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Conserved domains on  [gi|18424157|ref|NP_568888|]
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Subtilisin-like serine endopeptidase family protein [Arabidopsis thaliana]

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 ...
 104-529 1.58e-124

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: 372.70  E-value: 1.58e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 104 YKLQTTASWDFLGLkEGKNTKRNLAIE---SDTIIGFIDSGIWPESESFSDKGFGPPPKKWKGVCSGGKNFT---CNNKL 177
Cdd:cd04852   1 YQLHTTRSPDFLGL-PGAWGGSLLGAAnagEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNpfsCNNKL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 178 IGARDYtSEGT---------------RDLQGHGTHTASTAAGNAVADASFFGIGNGTARGGVPASRIAAYKVCSEKD-CT 241
Cdd:cd04852  80 IGARYF-SDGYdayggfnsdgeyrspRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGgCF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 242 AASLLSAFDDAIADGVDLISISLASeFPQKYYKDAIAIGAFHANVKGILTVNSAGNSGSFPSTTASVAPWILSVAASNtn 321
Cdd:cd04852 159 GSDILAAIDQAIADGVDVISYSIGG-GSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST-- 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 322 rgfftkvvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfs 401
Cdd:cd04852     --------------------------------------------------------------------------------

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 402 llppddfdslvsyinstrspqgtflkteaffnqtaptvasfssrgpnfiavdlLKPDISAPGVEILAAYSPLGSPSEees 481
Cdd:cd04852 236 -----------------------------------------------------LKPDIAAPGVDILAAWTPEGADPG--- 259

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 18424157 482 DKRRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTTAW 529
Cdd:cd04852 260 DARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
 601-700 1.94e-32

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: 120.77  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   601 NLNYPSMSakIDGYNSSFTVTFKRTVTNLGTPNSTYKSKIVLNHGAKlVKVSPSVLSFKRVNEKQSFTVTFSGNLNLNLP 680
Cdd:pfam17766   1 DLNYPSIA--VSFENLNGSVTVTRTVTNVGDGPSTYTASVTAPPGVS-VTVSPSTLVFTKVGEKKSFTVTFTATKAPSGE 77

                          90       100
                  ....*....|....*....|.
gi 18424157   681 -TSANLIWSDGTHNVRSVIVV 700
Cdd:pfam17766  78 yVFGSLTWSDGKHTVRSPIVV 98
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 29-107 5.77e-18

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: 78.87  E-value: 5.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157    29 VYVVYMGSL--PSLLEYTPLSHHMSILQEVTGD-SSVEGRLVRSYKRSFNGFAARLTESERIRVAEMEGVVSVFPNINYK 105
Cdd:pfam05922   1 TYIVYLKEGaaAADSFSSHTEWHSSLLRSVLSEeSSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80


                  ..
gi 18424157   106 LQ 107
Cdd:pfam05922  81 LH 82
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 328-424 1.06e-08

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: 53.96  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 328 VVLGNGKTLVGRSVNSFDLkgKKYPLVYGDNF--------------NESLVQGKILV----SKFPTSSKV-------AVG 382
Cdd:cd02120   2 VTLGNGKTIVGQSLYPGNL--KTYPLVYKSANsgdvdaslclpgslDPSKVKGKIVLcdrgGNTSRVAKGdavkaagGAG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18424157 383 SILIDD--YQHYALLSSK--PFSLLPPDDFDSLVSYINSTRSPQGT 424
Cdd:cd02120  80 MILANDptDGLDVVADAHvlPAVHVDYEDGTAILSYINSTSNPTAT 125
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
 104-529 1.58e-124

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: 372.70  E-value: 1.58e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 104 YKLQTTASWDFLGLkEGKNTKRNLAIE---SDTIIGFIDSGIWPESESFSDKGFGPPPKKWKGVCSGGKNFT---CNNKL 177
Cdd:cd04852   1 YQLHTTRSPDFLGL-PGAWGGSLLGAAnagEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNpfsCNNKL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 178 IGARDYtSEGT---------------RDLQGHGTHTASTAAGNAVADASFFGIGNGTARGGVPASRIAAYKVCSEKD-CT 241
Cdd:cd04852  80 IGARYF-SDGYdayggfnsdgeyrspRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGgCF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 242 AASLLSAFDDAIADGVDLISISLASeFPQKYYKDAIAIGAFHANVKGILTVNSAGNSGSFPSTTASVAPWILSVAASNtn 321
Cdd:cd04852 159 GSDILAAIDQAIADGVDVISYSIGG-GSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST-- 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 322 rgfftkvvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfs 401
Cdd:cd04852     --------------------------------------------------------------------------------

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 402 llppddfdslvsyinstrspqgtflkteaffnqtaptvasfssrgpnfiavdlLKPDISAPGVEILAAYSPLGSPSEees 481
Cdd:cd04852 236 -----------------------------------------------------LKPDIAAPGVDILAAWTPEGADPG--- 259

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 18424157 482 DKRRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTTAW 529
Cdd:cd04852 260 DARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
 601-700 1.94e-32

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: 120.77  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   601 NLNYPSMSakIDGYNSSFTVTFKRTVTNLGTPNSTYKSKIVLNHGAKlVKVSPSVLSFKRVNEKQSFTVTFSGNLNLNLP 680
Cdd:pfam17766   1 DLNYPSIA--VSFENLNGSVTVTRTVTNVGDGPSTYTASVTAPPGVS-VTVSPSTLVFTKVGEKKSFTVTFTATKAPSGE 77

                          90       100
                  ....*....|....*....|.
gi 18424157   681 -TSANLIWSDGTHNVRSVIVV 700
Cdd:pfam17766  78 yVFGSLTWSDGKHTVRSPIVV 98
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 131-548 7.30e-31

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: 122.57  E-value: 7.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   131 SDTIIGFIDSGIWPESESFSDKGFGPPPKKWKGVCSGGKNFTCNNKLIgardytsegtRDLQGHGTHTASTAAGNAVADA 210
Cdd:pfam00082   2 KGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDFNNEWDDPRDDI----------DDKNGHGTHVAGIIAAGGNNSI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   211 SFFGIgngtarggVPASRIAAYKVCSEKDCTAASLLSAFDDAIADGVDLISISLASEFPQKY---YKDAIAiGAFHANVK 287
Cdd:pfam00082  72 GVSGV--------APGAKILGVRVFGDGGGTDAITAQAISWAIPQGADVINMSWGSDKTDGGpgsWSAAVD-QLGGAEAA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   288 GILTVNSAGNSGSFPSTTASVApwilsvaasntnrgfftkvvlgngktlvgrsvnsfdlkgkkyplvYGDNFNESLvqgk 367
Cdd:pfam00082 143 GSLFVWAAGNGSPGGNNGSSVG---------------------------------------------YPAQYKNVI---- 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   368 ilvskfptsskvAVGSILiddyqhyallsskpfsllppddfdslvsyinstrspqgtflkteaffNQTAPTVASFSSRGP 447
Cdd:pfam00082 174 ------------AVGAVD-----------------------------------------------EASEGNLASFSSYGP 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   448 NFIavDLLKPDISAPGVEIlAAYSPLGSPSEEESDKRRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTT 527
Cdd:pfam00082 195 TLD--GRLKPDIVAPGGNI-TGGNISSTLLTTTSDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNT 271

                         410       420
                  ....*....|....*....|.
gi 18424157   528 AWPMKPNRPgfastEFAYGAG 548
Cdd:pfam00082 272 ATDLGDAGL-----DRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 175-561 1.94e-30

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 125.21  E-value: 1.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 175 NKLIGARDYTS--EGTRDLQGHGTHTASTAAGNavadasffGIGNGTARGGVPASRIAAYKVCSEK-DCTAASLLSAFDD 251
Cdd:COG1404 129 GRVVGGYDFVDgdGDPSDDNGHGTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDDNgSGTTSDIAAAIDW 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 252 AIADGVDLISISLASEFPQKY--YKDAIAigafHANVKGILTVNSAGNSGSFPSTTAS--VAPWILSVAASNTNRgfftk 327
Cdd:COG1404 201 AADNGADVINLSLGGPADGYSdaLAAAVD----YAVDKGVLVVAAAGNSGSDDATVSYpaAYPNVIAVGAVDANG----- 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 328 vvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfsllppdd 407
Cdd:COG1404     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 408 fdslvsyinstrspqgtflkteaffnqtapTVASFSSRGPnfiavdllKPDISAPGVEILAAYsPLGSpseeesdkrrvk 487
Cdd:COG1404 272 ------------------------------QLASFSNYGP--------KVDVAAPGVDILSTY-PGGG------------ 300

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18424157 488 YSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTTAWPMKPNRPgfastefAYGAGHVDQIAAINPGLV 561
Cdd:COG1404 301 YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGP-------YYGYGLLADGAAGATSAG 367
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 29-107 5.77e-18

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: 78.87  E-value: 5.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157    29 VYVVYMGSL--PSLLEYTPLSHHMSILQEVTGD-SSVEGRLVRSYKRSFNGFAARLTESERIRVAEMEGVVSVFPNINYK 105
Cdd:pfam05922   1 TYIVYLKEGaaAADSFSSHTEWHSSLLRSVLSEeSSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80


                  ..
gi 18424157   106 LQ 107
Cdd:pfam05922  81 LH 82
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 328-424 1.06e-08

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: 53.96  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 328 VVLGNGKTLVGRSVNSFDLkgKKYPLVYGDNF--------------NESLVQGKILV----SKFPTSSKV-------AVG 382
Cdd:cd02120   2 VTLGNGKTIVGQSLYPGNL--KTYPLVYKSANsgdvdaslclpgslDPSKVKGKIVLcdrgGNTSRVAKGdavkaagGAG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18424157 383 SILIDD--YQHYALLSSK--PFSLLPPDDFDSLVSYINSTRSPQGT 424
Cdd:cd02120  80 MILANDptDGLDVVADAHvlPAVHVDYEDGTAILSYINSTSNPTAT 125
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 443-506 6.91e-07

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: 52.86  E-value: 6.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18424157   443 SSRGPNFIavDLLKPDISAPGVEILAAYsplgsPSEeesdkrrvKYSVMSGTSMSCPHVAGVAA 506
Cdd:NF040809  994 SSRGPTIR--NIQKPDIVAPGVNIIAPY-----PGN--------TYATITGTSAAAAHVSGVAA 1042
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 432-506 7.64e-05

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: 46.31  E-value: 7.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18424157   432 FNQTAPTVASFSSRGPnfIAVDLLKPDISAPGVEILAaYSPLGSPSeeesdkrrvkysVMSGTSMSCPHVAGVAA 506
Cdd:NF040809  411 FNSRTDVVSVFSGEGD--IENGIYKPDLLAPGENIVS-YLPGGTTG------------ALTGTSMATPHVTGVCS 470
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 418-516 3.64e-03

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 40.72  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157  418 TRSPQGTFLKTEAFFNQTAPTVASFSSRgpNFIAVDLLKPDISA-----PGVEILAAYSPLGSPSEE-ESDKRRVKYSVM 491
Cdd:PTZ00262 476 TKESKPDIPKCDLDVNKVYPPILSKKLR--NVITVSNLIKDKNNqyslsPNSFYSAKYCQLAAPGTNiYSTFPKNSYRKL 553

                         90       100
                 ....*....|....*....|....*
gi 18424157  492 SGTSMSCPHVAGVAAYIRTFHPKWS 516
Cdd:PTZ00262 554 NGTSMAAPHVAAIASLILSINPSLS 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 ...
 104-529 1.58e-124

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: 372.70  E-value: 1.58e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 104 YKLQTTASWDFLGLkEGKNTKRNLAIE---SDTIIGFIDSGIWPESESFSDKGFGPPPKKWKGVCSGGKNFT---CNNKL 177
Cdd:cd04852   1 YQLHTTRSPDFLGL-PGAWGGSLLGAAnagEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNpfsCNNKL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 178 IGARDYtSEGT---------------RDLQGHGTHTASTAAGNAVADASFFGIGNGTARGGVPASRIAAYKVCSEKD-CT 241
Cdd:cd04852  80 IGARYF-SDGYdayggfnsdgeyrspRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGgCF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 242 AASLLSAFDDAIADGVDLISISLASeFPQKYYKDAIAIGAFHANVKGILTVNSAGNSGSFPSTTASVAPWILSVAASNtn 321
Cdd:cd04852 159 GSDILAAIDQAIADGVDVISYSIGG-GSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST-- 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 322 rgfftkvvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfs 401
Cdd:cd04852     --------------------------------------------------------------------------------

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 402 llppddfdslvsyinstrspqgtflkteaffnqtaptvasfssrgpnfiavdlLKPDISAPGVEILAAYSPLGSPSEees 481
Cdd:cd04852 236 -----------------------------------------------------LKPDIAAPGVDILAAWTPEGADPG--- 259

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 18424157 482 DKRRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTTAW 529
Cdd:cd04852 260 DARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 134-555 1.42e-40

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: 150.56  E-value: 1.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 134 IIGFIDSGIWPESESFSDKGFgpPPKKWKGvcsgGKNFTCNNKLIGARDY-----TSEGTRDLQGHGTHTASTAAGNAVA 208
Cdd:cd07474   5 KVAVIDTGIDYTHPDLGGPGF--PNDKVKG----GYDFVDDDYDPMDTRPypsplGDASAGDATGHGTHVAGIIAGNGVN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 209 dasfFGIGNGTArggvPASRIAAYKVCSEKD-CTAASLLSAFDDAIADGVDLISISLASEFPQKYYKDAIAIGAfhANVK 287
Cdd:cd07474  79 ----VGTIKGVA----PKADLYAYKVLGPGGsGTTDVIIAAIEQAVDDGMDVINLSLGSSVNGPDDPDAIAINN--AVKA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 288 GILTVNSAGNSGSFPSTTAS--VAPWILSVAASNTNrgfftkvvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvq 365
Cdd:cd07474 149 GVVVVAAAGNSGPAPYTIGSpaTAPSAITVGASTVA-------------------------------------------- 184

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 366 gkilvskfptsskvavgsiliddyqhyallsskpfsllppddfdslvsyinsTRSPqgtflkteaffnqtAPTVASFSSR 445
Cdd:cd07474 185 ----------------------------------------------------DVAE--------------ADTVGPSSSR 198

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 446 GP---NFIavdlLKPDISAPGVEILAAYSPLGSpseeesdkrrvKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQS 522
Cdd:cd07474 199 GPptsDSA----IKPDIVAPGVDIMSTAPGSGT-----------GYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKA 263

                       410       420       430
                ....*....|....*....|....*....|...
gi 18424157 523 AIMTTAWPMKpNRPGFASTEFAYGAGHVDQIAA 555
Cdd:cd07474 264 ALMNTAKPLY-DSDGVVYPVSRQGAGRVDALRA 295
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
 601-700 1.94e-32

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: 120.77  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   601 NLNYPSMSakIDGYNSSFTVTFKRTVTNLGTPNSTYKSKIVLNHGAKlVKVSPSVLSFKRVNEKQSFTVTFSGNLNLNLP 680
Cdd:pfam17766   1 DLNYPSIA--VSFENLNGSVTVTRTVTNVGDGPSTYTASVTAPPGVS-VTVSPSTLVFTKVGEKKSFTVTFTATKAPSGE 77

                          90       100
                  ....*....|....*....|.
gi 18424157   681 -TSANLIWSDGTHNVRSVIVV 700
Cdd:pfam17766  78 yVFGSLTWSDGKHTVRSPIVV 98
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 131-548 7.30e-31

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: 122.57  E-value: 7.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   131 SDTIIGFIDSGIWPESESFSDKGFGPPPKKWKGVCSGGKNFTCNNKLIgardytsegtRDLQGHGTHTASTAAGNAVADA 210
Cdd:pfam00082   2 KGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDFNNEWDDPRDDI----------DDKNGHGTHVAGIIAAGGNNSI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   211 SFFGIgngtarggVPASRIAAYKVCSEKDCTAASLLSAFDDAIADGVDLISISLASEFPQKY---YKDAIAiGAFHANVK 287
Cdd:pfam00082  72 GVSGV--------APGAKILGVRVFGDGGGTDAITAQAISWAIPQGADVINMSWGSDKTDGGpgsWSAAVD-QLGGAEAA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   288 GILTVNSAGNSGSFPSTTASVApwilsvaasntnrgfftkvvlgngktlvgrsvnsfdlkgkkyplvYGDNFNESLvqgk 367
Cdd:pfam00082 143 GSLFVWAAGNGSPGGNNGSSVG---------------------------------------------YPAQYKNVI---- 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   368 ilvskfptsskvAVGSILiddyqhyallsskpfsllppddfdslvsyinstrspqgtflkteaffNQTAPTVASFSSRGP 447
Cdd:pfam00082 174 ------------AVGAVD-----------------------------------------------EASEGNLASFSSYGP 194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157   448 NFIavDLLKPDISAPGVEIlAAYSPLGSPSEEESDKRRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTT 527
Cdd:pfam00082 195 TLD--GRLKPDIVAPGGNI-TGGNISSTLLTTTSDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNT 271

                         410       420
                  ....*....|....*....|.
gi 18424157   528 AWPMKPNRPgfastEFAYGAG 548
Cdd:pfam00082 272 ATDLGDAGL-----DRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 175-561 1.94e-30

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 125.21  E-value: 1.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 175 NKLIGARDYTS--EGTRDLQGHGTHTASTAAGNavadasffGIGNGTARGGVPASRIAAYKVCSEK-DCTAASLLSAFDD 251
Cdd:COG1404 129 GRVVGGYDFVDgdGDPSDDNGHGTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDDNgSGTTSDIAAAIDW 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 252 AIADGVDLISISLASEFPQKY--YKDAIAigafHANVKGILTVNSAGNSGSFPSTTAS--VAPWILSVAASNTNRgfftk 327
Cdd:COG1404 201 AADNGADVINLSLGGPADGYSdaLAAAVD----YAVDKGVLVVAAAGNSGSDDATVSYpaAYPNVIAVGAVDANG----- 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 328 vvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfsllppdd 407
Cdd:COG1404     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 408 fdslvsyinstrspqgtflkteaffnqtapTVASFSSRGPnfiavdllKPDISAPGVEILAAYsPLGSpseeesdkrrvk 487
Cdd:COG1404 272 ------------------------------QLASFSNYGP--------KVDVAAPGVDILSTY-PGGG------------ 300

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18424157 488 YSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTTAWPMKPNRPgfastefAYGAGHVDQIAAINPGLV 561
Cdd:COG1404 301 YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGP-------YYGYGLLADGAAGATSAG 367
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 133-557 8.52e-26

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: 109.28  E-value: 8.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 133 TIIGFIDSGIWPESESF-----SDKGFGPPPKKWKGVCSGGKNFTCNNKLIGARDYTSE-----GTRDLQGHGTHTASTA 202
Cdd:cd07475  13 MVVAVIDSGVDPTHDAFrldddSKAKYSEEFEAKKKKAGIGYGKYYNEKVPFAYNYADNnddilDEDDGSSHGMHVAGIV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 203 AGNAVADASFFGIgngtaRGGVPASRIAAYKVCSEKD---CTAASLLSAFDDAIADGVDLISISL--ASEFPQKYYKDAI 277
Cdd:cd07475  93 AGNGDEEDNGEGI-----KGVAPEAQLLAMKVFSNPEggsTYDDAYAKAIEDAVKLGADVINMSLgsTAGFVDLDDPEQQ 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 278 AIGAfhANVKGILTVNSAGNSGSFPSTTASVapwilsvaasntnrgfftkvvlgngktlvgrsvnsfdlkgkkyplvygd 357
Cdd:cd07475 168 AIKR--AREAGVVVVVAAGNDGNSGSGTSKP------------------------------------------------- 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 358 nfneslvqgkilvskfptsskvavgsiLIDDYQHYALLSSkpfsllPPDDFDSLvsyinSTRSPQGTFLkteaffNQTAP 437
Cdd:cd07475 197 ---------------------------LATNNPDTGTVGS------PATADDVL-----TVASANKKVP------NPNGG 232

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 438 TVASFSSRGPnfiAVDL-LKPDISAPGVEILAAYspLGSpseeesdkrrvKYSVMSGTSMSCPHVAGVAA----YIRTFH 512
Cdd:cd07475 233 QMSGFSSWGP---TPDLdLKPDITAPGGNIYSTV--NDN-----------TYGYMSGTSMASPHVAGASAlvkqRLKEKY 296

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18424157 513 PKWSP----SVIQSAIMTTAWPMKPnrpgfaSTEFAY-------GAGHVDQIAAIN 557
Cdd:cd07475 297 PKLSGeelvDLVKNLLMNTATPPLD------SEDTKTyysprrqGAGLIDVAKAIA 346
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 133-527 1.26e-24

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: 103.05  E-value: 1.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 133 TIIGFIDSGIWPESESFSDkgfgpppkkWKGVCSGGKNFTCNNKligardyTSEGTRDLQGHGTHTASTAAGNAvadasf 212
Cdd:cd00306   1 VTVAVIDTGVDPDHPDLDG---------LFGGGDGGNDDDDNEN-------GPTDPDDGNGHGTHVAGIIAASA------ 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 213 fgiGNGTARGGVPASRIAAYKVCSEKD-CTAASLLSAFDDAIAD-GVDLISISLASEFPQKYYKDAIAIGAFHANvKGIL 290
Cdd:cd00306  59 ---NNGGGVGVAPGAKLIPVKVLDGDGsGSSSDIAAAIDYAAADqGADVINLSLGGPGSPPSSALSEAIDYALAK-LGVL 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 291 TVNSAGNSGSFPSTTAS---VAPWILSVAASNTNRGFFtkvvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqgk 367
Cdd:cd00306 135 VVAAAGNDGPDGGTNIGypaASPNVIAVGAVDRDGTPA------------------------------------------ 172

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 368 ilvskfptsskvavgsiliddyqhyallsskpfsllppddfdslvsyinstrspqgtflkteaffnqtaptvASFSSRGP 447
Cdd:cd00306 173 ------------------------------------------------------------------------SPSSNGGA 180

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 448 nfiavdllKPDISAPGVEILAAYSPLGSpseeesdkrrvKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTT 527
Cdd:cd00306 181 --------GVDIAAPGGDILSSPTTGGG-----------GYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 135-528 1.44e-23

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: 100.74  E-value: 1.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 135 IGFIDSGIWPESESFSDKGfgpppkkwkgvcsggknftCNNKLIGARDYTSEGTRDLQGHGTHTASTAAGNAVAdasffg 214
Cdd:cd07487   6 VAVLDTGIDAPHPDFDGRI-------------------IRFADFVNTVNGRTTPYDDNGHGTHVAGIIAGSGRA------ 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 215 iGNGTARGGVPASRIAAYKVCSEK-DCTAASLLSAFDDAIAD----GVDLISISLASEFPQKYYKDAIaIGAFHANVK-G 288
Cdd:cd07487  61 -SNGKYKGVAPGANLVGVKVLDDSgSGSESDIIAGIDWVVENnekyNIRVVNLSLGAPPDPSYGEDPL-CQAVERLWDaG 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 289 ILTVNSAGNSGSFPSTTAS--VAPWILSVAASNTNRgfftkvvlgngktlvgrsvnsfdlkgkkyplvygdnfneslvqg 366
Cdd:cd07487 139 IVVVVAAGNSGPGPGTITSpgNSPKVITVGAVDDNG-------------------------------------------- 174

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 367 kilvskfptsskvavgsiliddyqhyallsskpfsllPPDDfdslvsyinstrspqgtflkteaffnqtapTVASFSSRG 446
Cdd:cd07487 175 -------------------------------------PHDD------------------------------GISYFSSRG 187

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 447 PNFIAVdlLKPDISAPGVEILAAYSPLGSPSEEESDKrrvkYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMT 526
Cdd:cd07487 188 PTGDGR--IKPDVVAPGENIVSCRSPGGNPGAGVGSG----YFEMSGTSMATPHVSGAIALLLQANPILTPDEVKCILRD 261


                ..
gi 18424157 527 TA 528
Cdd:cd07487 262 TA 263
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 135-557 1.57e-23

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: 101.91  E-value: 1.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 135 IGFIDSGIWPESESFSDkGFGPPPKkwkgvCSGGKNFtcnnklIGArDYTSEGTR-------DLQGHGTHTASTAAGNav 207
Cdd:cd07489  17 VAVVDTGIDYTHPALGG-CFGPGCK-----VAGGYDF------VGD-DYDGTNPPvpdddpmDCQGHGTHVAGIIAAN-- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 208 adasffgiGNGTARGGV-PASRIAAYKV--CSeKDCTAASLLSAFDDAIADGVDLISISLASefPQKYYKDAIAIGAFHA 284
Cdd:cd07489  82 --------PNAYGFTGVaPEATLGAYRVfgCS-GSTTEDTIIAAFLRAYEDGADVITASLGG--PSGWSEDPWAVVASRI 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 285 NVKGILTVNSAGNSGSFpsttasvAPWILSVAASntnrgfftkvvlgngktlvGRSVnsfdlkgkkyplvygdnfneslv 364
Cdd:cd07489 151 VDAGVVVTIAAGNDGER-------GPFYASSPAS-------------------GRGV----------------------- 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 365 qgkilvskfptsskVAVGSIliddyqhyallsskpfsllppddfDSlvsyinstrspqgtflkteaffnqtaptvaSFSS 444
Cdd:cd07489 182 --------------IAVASV------------------------DS------------------------------YFSS 193

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 445 RGPNFiavDL-LKPDISAPGVEILAAYsPLGSPSeeesdkrrvkYSVMSGTSMSCPHVAGVAA-YIRTFHPKWSPSVIQS 522
Cdd:cd07489 194 WGPTN---ELyLKPDVAAPGGNILSTY-PLAGGG----------YAVLSGTSMATPYVAGAAAlLIQARHGKLSPAELRD 259

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 18424157 523 AIMTTAWPMK-----PNRPGFASTeFAYGAGHVDQIAAIN 557
Cdd:cd07489 260 LLASTAKPLPwsdgtSALPDLAPV-AQQGAGLVNAYKALY 298
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 135-527 1.72e-23

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: 99.53  E-value: 1.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 135 IGFIDSGIWPESESFsdkgfgpppkKWKGVcsGGKNFTcnnkligarDYTSEGTRDLQGHGTHTASTAAGnavadasffg 214
Cdd:cd07477   4 VAVIDTGIDSSHPDL----------KLNIV--GGANFT---------GDDNNDYQDGNGHGTHVAGIIAA---------- 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 215 IGNGTARGGV-PASRIAAYKVCSEKDC-TAASLLSAFDDAIADGVDLISISLASEFPQKYYKDAIAIgafhANVKGILTV 292
Cdd:cd07477  53 LDNGVGVVGVaPEADLYAVKVLNDDGSgTYSDIIAGIEWAIENGMDIINMSLGGPSDSPALREAIKK----AYAAGILVV 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 293 NSAGNSGSFPSTTASVApwilsvaasntnrgfftkvvlgngktlvgrsvnsfdlkgkKYPLVygdnfneslvqgkilvsk 372
Cdd:cd07477 129 AAAGNSGNGDSSYDYPA----------------------------------------KYPSV------------------ 150

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 373 fptsskVAVGSIliddyqhyallsskpfsllppdDFDSlvsyinstrspqgtflkteaffnqtapTVASFSSRGPNfiav 452
Cdd:cd07477 151 ------IAVGAV----------------------DSNN---------------------------NRASFSSTGPE---- 171

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18424157 453 dllkPDISAPGVEILAAYsPLGspseeesdkrrvKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTT 527
Cdd:cd07477 172 ----VELAAPGVDILSTY-PNN------------DYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 180-529 2.36e-23

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: 99.93  E-value: 2.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 180 ARDYTSEGTRDLQGHGTHTASTAAGNAVadasffgigNGTARGGVPASRIAAYKVCSEKDCTAASLLSAFDDAIADGVDL 259
Cdd:cd07490  31 NRRISATEVFDAGGHGTHVSGTIGGGGA---------KGVYIGVAPEADLLHGKVLDDGGGSLSQIIAGMEWAVEKDADV 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 260 ISISLASEfpqkYYKDAIAIGAFHA--NVKGILTVNSAGNSGSFPSTTASVAPWILSVAAsntnrgfftkvvlgngktlv 337
Cdd:cd07490 102 VSMSLGGT----YYSEDPLEEAVEAlsNQTGALFVVSAGNEGHGTSGSPGSAYAALSVGA-------------------- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 338 grsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsilIDDYQHYALLSSkpfsllppddfdslvsyins 417
Cdd:cd07490 158 ------------------------------------------------VDRDDEDAWFSS-------------------- 169

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 418 trspqgtflkteaFFNQTAPTVASFSSRGPNFiavdlLKPDISAPGVEILAAYSpLGSPSEEesdkrrvkYSVMSGTSMS 497
Cdd:cd07490 170 -------------FGSSGASLVSAPDSPPDEY-----TKPDVAAPGVDVYSARQ-GANGDGQ--------YTRLSGTSMA 222

                       330       340       350
                ....*....|....*....|....*....|..
gi 18424157 498 CPHVAGVAAYIRTFHPKWSPSVIQSAIMTTAW 529
Cdd:cd07490 223 APHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 29-107 5.77e-18

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: 78.87  E-value: 5.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157    29 VYVVYMGSL--PSLLEYTPLSHHMSILQEVTGD-SSVEGRLVRSYKRSFNGFAARLTESERIRVAEMEGVVSVFPNINYK 105
Cdd:pfam05922   1 TYIVYLKEGaaAADSFSSHTEWHSSLLRSVLSEeSSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80


                  ..
gi 18424157   106 LQ 107
Cdd:pfam05922  81 LH 82
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 190-528 7.29e-18

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: 83.78  E-value: 7.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 190 DLQGHGTHTASTAAgnAVADasffgigNGTARGGV-PASRIAAYKVC-SEKDCTAASLLSAFDDAIADGVDLISISLASE 267
Cdd:cd07473  61 DDNGHGTHVAGIIG--AVGN-------NGIGIAGVaWNVKIMPLKFLgADGSGTTSDAIKAIDYAVDMGAKIINNSWGGG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 268 FPQKYYKDAIAigafHANVKGILTVNSAGNSGS----FPSTTASVA-PWILSVAASNTNrgfftkvvlgngktlvgrsvn 342
Cdd:cd07473 132 GPSQALRDAIA----RAIDAGILFVAAAGNDGTnndkTPTYPASYDlDNIISVAATDSN--------------------- 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 343 sfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfsllppddfdslvsyinstrspq 422
Cdd:cd07473     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 423 gtflkteaffnqtaPTVASFSSRGPNFIavdllkpDISAPGVEILAAYSPLGspseeesdkrrvkYSVMSGTSMSCPHVA 502
Cdd:cd07473 187 --------------DALASFSNYGKKTV-------DLAAPGVDILSTSPGGG-------------YGYMSGTSMATPHVA 232

                       330       340
                ....*....|....*....|....*.
gi 18424157 503 GVAAYIRTFHPKWSPSVIQSAIMTTA 528
Cdd:cd07473 233 GAAALLLSLNPNLTAAQIKDAILSSA 258
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 132-506 2.90e-17

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: 84.98  E-value: 2.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 132 DTIIGFIDSGIWPESESFSDKGF-------------GPPPKKWKGVCSGGKNFTCNNKLIGARDYTSEGTRDLQGHGTHT 198
Cdd:cd07478   5 GVLVGIIDTGIDYLHPEFRNEDGttrilyiwdqtipGGPPPGGYYGGGEYTEEIINAALASDNPYDIVPSRDENGHGTHV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 199 ASTAAGNAVADASFFGIgngtarggVPASRIA--------AYKVCSEKDCTA---ASLLSAFD--DAIADGVDL---ISI 262
Cdd:cd07478  85 AGIAAGNGDNNPDFKGV--------APEAELIvvklkqakKYLREFYEDVPFyqeTDIMLAIKylYDKALELNKplvINI 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 263 SLASEF-------PQKYYKDAIAigafhaNVKGILTVNSAGN--------SGSFPSTTASV------------------- 308
Cdd:cd07478 157 SLGTNFgshdgtsLLERYIDAIS------RLRGIAVVVGAGNegntqhhhSGGIVPNGETKtvelnvgegekgfnleiwg 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 309 -APWILSVAASNTNrGFFTKVV-LGNGKTLVGRsvnsFDLKGKKYpLVYGDNFNESLVQGKILVSKFPTSS---KVAVGS 383
Cdd:cd07478 231 dFPDRFSVSIISPS-GESSGRInPGIGGSESYK----FVFEGTTV-YVYYYLPEPYTGDQLIFIRFKNIKPgiwKIRLTG 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 384 ILIDDYQHYALLSSKPF-----SLLPPDDFDSLVSYINSTRspqgtfLKTEAFFNQTAPTVASFSSRGPNfiAVDLLKPD 458
Cdd:cd07478 305 VSITDGRFDAWLPSRGLlsentRFLEPDPYTTLTIPGTARS------VITVGAYNQNNNSIAIFSGRGPT--RDGRIKPD 376

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 18424157 459 ISAPGVEILAAYSplgspseeesdkrRVKYSVMSGTSMSCPHVAGVAA 506
Cdd:cd07478 377 IAAPGVNILTASP-------------GGGYTTRSGTSVAAAIVAGACA 411
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 184-511 9.10e-17

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: 81.22  E-value: 9.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 184 TSEGTRDLQGHGTHTASTAAGNAVADASffgigNGTARGGVPASRIAAYKVCSEKdcTAASLLSAFDDAIADGVDLISI- 262
Cdd:cd04842  46 LSDTKDDVDGHGTHVAGIIAGKGNDSSS-----ISLYKGVAPKAKLYFQDIGDTS--GNLSSPPDLNKLFSPMYDAGARi 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 263 ---SLASEFPQKYYKDAIAIGAFHANVKGILTVNSAGNSGSFPS---TTASVAPWILSVAASNTNRgfftkvvlgngktl 336
Cdd:cd04842 119 ssnSWGSPVNNGYTLLARAYDQFAYNNPDILFVFSAGNDGNDGSntiGSPATAKNVLTVGASNNPS-------------- 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 337 vgrSVNSFDLKGKKYplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfsllppddfdslvsyin 416
Cdd:cd04842 185 ---VSNGEGGLGQSD----------------------------------------------------------------- 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 417 strspqgtflkteaffnqTAPTVASFSSRGPNFIAvdLLKPDISAPGVEILAAYSPLGSPSEEESDKrrvkYSVMSGTSM 496
Cdd:cd04842 197 ------------------NSDTVASFSSRGPTYDG--RIKPDLVAPGTGILSARSGGGGIGDTSDSA----YTSKSGTSM 252

                       330
                ....*....|....*
gi 18424157 497 SCPHVAGVAAYIRTF 511
Cdd:cd04842 253 ATPLVAGAAALLRQY 267
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 174-548 8.01e-16

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: 78.57  E-value: 8.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 174 NNKLIGARDYTSEGTR-DLQGHGTHTASTAAGNAVAdasffGIGNGTARGgvpASRIAAYKVCSEKDCTAASLLSAFDDA 252
Cdd:cd07480  27 AGRDITTKSFVGGEDVqDGHGHGTHCAGTIFGRDVP-----GPRYGVARG---AEIALIGKVLGDGGGGDGGILAGIQWA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 253 IADGVDLISISLASEFPqkyykdaiaigafhANVKGILTVNSAgnsgsfpsttASVApwiLSVAASNTNrgFFTKVVlgn 332
Cdd:cd07480  99 VANGADVISMSLGADFP--------------GLVDQGWPPGLA----------FSRA---LEAYRQRAR--LFDALM--- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 333 gktlvgrSVNSFDLKGKKYPLVYGDNFNESLVQGKI--LVSKFPTSSKVAVGSIliddyqhyallsskpfsllppddfds 410
Cdd:cd07480 147 -------TLVAAQAALARGTLIVAAAGNESQRPAGIppVGNPAACPSAMGVAAV-------------------------- 193

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 411 lvsyinstrspqGTFLKTEAFFNqtaptVASFSSRGPnfiavdllkpDISAPGVEILAAYSPlgspseeesdkrrVKYSV 490
Cdd:cd07480 194 ------------GALGRTGNFSA-----VANFSNGEV----------DIAAPGVDIVSAAPG-------------GGYRS 233

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18424157 491 MSGTSMSCPHVAGVAAYIRTFHPK---WSPSVIQSAIMTTAWPmKPNRPGFASTEFAYGAG 548
Cdd:cd07480 234 MSGTSMATPHVAGVAALWAEALPKaggRALAALLQARLTAART-TQFAPGLDLPDRGVGLG 293
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 189-528 5.14e-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: 5.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 189 RDLQGHGTHTASTAAGNAvadasffgiGNGTARGGVPASRIAAYKVCSEKDCTAASLLSAFDDAIA---DGVDLISISLA 265
Cdd:cd07481  49 YDDNGHGTHTMGTMVGND---------GDGQQIGVAPGARWIACRALDRNGGNDADYLRCAQWMLAptdSAGNPADPDLA 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 266 SE-------FPQK---YYKDAIAigAFHAnvKGILTVNSAGNSGSFPSTTASvapwilSVAAsntnrgfftkvvlgngkt 335
Cdd:cd07481 120 PDvinnswgGPSGdneWLQPAVA--AWRA--AGIFPVFAAGNDGPRCSTLNA------PPAN------------------ 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 336 lvgrsvnsfdlkgkkYPLVYgdnfneslvqgkilvskfptsskvAVGSILIDDYqhyallsskpfsllppddfdslvsyi 415
Cdd:cd07481 172 ---------------YPESF------------------------AVGATDRNDV-------------------------- 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 416 nstrspqgtflkteaffnqtaptVASFSSRGPnfIAVDLLKPDISAPGVEILAAySPLGSpseeesdkrrvkYSVMSGTS 495
Cdd:cd07481 187 -----------------------LADFSSRGP--STYGRIKPDISAPGVNIRSA-VPGGG------------YGSSSGTS 228

                       330       340       350
                ....*....|....*....|....*....|....*
gi 18424157 496 MSCPHVAGVAAYIRTFHPKWSPSV--IQSAIMTTA 528
Cdd:cd07481 229 MAAPHVAGVAALLWSANPSLIGDVdaTEAILTETA 263
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 104-528 1.99e-12

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: 68.06  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 104 YKLQTTASWDFLGLkegkntkrnlaieSDTIIGFIDSGIWPESesfsdkgfgppPKKWKGVCSGGKNFTCNNkligardy 183
Cdd:cd07484  14 DQIGAPKAWDITGG-------------SGVTVAVVDTGVDPTH-----------PDLLKVKFVLGYDFVDND-------- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 184 tsEGTRDLQGHGTHTASTAAgnAVADasffgigNGTARGGV-PASRIAAYKVCSEkdcTAASLLSAFDDAI---AD-GVD 258
Cdd:cd07484  62 --SDAMDDNGHGTHVAGIIA--AATN-------NGTGVAGVaPKAKIMPVKVLDA---NGSGSLADIANGIryaADkGAK 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 259 LISISLASEFPQKYYKDAIAigafHANVKGILTVNSAGNSGSFPSTTASVAPWILSVAASNtnrgfftkvvlgngktlvg 338
Cdd:cd07484 128 VINLSLGGGLGSTALQEAIN----YAWNKGVVVVAAAGNEGVSSVSYPAAYPGAIAVAATD------------------- 184

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 339 rsvnsfdlkgkkyplvygdnfneslvqgkilvskfptsskvavgsiliddyqhyallsskpfsllpPDDfdslvsyinst 418
Cdd:cd07484 185 ------------------------------------------------------------------QDD----------- 187

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 419 rspqgtflkteaffnqtapTVASFSSRGPNFiavdllkpDISAPGVEILAAYSPLGspseeesdkrrvkYSVMSGTSMSC 498
Cdd:cd07484 188 -------------------KRASFSNYGKWV--------DVSAPGGGILSTTPDGD-------------YAYMSGTSMAT 227

                       410       420       430
                ....*....|....*....|....*....|
gi 18424157 499 PHVAGVAAYIRTFHPkWSPSVIQSAIMTTA 528
Cdd:cd07484 228 PHVAGVAALLYSQGP-LSASEVRDALKKTA 256
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 438-528 2.15e-12

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: 67.54  E-value: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 438 TVASFSSRGPnfiAVDLLkpdisAPGVEILAAYSplGSPSEeesdkrrvkYSVMSGTSMSCPHVAGVAAYIRTFHPKWSP 517
Cdd:cd04077 182 ARASFSNYGS---CVDIF-----APGVDILSAWI--GSDTA---------TATLSGTSMAAPHVAGLAAYLLSLGPDLSP 242

                        90
                ....*....|.
gi 18424157 518 SVIQSAIMTTA 528
Cdd:cd04077 243 AEVKARLLNLA 253
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 328-424 1.06e-08

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: 53.96  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 328 VVLGNGKTLVGRSVNSFDLkgKKYPLVYGDNF--------------NESLVQGKILV----SKFPTSSKV-------AVG 382
Cdd:cd02120   2 VTLGNGKTIVGQSLYPGNL--KTYPLVYKSANsgdvdaslclpgslDPSKVKGKIVLcdrgGNTSRVAKGdavkaagGAG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18424157 383 SILIDD--YQHYALLSSK--PFSLLPPDDFDSLVSYINSTRSPQGT 424
Cdd:cd02120  80 MILANDptDGLDVVADAHvlPAVHVDYEDGTAILSYINSTSNPTAT 125
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 135-506 1.34e-08

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: 56.56  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 135 IGFIDSGIWPESESFSDKGFGpppkkwkgvcsggknftcNNKLIGARDYTSEGTRDLQGHGTHTASTAAGNAvadasffg 214
Cdd:cd04848   7 VGVIDSGIDLSHPEFAGRVSE------------------ASYYVAVNDAGYASNGDGDSHGTHVAGVIAAAR-------- 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 215 igNGTARGGV-PASRIAAYKVCSEKDCTAAS--LLSAFDDAIADGVDLISISLASEFPQKYYKDAIAIGAFHAN------ 285
Cdd:cd04848  61 --DGGGMHGVaPDATLYSARASASAGSTFSDadIAAAYDFLAASGVRIINNSWGGNPAIDTVSTTYKGSAATQGntllaa 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 286 -----VKGILTVNSAGNSG-SFPSTTASVAPWILSvaasntnrgfftkvvlgngktlvgrsvnsfDLKGkkyplvygdnf 359
Cdd:cd04848 139 laraaNAGGLFVFAAGNDGqANPSLAAAALPYLEP------------------------------ELEG----------- 177

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 360 neslvqgkilvskfptsSKVAVGSIliddyqhyallsskpfsllppDDFDSLVSYINSTRspqgtFLKTEAFFnqtaptv 439
Cdd:cd04848 178 -----------------GWIAVVAV---------------------DPNGTIASYSYSNR-----CGVAANWC------- 207

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18424157 440 asfssrgpnfiavdllkpdISAPGVEILAAYSPLGSpseeesdkrrvKYSVMSGTSMSCPHVAGVAA 506
Cdd:cd04848 208 -------------------LAAPGENIYSTDPDGGN-----------GYGRVSGTSFAAPHVSGAAA 244
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 438-528 1.94e-08

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: 55.77  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 438 TVASFSSRGPNfiAVDLLKPDISAPGVEIlAAYSPLGSpseeesdkrrvkYSVMSGTSMSCPHVAGVAAYIRTFHPKWSP 517
Cdd:cd07493 185 NKASFSSIGPT--ADGRLKPDVMALGTGI-YVINGDGN------------ITYANGTSFSCPLIAGLIACLWQAHPNWTN 249

                        90
                ....*....|.
gi 18424157 518 SVIQSAIMTTA 528
Cdd:cd07493 250 LQIKEAILKSA 260
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 190-299 2.36e-08

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: 56.22  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 190 DLQGHGTHTASTAAGNavadasffgignGTARGGVPASRIAAYKVC-SEKDCTAASLLSAFDDAIADGVDLISISLAS-- 266
Cdd:cd07482  51 DKLGHGTAVAGQIAAN------------GNIKGVAPGIGIVSYRVFgSCGSAESSWIIKAIIDAADDGVDVINLSLGGyl 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18424157 267 -------EFPQKY--YKDAIAigafHANVKGILTVNSAGNSG 299
Cdd:cd07482 119 iiggeyeDDDVEYnaYKKAIN----YAKSKGSIVVAAAGNDG 156
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 438-508 3.50e-08

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: 55.18  E-value: 3.50e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18424157 438 TVASFSSRGPNFiavdllkpDISAPGVEILAAYSPLGSPSEEESdkrrvkYSVMSGTSMSCPHVAGVAAYI 508
Cdd:cd07485 197 NKASFSNYGRWV--------DIAAPGVGTILSTVPKLDGDGGGN------YEYLSGTSMAAPHVSGVAALV 253
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 439-528 5.30e-07

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: 51.98  E-value: 5.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 439 VASFSSRGPNFIavdllkpDISAPGVEILAAysplgSPSEEesdkrrvkYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPS 518
Cdd:cd07483 221 VANFSNYGKKNV-------DVFAPGERIYST-----TPDNE--------YETDSGTSMAAPVVSGVAALIWSYYPNLTAK 280

                        90
                ....*....|
gi 18424157 519 VIQSAIMTTA 528
Cdd:cd07483 281 EVKQIILESG 290
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 432-556 5.97e-07

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: 51.52  E-value: 5.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 432 FNQTAPTVASFSSRGPNFIA----VDLLKPDISAP-GVEILAAYSPLGSPseeesdkrrvkysVMSGTSMSCPHVAGVAA 506
Cdd:cd05562 162 FGSDPAPGGTPSSFDPVGIRlptpEVRQKPDVTAPdGVNGTVDGDGDGPP-------------NFFGTSAAAPHAAGVAA 228

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18424157 507 YIRTFHPKWSPSVIQSAIMTTAWPMKPnrPGFastEFAYGAGHVDQIAAI 556
Cdd:cd05562 229 LVLSANPGLTPADIRDALRSTALDMGE--PGY---DNASGSGLVDADRAV 273
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 440-527 6.83e-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: 51.52  E-value: 6.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 440 ASFSSRGPnfiAVDLLKP--DISAPGVEILAAYSPLGSPSEEESdkrrvKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSP 517
Cdd:cd07496 204 ASYSNYGP---AVDVSAPggDCASDVNGDGYPDSNTGTTSPGGS-----TYGFLQGTSMAAPHVAGVAALMKSVNPSLTP 275

                        90
                ....*....|
gi 18424157 518 SVIQSAIMTT 527
Cdd:cd07496 276 AQIESLLQST 285
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 443-506 6.91e-07

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: 52.86  E-value: 6.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18424157   443 SSRGPNFIavDLLKPDISAPGVEILAAYsplgsPSEeesdkrrvKYSVMSGTSMSCPHVAGVAA 506
Cdd:NF040809  994 SSRGPTIR--NIQKPDIVAPGVNIIAPY-----PGN--------TYATITGTSAAAAHVSGVAA 1042
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 440-527 6.71e-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: 48.11  E-value: 6.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 440 ASFSSRGPNFiavdllkpDISAPGVEIlaaySPLGSPSEEESDKRRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSV 519
Cdd:cd07498 167 ASYSNYGNYV--------DLVAPGVGI----WTTGTGRGSAGDYPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAE 234


                ....*...
gi 18424157 520 IQSAIMTT 527
Cdd:cd07498 235 VEDILTST 242
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 133-321 2.20e-05

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: 46.57  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 133 TIIGFIDSGIWPESESFSDKGFGPPpkkwkgvcsgGKNFTCNNKLIGARDytsegtrdlqGHGTHTASTAAGNAvadasf 212
Cdd:cd07498   1 VVVAIIDTGVDLNHPDLSGKPKLVP----------GWNFVSNNDPTSDID----------GHGTACAGVAAAVG------ 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 213 fGIGNGTArGGVPASRIAAYKVcsekdctAASLLSAFDDAIAD--------GVDLISISLASEFPQKYYKDAIAIGAFHA 284
Cdd:cd07498  55 -NNGLGVA-GVAPGAKLMPVRI-------ADSLGYAYWSDIAQaitwaadnGADVISNSWGGSDSTESISSAIDNAATYG 125

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 18424157 285 -NVKGILTVNSAGNSGSFPSTTASVAPWILSVAASNTN 321
Cdd:cd07498 126 rNGKGGVVLFAAGNSGRSVSSGYAANPSVIAVAATDSN 163
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 432-506 7.64e-05

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: 46.31  E-value: 7.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18424157   432 FNQTAPTVASFSSRGPnfIAVDLLKPDISAPGVEILAaYSPLGSPSeeesdkrrvkysVMSGTSMSCPHVAGVAA 506
Cdd:NF040809  411 FNSRTDVVSVFSGEGD--IENGIYKPDLLAPGENIVS-YLPGGTTG------------ALTGTSMATPHVTGVCS 470
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 439-528 9.69e-05

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: 45.15  E-value: 9.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 439 VASFSSRGPNFIAVdlLKPDISAPGVEILAAYSPLGSPSeeeSDKRRVKYSVMSGTSMSCPHVAGVAAYI------RTFH 512
Cdd:cd07497 221 VVSWSSRGPSIAGD--PKPDLAAIGAFAWAPGRVLDSGG---ALDGNEAFDLFGGTSMATPMTAGSAALVisalkeKEGV 295

                        90
                ....*....|....*.
gi 18424157 513 PKWSPSVIQSAIMTTA 528
Cdd:cd07497 296 GEYDPFLVRTILMSTA 311
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
 458-528 1.42e-04

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: 43.82  E-value: 1.42e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18424157 458 DISAPGVEILAAYSplgspseeesdkrRVKYSVMSGTSMSCPHVAGVAAYIRTFHPKWSPSVIQSAIMTTA 528
Cdd:cd05561 168 DFAAPGVDVWVAAP-------------GGGYRYVSGTSFAAPFVTAALALLLQASPLAPDDARARLAATAK 225
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
 194-307 9.89e-04

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: 41.51  E-value: 9.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 194 HGTHTASTAAGNAVAdasffgiGNGTARGGVPASRIAAYKVCSEKDCTAASLLSAFDDAIADGVDLISISLASEfPQKYY 273
Cdd:cd05561  38 HGTAVASLLAGAGAQ-------RPGLLPGADLYGADVFGRAGGGEGASALALARALDWLAEQGVRVVNISLAGP-PNALL 109

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18424157 274 KDAIAIgafhANVKGILTVNSAGNSG--SFPSTTAS 307
Cdd:cd05561 110 AAAVAA----AAARGMVLVAAAGNDGpaAPPLYPAA 141
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 418-516 3.64e-03

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 40.72  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157  418 TRSPQGTFLKTEAFFNQTAPTVASFSSRgpNFIAVDLLKPDISA-----PGVEILAAYSPLGSPSEE-ESDKRRVKYSVM 491
Cdd:PTZ00262 476 TKESKPDIPKCDLDVNKVYPPILSKKLR--NVITVSNLIKDKNNqyslsPNSFYSAKYCQLAAPGTNiYSTFPKNSYRKL 553

                         90       100
                 ....*....|....*....|....*
gi 18424157  492 SGTSMSCPHVAGVAAYIRTFHPKWS 516
Cdd:PTZ00262 554 NGTSMAAPHVAAIASLILSINPSLS 578
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 443-531 7.10e-03

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: 39.57  E-value: 7.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424157 443 SSRGPnfiAVD-LLKPDISAPGVEIlaAYSPLGSPSeeesdkrrvKYSVMSGTSMSCPHVAG-VAAYIRTFHP---KWSP 517
Cdd:cd04857 333 SSRGP---TADgALGVSISAPGGAI--ASVPNWTLQ---------GSQLMNGTSMSSPNACGgIALLLSGLKAegiPYTP 398

                        90
                ....*....|....
gi 18424157 518 SVIQSAIMTTAWPM 531
Cdd:cd04857 399 YSVRRALENTAKKL 412
 
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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