVAPFSSRGPsrqnqgilKPDITGPGVNIIAGVPvTS 537
Cdd:COG1404  269 ----------------------------------------ANGQLASFSNYGP--------KVDVAAPGVDILSTYP-GG 299

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215713514 538 GLATppnplaakfdiMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTADTLD 594
Cdd:COG1404  300 GYAT-----------LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLG 345
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 155-596 4.71e-27

Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 111.78  E-value: 4.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  155 GEGMIIGVLDDGIAAGHPSFDAAGMGPPPARWKGRCDFNSSVCNNKligarsffesakwkwRGVDDpvlpvyELAHGTHT 234
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDFNNEWDDPR---------------DDIDD------KNGHGTHV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  235 SSTAGGNfvpganvmGNGFGTAAGMAPRAHLALYQVCSEDRGCDrDDILAAMDDAVDEGVDVLSISLGDDEAGDFAGDPV 314
Cdd:pfam00082  60 AGIIAAG--------GNNSIGVSGVAPGAKILGVRVFGDGGGTD-AITAQAISWAIPQGADVINMSWGSDKTDGGPGSWS 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  315 AL--GAYTAIMRGVFVSSSAGNNGP---NPLTVSNEA--PWLLTVAASTTgrkfvatvklgtgvefdgealyqppnfpst 387
Cdd:pfam00082 131 AAvdQLGGAEAAGSLFVWAAGNGSPggnNGSSVGYPAqyKNVIAVGAVDE------------------------------ 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  388 qwpliadtrgdgtcsdehlmkehvagklvvCNQGgnltglrkgsylhdagaagmvligpefmgsmvqpkshilpvaqivy 467
Cdd:pfam00082 181 ------------------------------ASEG---------------------------------------------- 184

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  468 lsgeelkaymkstksptaaliykgtvfgdrktpEVAPFSSRGPSrqNQGILKPDITGPGVNIIAGVPVTSGLATPPNPLA 547
Cdd:pfam00082 185 ---------------------------------NLASFSSYGPT--LDGRLKPDIVAPGGNITGGNISSTLLTTTSDPPN 229

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 215713514  548 AKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTADTLDRR 596
Cdd:pfam00082 230 QGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDA 278
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 364-485 6.82e-27

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239035 [Multi-domain]  Cd Length: 126  Bit Score: 105.96  E-value: 6.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 364 TVKLGTGVEFDGEALYQPPN--FPSTQWPLIADTRGDGTCSDEHLMKEHVAGKLVVCNQGGNLTGLRKGSYLHDAGAAGM 441
Cdd:cd02120    1 VVTLGNGKTIVGQSLYPGNLktYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNTSRVAKGDAVKAAGGAGM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 215713514 442 VLIGPEFMGSMVQPKSHILPVAQIVYLSGEELKAYMKSTKSPTA 485
Cdd:cd02120   81 ILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTA 124
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 41-127 6.78e-10

Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'.


Pssm-ID: 428674  Cd Length: 82  Bit Score: 56.15  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514   41 IIVRKPYEYDHNVYKTVSSWHASLLASVcdtAKEELatdpGAETRLIYSYRNVVNGFCARVTREEVYEMAKKDWFVKAIP 120
Cdd:pfam05922   3 IVYLKEGAAAADSFSSHTEWHSSLLRSV---LSEES----SAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEP 75


                  ....*..
gi 215713514  121 EKTYKLM 127
Cdd:pfam05922  76 DQVVKLH 82
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 499-623 4.16e-09

type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 59.26  E-value: 4.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  499 TPEVAPFSSRG----PSRQNQGILKPDITGPGVNIIAGVPVTSGLATppnplaakfdiMSGTSMAAPHLSGIAALIKKAH 574
Cdd:TIGR03921 175 YPGVLAVGSIDrdgtPSSFSLPGPWVDLAAPGENIVSLSPGGDGLAT-----------TSGTSFAAPFVSGTAALVRSRF 243

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 215713514  575 PKWSPAAIKSAMMTTADtldrrrRPitdqkGNNANMFGLGAGFINPTKA 623
Cdd:TIGR03921 244 PDLTAAQVRRRIEATAD------HP-----ARGGRDDYVGYGVVDPVAA 281
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 504-569 6.79e-08

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 56.33  E-value: 6.79e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215713514  504 PFSSRGPSRQNqgILKPDITGPGVNIIAgvpvtsglATPPNplaaKFDIMSGTSMAAPHLSGIAAL 569
Cdd:NF040809  992 PTSSRGPTIRN--IQKPDIVAPGVNIIA--------PYPGN----TYATITGTSAAAAHVSGVAAL 1043
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 498-613 2.48e-06

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 51.32  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  498 KTPEVAPFSSRGPSrqNQGILKPDITGPGVNIIAGVPV-TSGLATppnplaakfdimsGTSMAAPHLSGIAAL------I 570
Cdd:NF040809  414 RTDVVSVFSGEGDI--ENGIYKPDLLAPGENIVSYLPGgTTGALT-------------GTSMATPHVTGVCSLlmqwgiV 478

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 215713514  571 KKAHPKWSPAAIKSAMMTTADTLDRRRRPitdqkgNNANMFGL 613
Cdd:NF040809  479 EGNDLFLYSQKLKALLLQNARRSPNRTYP------NNSSGYGF 515
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 397-473 1.42e-04

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 41.35  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  397 GDGTCSDEHLMKEHVAGKLVVCNQGGNLTGLrKGSYLHDAGAAGMVLI--------GPEFMGSMVQPKSHILPVAQIVYL 468
Cdd:pfam02225   8 PGCYAGDGIPADFDVKGKIVLVRCTFGFRAE-KVRNAQAAGAAGVIIYnnveglggPPGAGGNELYPDGIYIPAVGVSRA 86


                  ....*
gi 215713514  469 SGEEL 473
Cdd:pfam02225  87 DGEAL 91
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 522-578 2.34e-03

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 41.49  E-value: 2.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215713514 522 ITGPGVNIIAGVPVTSglatppnplaakFDIMSGTSMAAPHLSGIAALIKKAHPKWS 578
Cdd:PTZ00262 534 LAAPGTNIYSTFPKNS------------YRKLNGTSMAAPHVAAIASLILSINPSLS 578
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
 124-591 6.95e-118

Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173795 [Multi-domain]  Cd Length: 307  Bit Score: 358.06  E-value: 6.95e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 124 YKLMTTYTPKMVGLTGApaaYHGGLWNRSNMGEGMIIGVLDDGIAAGHPSFDAAGMGPPPARWKGRC----DFNSSVCNN 199
Cdd:cd04852    1 YQLHTTRSPDFLGLPGA---WGGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCvtgeDFNPFSCNN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 200 KLIGARSFFES--AKWKWRGVDDPVLPVYELAHGTHTSSTAGGNFVPGANVMGNGFGTAAGMAPRAHLALYQVCSEDRGC 277
Cdd:cd04852   78 KLIGARYFSDGydAYGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 278 DRDDILAAMDDAVDEGVDVLSISLGDDeAGDFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSNEAPWLLTVAASTt 357
Cdd:cd04852  158 FGSDILAAIDQAIADGVDVISYSIGGG-SPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 358 grkfvatvklgtgvefdgealyqppnfpstqwpliadtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdag 437
Cdd:cd04852      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 438 aagmvligpefmgsmvqpkshilpvaqivylsgeelkaymkstksptaaliykgtvfgdrktpevapfssrgpsrqnqgi 517
Cdd:cd04852      --------------------------------------------------------------------------------

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215713514 518 LKPDITGPGVNIIAGVPVTSGLATPPNPlaAKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTAD 591
Cdd:cd04852  236 LKPDIAAPGVDILAAWTPEGADPGDARG--EDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 155-623 3.69e-47

Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173800 [Multi-domain]  Cd Length: 295  Bit Score: 169.82  E-value: 3.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 155 GEGMIIGVLDDGIAAGHPSFdaAGMGPPPARWKGRCDFnssVCNNKLIGARSFFESakwkwrgVDDPVLPVYELAHGTHT 234
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDL--GGPGFPNDKVKGGYDF---VDDDYDPMDTRPYPS-------PLGDASAGDATGHGTHV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 235 SSTAGGNfvpganvmGNGFGTAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSISLGDDEAGdfAGDPV 314
Cdd:cd07474   69 AGIIAGN--------GVNVGTIKGVAPKADLYAYKVLGPGGSGTTDVIIAAIEQAVDDGMDVINLSLGSSVNG--PDDPD 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 315 ALGAYTAIMRGVFVSSSAGNNGPNPLTVSN--EAPWLLTVAASTTGRKFVAtvklgtgvefdgealyqppnfpstqwpli 392
Cdd:cd07474  139 AIAINNAVKAGVVVVAAAGNSGPAPYTIGSpaTAPSAITVGASTVADVAEA----------------------------- 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 393 adtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdagaagmvligpefmgsmvqpkshilpvaqivylsgee 472
Cdd:cd07474      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 473 lkaymkstksptaaliykgtvfgdrktPEVAPFSSRGPSRQNQGIlKPDITGPGVNIIAGVPVTSGlatppnplaaKFDI 552
Cdd:cd07474  190 ---------------------------DTVGPSSSRGPPTSDSAI-KPDIVAPGVDIMSTAPGSGT----------GYAR 231

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215713514 553 MSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTADtldrrrrPITDQKGNNANMFGLGAGFINPTKA 623
Cdd:cd07474  232 MSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAK-------PLYDSDGVVYPVSRQGAGRVDALRA 295
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
 673-773 2.11e-36

Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins.


Pssm-ID: 465493  Cd Length: 98  Bit Score: 132.32  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  673 DLNYPSITVFLDREPYVVSVSRAVTNVGPrGKAVYAAKVDMPATVLVTVTPDTLRFKKVNQVRKFTVTFRGANGGpmKGG 752
Cdd:pfam17766   1 DLNYPSIAVSFENLNGSVTVTRTVTNVGD-GPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAP--SGE 77

                          90       100
                  ....*....|....*....|.
gi 215713514  753 VAEGQLRWVSPDHVVRSPIVV 773
Cdd:pfam17766  78 YVFGSLTWSDGKHTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 140-594 3.96e-30

Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 124.44  E-value: 3.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 140 APAAYHGGLWNRSNMGEGMIIGVLDDGIAAGHPSFdaagmgppparwkgrcdfnssvcNNKLIGARSFfesakwkwrgVD 219
Cdd:COG1404   93 LLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDL-----------------------AGRVVGGYDF----------VD 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 220 DPVLPVYELAHGTHTSSTAGGNfvpganvmGNGFGTAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSI 299
Cdd:COG1404  140 GDGDPSDDNGHGTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNGADVINL 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 300 SLGDDeaGDFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSNEA--PWLLTVAASTtgrkfvatvklgtgvefdgea 377
Cdd:COG1404  212 SLGGP--ADGYSDALAAAVDYAVDKGVLVVAAAGNSGSDDATVSYPAayPNVIAVGAVD--------------------- 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 378 lyqppnfpstqwpliadtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdagaagmvligpefmgsmvqpks 457
Cdd:COG1404      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 458 hilpvaqivylsgeelkaymkstksptaaliykgtvfgdrKTPEVAPFSSRGPsrqnqgilKPDITGPGVNIIAGVPvTS 537
Cdd:COG1404  269 ----------------------------------------ANGQLASFSNYGP--------KVDVAAPGVDILSTYP-GG 299

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215713514 538 GLATppnplaakfdiMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTADTLD 594
Cdd:COG1404  300 GYAT-----------LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLG 345
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 155-596 4.71e-27

Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 111.78  E-value: 4.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  155 GEGMIIGVLDDGIAAGHPSFDAAGMGPPPARWKGRCDFNSSVCNNKligarsffesakwkwRGVDDpvlpvyELAHGTHT 234
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDFNNEWDDPR---------------DDIDD------KNGHGTHV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  235 SSTAGGNfvpganvmGNGFGTAAGMAPRAHLALYQVCSEDRGCDrDDILAAMDDAVDEGVDVLSISLGDDEAGDFAGDPV 314
Cdd:pfam00082  60 AGIIAAG--------GNNSIGVSGVAPGAKILGVRVFGDGGGTD-AITAQAISWAIPQGADVINMSWGSDKTDGGPGSWS 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  315 AL--GAYTAIMRGVFVSSSAGNNGP---NPLTVSNEA--PWLLTVAASTTgrkfvatvklgtgvefdgealyqppnfpst 387
Cdd:pfam00082 131 AAvdQLGGAEAAGSLFVWAAGNGSPggnNGSSVGYPAqyKNVIAVGAVDE------------------------------ 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  388 qwpliadtrgdgtcsdehlmkehvagklvvCNQGgnltglrkgsylhdagaagmvligpefmgsmvqpkshilpvaqivy 467
Cdd:pfam00082 181 ------------------------------ASEG---------------------------------------------- 184

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  468 lsgeelkaymkstksptaaliykgtvfgdrktpEVAPFSSRGPSrqNQGILKPDITGPGVNIIAGVPVTSGLATPPNPLA 547
Cdd:pfam00082 185 ---------------------------------NLASFSSYGPT--LDGRLKPDIVAPGGNITGGNISSTLLTTTSDPPN 229

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 215713514  548 AKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTADTLDRR 596
Cdd:pfam00082 230 QGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDA 278
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 364-485 6.82e-27

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239035 [Multi-domain]  Cd Length: 126  Bit Score: 105.96  E-value: 6.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 364 TVKLGTGVEFDGEALYQPPN--FPSTQWPLIADTRGDGTCSDEHLMKEHVAGKLVVCNQGGNLTGLRKGSYLHDAGAAGM 441
Cdd:cd02120    1 VVTLGNGKTIVGQSLYPGNLktYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNTSRVAKGDAVKAAGGAGM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 215713514 442 VLIGPEFMGSMVQPKSHILPVAQIVYLSGEELKAYMKSTKSPTA 485
Cdd:cd02120   81 ILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTA 124
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 155-591 1.74e-25

Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173812 [Multi-domain]  Cd Length: 264  Bit Score: 106.52  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 155 GEGMIIGVLDDGIAAGHPSFDAAGmgpppARWKGRCDFnssvcnnkligarsffesakwkwrgVDDPVLPVYELAHGTHT 234
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDGRI-----IRFADFVNT-------------------------VNGRTTPYDDNGHGTHV 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 235 SSTAGGNFVPGAnvmgngfGTAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDE----GVDVLSISLGDDEAGDFA 310
Cdd:cd07487   51 AGIIAGSGRASN-------GKYKGVAPGANLVGVKVLDDSGSGSESDIIAGIDWVVENnekyNIRVVNLSLGAPPDPSYG 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 311 GDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSN--EAPWLLTVAASTTgrkfvatvklgtgvefdgealyqppnfpstq 388
Cdd:cd07487  124 EDPLCQAVERLWDAGIVVVVAAGNSGPGPGTITSpgNSPKVITVGAVDD------------------------------- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 389 wpliADTRGDGtcsdehlmkehvagklvvcnqggnltglrkgsylhdagaagmvligpefmgsmvqpkshilpvaqivyl 468
Cdd:cd07487  173 ----NGPHDDG--------------------------------------------------------------------- 179

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 469 sgeelkaymkstksptaaliykgtvfgdrktpeVAPFSSRGPSrqNQGILKPDITGPGVNIIAgvpVTSGLATPPNPLAA 548
Cdd:cd07487  180 ---------------------------------ISYFSSRGPT--GDGRIKPDVVAPGENIVS---CRSPGGNPGAGVGS 221

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 215713514 549 KFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTAD 591
Cdd:cd07487  222 GYFEMSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDTAT 264
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 155-625 9.64e-25

Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173801 [Multi-domain]  Cd Length: 346  Bit Score: 106.20  E-value: 9.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 155 GEGMIIGVLDDGIAAGHPSFdaagMGPPPARWKGRCDFNSSVcNNKLIGARSFFEsakWK-------WRGVDDPVLPVYE 227
Cdd:cd07475   10 GEGMVVAVIDSGVDPTHDAF----RLDDDSKAKYSEEFEAKK-KKAGIGYGKYYN---EKvpfaynyADNNDDILDEDDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 228 LAHGTHTSSTAGGNFVPGANvmGNGFgtaAGMAPRAHLALYQVCS--EDRGCDRDDILAAMDDAVDEGVDVLSISLGDDE 305
Cdd:cd07475   82 SSHGMHVAGIVAGNGDEEDN--GEGI---KGVAPEAQLLAMKVFSnpEGGSTYDDAYAKAIEDAVKLGADVINMSLGSTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 306 AGDFAGDPValgaYTAIMR----GVFVSSSAGNNGpnpltvsneapwllTVAASTTGRKFVATVKLGTGVEfdgealyqP 381
Cdd:cd07475  157 GFVDLDDPE----QQAIKRareaGVVVVVAAGNDG--------------NSGSGTSKPLATNNPDTGTVGS--------P 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 382 PNFPSTqwpliadtrgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdagaagmvligpefmgsmvqpkshiLP 461
Cdd:cd07475  211 ATADDV------------------------------------------------------------------------LT 218

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 462 VAqivylsgeelkAYMKSTKSPTAaliykgtvfgdrktPEVAPFSSRGPSrqNQGILKPDITGPGVNIIAGVPVTsglat 541
Cdd:cd07475  219 VA-----------SANKKVPNPNG--------------GQMSGFSSWGPT--PDLDLKPDITAPGGNIYSTVNDN----- 266

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 542 ppnplaaKFDIMSGTSMAAPHLSGIAALIKKA----HPKWSPA----AIKSAMMTTADtldrrrrPITDQKGNNANMF-- 611
Cdd:cd07475  267 -------TYGYMSGTSMASPHVAGASALVKQRlkekYPKLSGEelvdLVKNLLMNTAT-------PPLDSEDTKTYYSpr 332

                        490
                 ....*....|....
gi 215713514 612 GLGAGFINPTKAMN 625
Cdd:cd07475  333 RQGAGLIDVAKAIA 346
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 157-591 2.29e-21

Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173815 [Multi-domain]  Cd Length: 254  Bit Score: 94.15  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 157 GMIIGVLDDGIAAGHPsfDAAGmgppparwkgrcdfnssvcnnKLIGARSFFESakwkwrGVDDPVLPVYELAHGTHTSS 236
Cdd:cd07490    1 GVTVAVLDTGVDADHP--DLAG---------------------RVAQWADFDEN------RRISATEVFDAGGHGTHVSG 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 237 TAGGnfvpganvmGNGFGTAAGMAPRAHLALYQVCsEDRGCDRDDILAAMDDAVDEGVDVLSISLG-DDEAGDFAGDPV- 314
Cdd:cd07490   52 TIGG---------GGAKGVYIGVAPEADLLHGKVL-DDGGGSLSQIIAGMEWAVEKDADVVSMSLGgTYYSEDPLEEAVe 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 315 ALGAYTaimrGVFVSSSAGNNGPNPLTVSNEAPWLLTVAAsttgrkfvatvklgtgVEFDGEalyqppnfpstqwpliad 394
Cdd:cd07490  122 ALSNQT----GALFVVSAGNEGHGTSGSPGSAYAALSVGA----------------VDRDDE------------------ 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 395 trgdgtcsdehlmkehvagklvvcnqggnltglrkgsylhdagaagmvligpefmgsmvqpkshilpvaQIVYLSGEELK 474
Cdd:cd07490  164 ---------------------------------------------------------------------DAWFSSFGSSG 174

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 475 AYMKStksptaaliykgtvfgdrktpevapfssrGPSRQNQGILKPDITGPGVNIIAGVPVTSGlatppnplAAKFDIMS 554
Cdd:cd07490  175 ASLVS-----------------------------APDSPPDEYTKPDVAAPGVDVYSARQGANG--------DGQYTRLS 217

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 215713514 555 GTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTAD 591
Cdd:cd07490  218 GTSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 155-623 4.52e-18

Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 85.73  E-value: 4.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 155 GEGMIIGVLDDGIAAGHPSFdAAGMGPPPaRWKGRCDFnssvcnnklIGArsffesakwKWRGVDDPVL---PVYELAHG 231
Cdd:cd07489   12 GKGVKVAVVDTGIDYTHPAL-GGCFGPGC-KVAGGYDF---------VGD---------DYDGTNPPVPdddPMDCQGHG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 232 THTSSTAGGNfvpganvmGNGFGtAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSISLGDDeaGDFAG 311
Cdd:cd07489   72 THVAGIIAAN--------PNAYG-FTGVAPEATLGAYRVFGCSGSTTEDTIIAAFLRAYEDGADVITASLGGP--SGWSE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 312 DPVALGAYTAIMRGVFVSSSAGNNGPNpltvsneapwlltvaasttgrkfvatvklgtgvefdgealyqppnfpstqwpl 391
Cdd:cd07489  141 DPWAVVASRIVDAGVVVTIAAGNDGER----------------------------------------------------- 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 392 iadtrgdgtcsdehlmkehvagklvvcnqggnltglrkGSYLHDAGAAGmvligpefmgsmvqpkSHILPVAQIvylsge 471
Cdd:cd07489  168 --------------------------------------GPFYASSPASG----------------RGVIAVASV------ 187

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 472 elkaymKSTksptaaliykgtvfgdrktpevapFSSRGPSrqNQGILKPDITGPGVNIIAGVPVTSGlatppnplaaKFD 551
Cdd:cd07489  188 ------DSY------------------------FSSWGPT--NELYLKPDVAAPGGNILSTYPLAGG----------GYA 225

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215713514 552 IMSGTSMAAPHLSGIAALIKKA-HPKWSPAAIKSAMMTTADTLDRRRRPITDqkGNNANMFGLGAGFINPTKA 623
Cdd:cd07489  226 VLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKPLPWSDGTSAL--PDLAPVAQQGAGLVNAYKA 296
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 159-589 4.33e-17

Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


Pssm-ID: 173787 [Multi-domain]  Cd Length: 241  Bit Score: 81.48  E-value: 4.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 159 IIGVLDDGIAAGHPSFDAAGMGPPPARWKGRCDfnssvcnnkligarsffesakwkwrgvDDPVLPVYELAHGTHTSSTA 238
Cdd:cd00306    2 TVAVIDTGVDPDHPDLDGLFGGGDGGNDDDDNE---------------------------NGPTDPDDGNGHGTHVAGII 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 239 GGNFVPGANVmgngfgtaaGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAV-DEGVDVLSISLGDDEAGDFAGDPVALg 317
Cdd:cd00306   55 AASANNGGGV---------GVAPGAKLIPVKVLDGDGSGSSSDIAAAIDYAAaDQGADVINLSLGGPGSPPSSALSEAI- 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 318 AYTAIMRGVFVSSSAGNNGPNPLTVSNE---APWLLTVAAsttgrkfvatvklgtgvefdgealyqppnfpstqwpliad 394
Cdd:cd00306  125 DYALAKLGVLVVAAAGNDGPDGGTNIGYpaaSPNVIAVGA---------------------------------------- 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 395 trgdgtcsdehlmkehvagklvvCNQGGNLTGlrkgsylhdagaagmvligpefmgsmvqpkshilpvaqivylsgeelk 474
Cdd:cd00306  165 -----------------------VDRDGTPAS------------------------------------------------ 173

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 475 aymkstksptaaliykgtvfgdrktpevaPFSSRGPsrqnqgilKPDITGPGVNIIAGVPVTSGlatppnplaaKFDIMS 554
Cdd:cd00306  174 -----------------------------PSSNGGA--------GVDIAAPGGDILSSPTTGGG----------GYATLS 206

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 215713514 555 GTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTT 589
Cdd:cd00306  207 GTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 501-589 4.28e-16

Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173803 [Multi-domain]  Cd Length: 229  Bit Score: 78.34  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 501 EVAPFSSRGPsrqnqgilKPDITGPGVNIIAGVPVTsglatppnplaaKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPA 580
Cdd:cd07477  161 NRASFSSTGP--------EVELAAPGVDILSTYPNN------------DYAYLSGTSMATPHVAGVAALVWSKRPELTNA 220


                 ....*....
gi 215713514 581 AIKSAMMTT 589
Cdd:cd07477  221 QVRQALNKT 229
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 479-591 2.35e-15

Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases


Pssm-ID: 173791 [Multi-domain]  Cd Length: 293  Bit Score: 77.37  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 479 STKSPTAALIYKGTVFGDRKtPEVAPFSSRGPSRQnqGILKPDITGPGVNIIAGVPVTSGLATPPNPLAAKfdiMSGTSM 558
Cdd:cd04842  179 ASNNPSVSNGEGGLGQSDNS-DTVASFSSRGPTYD--GRIKPDLVAPGTGILSARSGGGGIGDTSDSAYTS---KSGTSM 252

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 215713514 559 AAPHLSGIAALI----------KKAHPkwSPAAIKSAMMTTAD 591
Cdd:cd04842  253 ATPLVAGAAALLrqyfvdgyypTKFNP--SAALLKALLINSAR 293
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 502-575 6.53e-15

Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity.


Pssm-ID: 173807 [Multi-domain]  Cd Length: 264  Bit Score: 75.49  E-value: 6.53e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215713514 502 VAPFSSRGPSRQNQgiLKPDITGPGVNIIAGVPVTSglatppnplaakFDIMSGTSMAAPHLSGIAALIKKAHP 575
Cdd:cd07481  187 LADFSSRGPSTYGR--IKPDISAPGVNIRSAVPGGG------------YGSSSGTSMAAPHVAGVAALLWSANP 246
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 502-601 1.16e-14

Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173804 [Multi-domain]  Cd Length: 455  Bit Score: 77.27  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 502 VAPFSSRGPSRQNqgILKPDITGPGVNIIAgvpvtsglATPPNplaaKFDIMSGTSMAAPHLSGIAALI------KKAHP 575
Cdd:cd07478  359 IAIFSGRGPTRDG--RIKPDIAAPGVNILT--------ASPGG----GYTTRSGTSVAAAIVAGACALLlqwgivRGNDP 424

                         90       100
                 ....*....|....*....|....*.
gi 215713514 576 KWSPAAIKSAMMTTAdtldRRRRPIT 601
Cdd:cd07478  425 YLYGEKIKTYLIRGA----RRRPGDE 446
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 498-591 5.67e-13

Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 69.53  E-value: 5.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 498 KTPEVAPFSSRGPSrqnqgilKPDITGPGVNIIAGVPVTSglatppnplaakFDIMSGTSMAAPHLSGIAALIKKAHPKW 577
Cdd:cd07473  185 SNDALASFSNYGKK-------TVDLAAPGVDILSTSPGGG------------YGYMSGTSMATPHVAGAAALLLSLNPNL 245

                         90
                 ....*....|....
gi 215713514 578 SPAAIKSAMMTTAD 591
Cdd:cd07473  246 TAAQIKDAILSSAD 259
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 503-593 2.23e-11

Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


Pssm-ID: 173810 [Multi-domain]  Cd Length: 260  Bit Score: 64.98  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 503 APFSSRGPsrqnqGIlkpDITGPGVNIIAGVPVTSglatppnplaakFDIMSGTSMAAPHLSGIAALIKKAHPkWSPAAI 582
Cdd:cd07484  190 ASFSNYGK-----WV---DVSAPGGGILSTTPDGD------------YAYMSGTSMATPHVAGVAALLYSQGP-LSASEV 248

                         90
                 ....*....|.
gi 215713514 583 KSAMMTTADTL 593
Cdd:cd07484  249 RDALKKTADDI 259
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 155-616 5.82e-11

Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173806 [Multi-domain]  Cd Length: 297  Bit Score: 64.32  E-value: 5.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 155 GEGMIIGVLDDGIAAGHPSFdaAGMgppparwkgrcdfnssvcnnkLIGARSFFESAKwkwrgVDDpvlpvyELAHGTHT 234
Cdd:cd07480    7 GAGVRVAVLDTGIDLTHPAF--AGR---------------------DITTKSFVGGED-----VQD------GHGHGTHC 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 235 SSTAGGNFVPGANVmgngfgtaaGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSISLGDDEAGDFA-GDP 313
Cdd:cd07480   53 AGTIFGRDVPGPRY---------GVARGAEIALIGKVLGDGGGGDGGILAGIQWAVANGADVISMSLGADFPGLVDqGWP 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 314 VALGaytaimrgvfvsssagnngpnpltvsneapwllTVAASTTGRKFVATVKLGTGVEFDGEALYQppnfpstqwplia 393
Cdd:cd07480  124 PGLA---------------------------------FSRALEAYRQRARLFDALMTLVAAQAALAR------------- 157

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 394 dtrgdgtcsdehlmkehvaGKLVVCnqggnltglrkgsylhdagAAGMVLIGPEFmgsmVQPKSHIlpvaqivylsgeel 473
Cdd:cd07480  158 -------------------GTLIVA-------------------AAGNESQRPAG----IPPVGNP-------------- 181

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 474 kaymkstkSPTAALIYKGTVFGDRKTP---EVAPFSsrgpsrqNQGilkPDITGPGVNIIAgVPVTSGLATppnplaakf 550
Cdd:cd07480  182 --------AACPSAMGVAAVGALGRTGnfsAVANFS-------NGE---VDIAAPGVDIVS-AAPGGGYRS--------- 233

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215713514 551 diMSGTSMAAPHLSGIAALikkahpkWSPAAIKSAMMTTADTLDRRRRPITD---QKGNNANMFGLGAG 616
Cdd:cd07480  234 --MSGTSMATPHVAGVAAL-------WAEALPKAGGRALAALLQARLTAARTtqfAPGLDLPDRGVGLG 293
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 498-591 9.46e-11

Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173818 [Multi-domain]  Cd Length: 261  Bit Score: 63.09  E-value: 9.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 498 KTPEVAPFSSRGPSrqNQGILKPDITGPGVNIIAGVPVTSglatppnplaakFDIMSGTSMAAPHLSGIAALIKKAHPKW 577
Cdd:cd07493  182 ANGNKASFSSIGPT--ADGRLKPDVMALGTGIYVINGDGN------------ITYANGTSFSCPLIAGLIACLWQAHPNW 247

                         90
                 ....*....|....
gi 215713514 578 SPAAIKSAMMTTAD 591
Cdd:cd07493  248 TNLQIKEAILKSAS 261
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 503-594 2.35e-10

Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.


Pssm-ID: 173798 [Multi-domain]  Cd Length: 275  Bit Score: 62.31  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 503 APFSSRGPSrqNQGILKPDITGP-GVNiiagVPVTSGLATPPNplaakfdiMSGTSMAAPHLSGIAALIKKAHPKWSPAA 581
Cdd:cd05562  176 DPVGIRLPT--PEVRQKPDVTAPdGVN----GTVDGDGDGPPN--------FFGTSAAAPHAAGVAALVLSANPGLTPAD 241

                         90
                 ....*....|...
gi 215713514 582 IKSAMMTTADTLD 594
Cdd:cd05562  242 IRDALRSTALDMG 254
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 41-127 6.78e-10

Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'.


Pssm-ID: 428674  Cd Length: 82  Bit Score: 56.15  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514   41 IIVRKPYEYDHNVYKTVSSWHASLLASVcdtAKEELatdpGAETRLIYSYRNVVNGFCARVTREEVYEMAKKDWFVKAIP 120
Cdd:pfam05922   3 IVYLKEGAAAADSFSSHTEWHSSLLRSV---LSEES----SAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEP 75


                  ....*..
gi 215713514  121 EKTYKLM 127
Cdd:pfam05922  76 DQVVKLH 82
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 524-590 3.52e-09

Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.


Pssm-ID: 173790 [Multi-domain]  Cd Length: 255  Bit Score: 58.30  E-value: 3.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215713514 524 GPGVNIIA-GVPVTSGLATPPNplaaKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTA 590
Cdd:cd04077  190 GSCVDIFApGVDILSAWIGSDT----ATATLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 499-623 4.16e-09

type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 59.26  E-value: 4.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  499 TPEVAPFSSRG----PSRQNQGILKPDITGPGVNIIAGVPVTSGLATppnplaakfdiMSGTSMAAPHLSGIAALIKKAH 574
Cdd:TIGR03921 175 YPGVLAVGSIDrdgtPSSFSLPGPWVDLAAPGENIVSLSPGGDGLAT-----------TSGTSFAAPFVSGTAALVRSRF 243

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 215713514  575 PKWSPAAIKSAMMTTADtldrrrRPitdqkGNNANMFGLGAGFINPTKA 623
Cdd:TIGR03921 244 PDLTAAQVRRRIEATAD------HP-----ARGGRDDYVGYGVVDPVAA 281
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 501-590 1.66e-08

Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 57.09  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 501 EVAPFSSRGPSRQnqGILKPDITGPGVNIIAGVPVTSGLATPPNPLAakFDIMSGTSMAAPHLSGIAALIKKAH------ 574
Cdd:cd07497  220 DVVSWSSRGPSIA--GDPKPDLAAIGAFAWAPGRVLDSGGALDGNEA--FDLFGGTSMATPMTAGSAALVISALkekegv 295

                         90
                 ....*....|....*.
gi 215713514 575 PKWSPAAIKSAMMTTA 590
Cdd:cd07497  296 GEYDPFLVRTILMSTA 311
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 504-569 6.79e-08

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 56.33  E-value: 6.79e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215713514  504 PFSSRGPSRQNqgILKPDITGPGVNIIAgvpvtsglATPPNplaaKFDIMSGTSMAAPHLSGIAAL 569
Cdd:NF040809  992 PTSSRGPTIRN--IQKPDIVAPGVNIIA--------PYPGN----TYATITGTSAAAAHVSGVAAL 1043
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 503-589 1.68e-07

Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173820 [Multi-domain]  Cd Length: 285  Bit Score: 53.45  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 503 APFSSRGPSrqnqgilkPDITGPGVNIIAGVPVTSGLATPP---NPLAAKFDIMSGTSMAAPHLSGIAALIKKAHPKWSP 579
Cdd:cd07496  204 ASYSNYGPA--------VDVSAPGGDCASDVNGDGYPDSNTgttSPGGSTYGFLQGTSMAAPHVAGVAALMKSVNPSLTP 275

                         90
                 ....*....|
gi 215713514 580 AAIKSAMMTT 589
Cdd:cd07496  276 AQIESLLQST 285
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 498-613 2.48e-06

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 51.32  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  498 KTPEVAPFSSRGPSrqNQGILKPDITGPGVNIIAGVPV-TSGLATppnplaakfdimsGTSMAAPHLSGIAAL------I 570
Cdd:NF040809  414 RTDVVSVFSGEGDI--ENGIYKPDLLAPGENIVSYLPGgTTGALT-------------GTSMATPHVTGVCSLlmqwgiV 478

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 215713514  571 KKAHPKWSPAAIKSAMMTTADTLDRRRRPitdqkgNNANMFGL 613
Cdd:NF040809  479 EGNDLFLYSQKLKALLLQNARRSPNRTYP------NNSSGYGF 515
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 502-590 3.74e-06

Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin.. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173809 [Multi-domain]  Cd Length: 291  Bit Score: 49.28  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 502 VAPFSsrgpsrqNQGILKPDITGPGVNIIAgvpvtsglATPPNplaaKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAA 581
Cdd:cd07483  221 VANFS-------NYGKKNVDVFAPGERIYS--------TTPDN----EYETDSGTSMAAPVVSGVAALIWSYYPNLTAKE 281


                 ....*....
gi 215713514 582 IKSAMMTTA 590
Cdd:cd07483  282 VKQIILESG 290
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 502-589 3.95e-06

Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


Pssm-ID: 173811 [Multi-domain]  Cd Length: 273  Bit Score: 49.41  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 502 VAPFSSRGpsrqnqgiLKPDITGPGVNIIagvpvtsgLATPP---NPLAAKFDIMSGTSMAAPHLSGIAALIKKAHPK-W 577
Cdd:cd07485  198 KASFSNYG--------RWVDIAAPGVGTI--------LSTVPkldGDGGGNYEYLSGTSMAAPHVSGVAALVLSKFPDvF 261

                         90
                 ....*....|..
gi 215713514 578 SPAAIKSAMMTT 589
Cdd:cd07485  262 TPEQIRKLLEES 273
Peptidases_S8_thiazoline_oxidase_subtilisin-like_p cd07476
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ...
 148-354 4.33e-06

Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase/subtilisin-like protease is produced by the symbiotic bacteria Prochloron spp. that inhabit didemnid family ascidians. The cyclic peptides of the patellamide class found in didemnid extracts are now known to be synthesized by the Prochloron spp. The prepatellamide is heterocyclized to form thiazole and oxazoline rings and the peptide is cleaved to form the two cyclic patellamides A and C. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution).


Pssm-ID: 173802 [Multi-domain]  Cd Length: 267  Bit Score: 49.25  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 148 LWNRSNMGEGMIIGVLDDGIAAGHPSFDAAGMGPPPARWKGRCDfnssvcnnkligarsffesakwkwRGVDDpvlpvye 227
Cdd:cd07476    2 LFAFGGGDPRITIAILDGPVDRTHPCFRGANLTPLFTYAAAACQ------------------------DGGAS------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 228 lAHGTHTSSTAGGNfvPGANVmgngfgtaAGMAPRAHLALYQVCSEDR-GCDRDDILAAMDDAVDEGVDVLSISLG---- 302
Cdd:cd07476   51 -AHGTHVASLIFGQ--PCSSV--------EGIAPLCRGLNIPIFAEDRrGCSQLDLARAINLALEQGAHIINISGGrltq 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 215713514 303 DDEAGDFAGDPVALgaytAIMRGVFVSSSAGNNGPNPLTVSNEAPWLLTVAA 354
Cdd:cd07476  120 TGEADPILANAVAM----CQQNNVLIVAAAGNEGCACLHVPAALPSVLAVGA 167
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 255-336 4.83e-06

Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.


Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 49.62  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 255 TAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDeGVDVLSISLGDDEAGDFAGDPVALGAY--TAIMRGVFVSSSA 332
Cdd:cd04056   82 YAGAIAPGANITLYFAPGTVTNGPLLAFLAAVLDNPN-LPSVISISYGEPEQSLPPAYAQRVCNLfaQAAAQGITVLAAS 160


                 ....
gi 215713514 333 GNNG 336
Cdd:cd04056  161 GDSG 164
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 159-356 5.09e-06

Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173822 [Multi-domain]  Cd Length: 242  Bit Score: 48.49  E-value: 5.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 159 IIGVLDDGIAAGHPSFDAAGMGPPParwkgrcdfnssvcnnkligarsffesakwkWRGVDDPVLPVYELAHGTHTSSTA 238
Cdd:cd07498    2 VVAIIDTGVDLNHPDLSGKPKLVPG-------------------------------WNFVSNNDPTSDIDGHGTACAGVA 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 239 GGNfvpgANvmgNGFGtAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSISLGddeAGDFAGDPVAlgA 318
Cdd:cd07498   51 AAV----GN---NGLG-VAGVAPGAKLMPVRIADSLGYAYWSDIAQAITWAADNGADVISNSWG---GSDSTESISS--A 117

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 215713514 319 YTAI---MR---GVFVSSSAGNNGPNPLTVSNEAPWLLTVAAST 356
Cdd:cd07498  118 IDNAatyGRngkGGVVLFAAGNSGRSVSSGYAANPSVIAVAATD 161
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 230-336 5.25e-06

Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


Pssm-ID: 173808 [Multi-domain]  Cd Length: 294  Bit Score: 48.90  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 230 HGTHTSSTAGGNfvpganvmGNGFGtaagMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSISLG--DDEAG 307
Cdd:cd07482   55 HGTAVAGQIAAN--------GNIKG----VAPGIGIVSYRVFGSCGSAESSWIIKAIIDAADDGVDVINLSLGgyLIIGG 122

                         90       100       110
                 ....*....|....*....|....*....|....
gi 215713514 308 DFAGDPVALGAYTAIMR-----GVFVSSSAGNNG 336
Cdd:cd07482  123 EYEDDDVEYNAYKKAINyakskGSIVVAAAGNDG 156
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 522-591 5.35e-06

Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.


Pssm-ID: 173794 [Multi-domain]  Cd Length: 267  Bit Score: 48.86  E-value: 5.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 522 ITGPGVNIIAGVPVTSGlatppnplaaKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTAD 591
Cdd:cd04848  208 LAAPGENIYSTDPDGGN----------GYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 504-590 1.32e-05

Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II are member of the peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing.


Pssm-ID: 173796 [Multi-domain]  Cd Length: 412  Bit Score: 48.43  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 504 PFSSRGPSrqNQGILKPDITGPGvNIIAGVPvtsglatppNPLAAKFDIMSGTSMAAPHLSGIAALI----KKAHPKWSP 579
Cdd:cd04857  331 TWSSRGPT--ADGALGVSISAPG-GAIASVP---------NWTLQGSQLMNGTSMSSPNACGGIALLlsglKAEGIPYTP 398

                         90
                 ....*....|.
gi 215713514 580 AAIKSAMMTTA 590
Cdd:cd04857  399 YSVRRALENTA 409
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
 521-600 4.12e-05

Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173797 [Multi-domain]  Cd Length: 239  Bit Score: 45.74  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 521 DITGPGVNIIAGvpvtsglatppnPLAAKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTADTLDRRRRPI 600
Cdd:cd05561  168 DFAAPGVDVWVA------------APGGGYRYVSGTSFAAPFVTAALALLLQASPLAPDDARARLAATAKDLGPPGRDPV 235
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 504-587 1.24e-04

Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173793 [Multi-domain]  Cd Length: 291  Bit Score: 44.60  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 504 PFSSRGPSRQnqGILKPDITGPGVNIIAGVPVT------SGLATPPNPLAAKFDIMSGTSMAAPHLSGIAALIKKAHPKW 577
Cdd:cd04847  200 ATTSSGPGSP--GPIKPDVVAFGGNLAYDPSGNaadgdlSLLTTLSSPSGGGFVTVGGTSFAAPLAARLAAGLFAELPEL 277

                         90
                 ....*....|
gi 215713514 578 SPAAIKsAMM 587
Cdd:cd04847  278 SPETIR-ALL 286
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 397-473 1.42e-04

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 41.35  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514  397 GDGTCSDEHLMKEHVAGKLVVCNQGGNLTGLrKGSYLHDAGAAGMVLI--------GPEFMGSMVQPKSHILPVAQIVYL 468
Cdd:pfam02225   8 PGCYAGDGIPADFDVKGKIVLVRCTFGFRAE-KVRNAQAAGAAGVIIYnnveglggPPGAGGNELYPDGIYIPAVGVSRA 86


                  ....*
gi 215713514  469 SGEEL 473
Cdd:pfam02225  87 DGEAL 91
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 229-342 1.83e-04

Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II are member of the peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing.


Pssm-ID: 173796 [Multi-domain]  Cd Length: 412  Bit Score: 44.58  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 229 AHGTHTSSTAGGNFV--PGANvmgngfgtaaGMAPRAhlalyQVCSEDRGCDRDD-------ILAAMDDAVDEGVDVLSI 299
Cdd:cd04857  186 AHGTHVAGIAAAHFPeePERN----------GVAPGA-----QIVSIKIGDTRLGsmetgtaLVRAMIAAIETKCDLINM 250

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 215713514 300 SLGDDEAGDFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTV 342
Cdd:cd04857  251 SYGEATHWPNSGRIIELMNEAVNKHGVIFVSSAGNNGPALSTV 293
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 149-346 3.91e-04

Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound subtilisin-kexin-isoenzyme) proteins are secretory Ca2+-dependent serine proteinases cleave at nonbasic residues: Thr, Leu, and Lys. SKI-1s play a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 42.83  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 149 WNRSNMGEGMIIGVLDDGIAAGHPSFdaagmgppparwkgrcdfnssvcnnkligaRSFFESAKW-KWRGVDDpvlpvyE 227
Cdd:cd07479    1 WQLGYTGAGVKVAVFDTGLAKDHPHF------------------------------RNVKERTNWtNEKTLDD------G 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 228 LAHGThtsstaggnFVPGanVMGNGFGTAAGMAPRAHLALYQVCSEDRGCDRDDILAAMDDAVDEGVDVLSISLGddeAG 307
Cdd:cd07479   45 LGHGT---------FVAG--VIASSREQCLGFAPDAEIYIFRVFTNNQVSYTSWFLDAFNYAILTKIDVLNLSIG---GP 110

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 215713514 308 DFAGDPVALGAYTAIMRGVFVSSSAGNNGPNPLTVSNEA 346
Cdd:cd07479  111 DFMDKPFVDKVWELTANNIIMVSAIGNDGPLYGTLNNPA 149
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 465-590 3.92e-04

Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173813  Cd Length: 247  Bit Score: 42.84  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 465 IVYLSGEELKAYMKSTKSPTAALIYKGTVFG---DRKTPEVAPFSSRGPSRQNQGIL-KPDITGPGVNIiagvpvtsgla 540
Cdd:cd07488  126 NVFSAGNQGKEKEKFGGISIPTLAYNSIVVGstdRNGDRFFASDVSNAGSEINSYGRrKVLIVAPGSNY----------- 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215713514 541 tppNPLAAKFDIMSGTSMAAPHLSGIAALI------KKAHPKWSPAAIKSAMMTTA 590
Cdd:cd07488  195 ---NLPDGKDDFVSGTSFSAPLVTGIIALLlefydrQYKKGNNNLIALRALVSSSV 247
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 503-589 4.14e-04

Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173822 [Multi-domain]  Cd Length: 242  Bit Score: 42.71  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 503 APFSSRGPSrqnqgilkPDITGPGVNI-IAGVPVTSGLATPPNplaaKFDIMSGTSMAAPHLSGIAALIKKAHPKWSPAA 581
Cdd:cd07498  167 ASYSNYGNY--------VDLVAPGVGIwTTGTGRGSAGDYPGG----GYGSFSGTSFASPVAAGVAALILSANPNLTPAE 234


                 ....*...
gi 215713514 582 IKSAMMTT 589
Cdd:cd07498  235 VEDILTST 242
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 541-590 4.15e-04

Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 43.23  E-value: 4.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 215713514 541 TPPNPLAAKFdimSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTTA 590
Cdd:cd07494  236 TPPNDGWGVF---SGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTA 282
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 502-593 4.17e-04

Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound subtilisin-kexin-isoenzyme) proteins are secretory Ca2+-dependent serine proteinases cleave at nonbasic residues: Thr, Leu, and Lys. SKI-1s play a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 42.83  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 502 VAPFSSRGPSR----QNQGILKPDITGPGVNIIaGVPVTSGLATppnplaakfdiMSGTSMAAPHLSGIAALIKKAHPK- 576
Cdd:cd07479  166 IARFSSRGMTTwelpGGYGRVKPDIVTYGSGVY-GSKLKGGCRA-----------LSGTSVASPVVAGAVALLLSTVPEk 233

                         90       100
                 ....*....|....*....|
gi 215713514 577 ---WSPAAIKSAMMTTADTL 593
Cdd:cd07479  234 rdlINPASMKQALIESATRL 253
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 512-590 6.70e-04

Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173817 [Multi-domain]  Cd Length: 222  Bit Score: 41.94  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 512 RQNQGILKPDIT--GPGVNIIAGVPVTSGLATppnplaakfdimSGTSMAAPHLSGIAALIKKAHPKWSPAAIKSAMMTT 589
Cdd:cd07492  153 DDPKSFWYIYVEfsADGVDIIAPAPHGRYLTV------------SGNSFAAPHVTGMVALLLSEKPDIDANDLKRLLQRL 220


                 .
gi 215713514 590 A 590
Cdd:cd07492  221 A 221
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 230-356 7.53e-04

Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.


Pssm-ID: 173790 [Multi-domain]  Cd Length: 255  Bit Score: 42.12  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215713514 230 HGTHTSSTAGGN---FVPGANVMG------NGFGTAAGmaprahlalyqvcsedrgcdrddILAAMDDAVDEGVD----- 295
Cdd:cd04077   65 HGTHVAGTVGGKtygVAKKANLVAvkvldcNGSGTLSG-----------------------IIAGLEWVANDATKrgkpa 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215713514 296 VLSISLGddeagdfagdpvalGAYTAIM---------RGVFVSSSAGNNGPNPLTVSNE-APWLLTVAAST 356
Cdd:cd04077  122 VANMSLG--------------GGASTALdaavaaavnAGVVVVVAAGNSNQDACNYSPAsAPEAITVGATD 178
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 522-578 2.34e-03

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 41.49  E-value: 2.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215713514 522 ITGPGVNIIAGVPVTSglatppnplaakFDIMSGTSMAAPHLSGIAALIKKAHPKWS 578
Cdd:PTZ00262 534 LAAPGTNIYSTFPKNS------------YRKLNGTSMAAPHVAAIASLILSINPSLS 578
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 501-571 6.58e-03

Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


Pssm-ID: 173808 [Multi-domain]  Cd Length: 294  Bit Score: 39.27  E-value: 6.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215713514 501 EVAPFSSRGPSRQN-----QGILKPDITGPGVNIIAG-VPVTSGLATPPNplaAKFDIMSGTSMAAPHLSGIAALIK 571
Cdd:cd07482  202 NLSSFSNYGNSRIDlaapgGDFLLLDQYGKEKWVNNGlMTKEQILTTAPE---GGYAYMYGTSLAAPKVSGALALII 275
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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