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Conserved domains on  [gi|18425181|ref|NP_569048|]
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Subtilase 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 ...
103-576 1.26e-147

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: 433.56  E-value: 1.26e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 103 YELHTTRTPLFLGLDEHTADLFPEAGSY-SDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLI 181
Cdd:cd04852   1 YQLHTTRSPDFLGLPGAWGGSLLGAANAgEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPFSCNNKLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 182 GARFFARGYESTMGpIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCW-LGGCFS 260
Cdd:cd04852  81 GARYFSDGYDAYGG-FNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWpDGGCFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 261 SDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTldrd 340
Cdd:cd04852 160 SDILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST---- 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 341 fpalailgngknftgvslfkgealpdkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaa 420
Cdd:cd04852     --------------------------------------------------------------------------------
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 421 ggvgmilantaangeelvadahllpattvgekagdiirhyvttdpnptasisilgtvvgvkpspvvaafssrgpnsitpn 500
Cdd:cd04852     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18425181 501 iLKPDLIAPGVNILAAWTgaaGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAY 576
Cdd:cd04852 236 -LKPDIAAPGVDILAAWT---PEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
346-471 6.62e-40

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: 142.94  E-value: 6.62e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 346 ILGNGKNFTGVSLFKGealPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGIN-ARVQKGDVVKAAGGVG 424
Cdd:cd02120   3 TLGNGKTIVGQSLYPG---NLKTYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNtSRVAKGDAVKAAGGAG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18425181 425 MILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASI 471
Cdd:cd02120  80 MILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
657-754 3.79e-36

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


:

Pssm-ID: 465493  Cd Length: 98  Bit Score: 131.17  E-value: 3.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   657 DLNYPSFAVNV-DGVGAYKYTRTVTSVG-GAGTYSVKVTSeTTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSkPSGSN 734
Cdd:pfam17766   1 DLNYPSIAVSFeNLNGSVTVTRTVTNVGdGPSTYTASVTA-PPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKA-PSGEY 78
                          90       100
                  ....*....|....*....|
gi 18425181   735 SFGSIEWSDGKHVVGSPVAI 754
Cdd:pfam17766  79 VFGSLTWSDGKHTVRSPIVV 98
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
31-106 1.06e-21

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: 89.66  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181    31 TYIVHMAK-SQMPSSFDLHSNWYDSSLRSI-----SDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYE 104
Cdd:pfam05922   1 TYIVYLKEgAAAADSFSSHTEWHSSLLRSVlseesSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80

                  ..
gi 18425181   105 LH 106
Cdd:pfam05922  81 LH 82
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
103-576 1.26e-147

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: 433.56  E-value: 1.26e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 103 YELHTTRTPLFLGLDEHTADLFPEAGSY-SDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLI 181
Cdd:cd04852   1 YQLHTTRSPDFLGLPGAWGGSLLGAANAgEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPFSCNNKLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 182 GARFFARGYESTMGpIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCW-LGGCFS 260
Cdd:cd04852  81 GARYFSDGYDAYGG-FNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWpDGGCFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 261 SDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTldrd 340
Cdd:cd04852 160 SDILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST---- 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 341 fpalailgngknftgvslfkgealpdkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaa 420
Cdd:cd04852     --------------------------------------------------------------------------------
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 421 ggvgmilantaangeelvadahllpattvgekagdiirhyvttdpnptasisilgtvvgvkpspvvaafssrgpnsitpn 500
Cdd:cd04852     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18425181 501 iLKPDLIAPGVNILAAWTgaaGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAY 576
Cdd:cd04852 236 -LKPDIAAPGVDILAAWT---PEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
346-471 6.62e-40

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: 142.94  E-value: 6.62e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 346 ILGNGKNFTGVSLFKGealPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGIN-ARVQKGDVVKAAGGVG 424
Cdd:cd02120   3 TLGNGKTIVGQSLYPG---NLKTYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNtSRVAKGDAVKAAGGAG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18425181 425 MILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASI 471
Cdd:cd02120  80 MILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
657-754 3.79e-36

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


Pssm-ID: 465493  Cd Length: 98  Bit Score: 131.17  E-value: 3.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   657 DLNYPSFAVNV-DGVGAYKYTRTVTSVG-GAGTYSVKVTSeTTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSkPSGSN 734
Cdd:pfam17766   1 DLNYPSIAVSFeNLNGSVTVTRTVTNVGdGPSTYTASVTA-PPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKA-PSGEY 78
                          90       100
                  ....*....|....*....|
gi 18425181   735 SFGSIEWSDGKHVVGSPVAI 754
Cdd:pfam17766  79 VFGSLTWSDGKHTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
203-707 1.92e-28

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 119.43  E-value: 1.92e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 203 SRSPRDDDGHGTHTSSTAAGSvvegasllGYASGTARGMAPRARVAVYKVCW-LGGCFSSDILAAIDKAIADNVNVLSMS 281
Cdd:COG1404 141 DGDPSDDNGHGTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDdNGSGTTSDIAAAIDWAADNGADVINLS 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 282 LGG---GMSDYYRDGVAigafAAMERGILVSCSAGNAGPSSSSLSN--VAPWITTVGAgtldrdfpalailgngknftgv 356
Cdd:COG1404 213 LGGpadGYSDALAAAVD----YAVDKGVLVVAAAGNSGSDDATVSYpaAYPNVIAVGA---------------------- 266
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 357 slfkgealpdkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilantaangee 436
Cdd:COG1404     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 437 lvadahllpattvgekagdiirhyvtTDPNPTasisilgtvvgvkpspvVAAFSSRGPnsitpnilKPDLIAPGVNILAA 516
Cdd:COG1404 267 --------------------------VDANGQ-----------------LASFSNYGP--------KVDVAAPGVDILST 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 517 WTGAAgptglasdsrrveFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTayktykdgkplldiATGKPSTP 596
Cdd:COG1404 296 YPGGG-------------YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNT--------------ATPLGAPG 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 597 FDHGAGHVSPTTATNPGLIYDLTTEDylgflcALNYTSPQIRSVSRRNYTCDPSKSYSVADLNYPSFAVNVDGVGAYKYT 676
Cdd:COG1404 349 PYYGYGLLADGAAGATSAGAGLAAAA------GAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATAAG 422
                       490       500       510
                ....*....|....*....|....*....|.
gi 18425181 677 RTVTSVGGAGTYSVKVTSETTGVKISVEPAV 707
Cdd:COG1404 423 LLAAAALSTLAAVAAAVVVTTGTSTEALVAV 453
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
131-578 4.99e-24

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: 102.92  E-value: 4.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   131 SDVVVGVLDTGVwpeskSYSDEGFgpipsswKGGCEAGTNFTASLCNRkligarffaRGYESTMGPIDEskesrspRDDD 210
Cdd:pfam00082   2 KGVVVAVLDTGI-----DPNHPDL-------SGNLDNDPSDDPEASVD---------FNNEWDDPRDDI-------DDKN 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   211 GHGTHTSSTAAGSVVEGASLLGyasgtargMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGggmSDYY 290
Cdd:pfam00082  54 GHGTHVAGIIAAGGNNSIGVSG--------VAPGAKILGVRVFGDGGGTDAITAQAISWAIPQGADVINMSWG---SDKT 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   291 RDGV-----AIGAFA-AMERGILVSCSAGNAGPSSSSLSNVapwittvgagtldrDFPALAilgngKNFTGVslfkgeal 364
Cdd:pfam00082 123 DGGPgswsaAVDQLGgAEAAGSLFVWAAGNGSPGGNNGSSV--------------GYPAQY-----KNVIAV-------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   365 pdkllpfiyaGNASNATNGNLcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilantaangeelvadahll 444
Cdd:pfam00082 176 ----------GAVDEASEGNL----------------------------------------------------------- 186
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   445 pattvgekagdiirhyvttdpnptasisilgtvvgvkpspvvAAFSSRGPNSITPniLKPDLIAPGVNIlAAWTGAAGPT 524
Cdd:pfam00082 187 ------------------------------------------ASFSSYGPTLDGR--LKPDIVAPGGNI-TGGNISSTLL 221
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18425181   525 GLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKT 578
Cdd:pfam00082 222 TTTSDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDL 275
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
31-106 1.06e-21

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: 89.66  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181    31 TYIVHMAK-SQMPSSFDLHSNWYDSSLRSI-----SDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYE 104
Cdd:pfam05922   1 TYIVYLKEgAAAADSFSSHTEWHSSLLRSVlseesSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80

                  ..
gi 18425181   105 LH 106
Cdd:pfam05922  81 LH 82
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
380-457 3.66e-13

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


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 65.61  E-value: 3.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   380 ATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILAN--------TAANGEELVADAHLLPATTVGE 451
Cdd:pfam02225   6 LAPGCYAGDGIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNnveglggpPGAGGNELYPDGIYIPAVGVSR 85

                  ....*.
gi 18425181   452 KAGDII 457
Cdd:pfam02225  86 ADGEAL 91
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
461-575 2.65e-10

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


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 62.73  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   461 VTTDPNPTASISILgTVVGVKPSPVVAAFSSRGPnsitpnilKPDLIAPGVNILAAWTGAAGPTglasdsrrvefnIISG 540
Cdd:TIGR03921 166 KTTVVYPAWYPGVL-AVGSIDRDGTPSSFSLPGP--------WVDLAAPGENIVSLSPGGDGLA------------TTSG 224
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 18425181   541 TSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:TIGR03921 225 TSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATA 259
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
490-554 1.42e-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: 55.17  E-value: 1.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18425181   490 SSRGPNSItpNILKPDLIAPGVNILAAWTGAAGPTglasdsrrvefniISGTSMSCPHVSGLAAL 554
Cdd:NF040809  994 SSRGPTIR--NIQKPDIVAPGVNIIAPYPGNTYAT-------------ITGTSAAAAHVSGVAAL 1043
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
485-555 1.31e-06

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 52.09  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18425181   485 VVAAFSSRGpnSITPNILKPDLIAPGVNILAAWTGaaGPTGlasdsrrvefnIISGTSMSCPHVSGLAALL 555
Cdd:NF040809  417 VVSVFSGEG--DIENGIYKPDLLAPGENIVSYLPG--GTTG-----------ALTGTSMATPHVTGVCSLL 472
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
491-563 2.56e-03

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 41.11  E-value: 2.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18425181  491 SRGPNSITPNILkPDLIAPGVNILaawtgaagptglaSDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWS 563
Cdd:PTZ00262 520 SLSPNSFYSAKY-CQLAAPGTNIY-------------STFPKNSYRKLNGTSMAAPHVAAIASLILSINPSLS 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 ...
103-576 1.26e-147

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: 433.56  E-value: 1.26e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 103 YELHTTRTPLFLGLDEHTADLFPEAGSY-SDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLI 181
Cdd:cd04852   1 YQLHTTRSPDFLGLPGAWGGSLLGAANAgEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPFSCNNKLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 182 GARFFARGYESTMGpIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCW-LGGCFS 260
Cdd:cd04852  81 GARYFSDGYDAYGG-FNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWpDGGCFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 261 SDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTldrd 340
Cdd:cd04852 160 SDILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST---- 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 341 fpalailgngknftgvslfkgealpdkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaa 420
Cdd:cd04852     --------------------------------------------------------------------------------
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 421 ggvgmilantaangeelvadahllpattvgekagdiirhyvttdpnptasisilgtvvgvkpspvvaafssrgpnsitpn 500
Cdd:cd04852     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18425181 501 iLKPDLIAPGVNILAAWTgaaGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAY 576
Cdd:cd04852 236 -LKPDIAAPGVDILAAWT---PEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
346-471 6.62e-40

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: 142.94  E-value: 6.62e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 346 ILGNGKNFTGVSLFKGealPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGIN-ARVQKGDVVKAAGGVG 424
Cdd:cd02120   3 TLGNGKTIVGQSLYPG---NLKTYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNtSRVAKGDAVKAAGGAG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18425181 425 MILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASI 471
Cdd:cd02120  80 MILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
131-609 2.61e-37

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: 141.70  E-value: 2.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 131 SDVVVGVLDTGVwpeskSYSDEGFGPipsswkggceagtnftASLCNRKLIGARFFARGYESTMGPIDESKESR--SPRD 208
Cdd:cd07474   2 KGVKVAVIDTGI-----DYTHPDLGG----------------PGFPNDKVKGGYDFVDDDYDPMDTRPYPSPLGdaSAGD 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 209 DDGHGTHTSSTAAGSvvegasllGYASGTARGMAPRARVAVYKVCWLGG-CFSSDILAAIDKAIADNVNVLSMSLGGGMS 287
Cdd:cd07474  61 ATGHGTHVAGIIAGN--------GVNVGTIKGVAPKADLYAYKVLGPGGsGTTDVIIAAIEQAVDDGMDVINLSLGSSVN 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 288 DYYrDGVAIGAFAAMERGILVSCSAGNAGPsssslsnvAPWITtvgagtldrDFPAlailgngknftgvslfkgealpdk 367
Cdd:cd07474 133 GPD-DPDAIAINNAVKAGVVVVAAAGNSGP--------APYTI---------GSPA------------------------ 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 368 llpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilanTAANgeelvadahllpAT 447
Cdd:cd07474 171 --------------------------------------------------------------TAPS------------AI 176
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 448 TVGekagdiirhyvttdpnptASisilgTVVGVKPSPVVAAFSSRGPNSItPNILKPDLIAPGVNILAAWTGAAgpTGLA 527
Cdd:cd07474 177 TVG------------------AS-----TVADVAEADTVGPSSSRGPPTS-DSAIKPDIVAPGVDIMSTAPGSG--TGYA 230
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 528 SdsrrvefniISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAyktykdgKPLLDiATGKPSTPFDHGAGHVSPT 607
Cdd:cd07474 231 R---------MSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTA-------KPLYD-SDGVVYPVSRQGAGRVDAL 293

                ..
gi 18425181 608 TA 609
Cdd:cd07474 294 RA 295
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
657-754 3.79e-36

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


Pssm-ID: 465493  Cd Length: 98  Bit Score: 131.17  E-value: 3.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   657 DLNYPSFAVNV-DGVGAYKYTRTVTSVG-GAGTYSVKVTSeTTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSkPSGSN 734
Cdd:pfam17766   1 DLNYPSIAVSFeNLNGSVTVTRTVTNVGdGPSTYTASVTA-PPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKA-PSGEY 78
                          90       100
                  ....*....|....*....|
gi 18425181   735 SFGSIEWSDGKHVVGSPVAI 754
Cdd:pfam17766  79 VFGSLTWSDGKHTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
203-707 1.92e-28

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 119.43  E-value: 1.92e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 203 SRSPRDDDGHGTHTSSTAAGSvvegasllGYASGTARGMAPRARVAVYKVCW-LGGCFSSDILAAIDKAIADNVNVLSMS 281
Cdd:COG1404 141 DGDPSDDNGHGTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDdNGSGTTSDIAAAIDWAADNGADVINLS 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 282 LGG---GMSDYYRDGVAigafAAMERGILVSCSAGNAGPSSSSLSN--VAPWITTVGAgtldrdfpalailgngknftgv 356
Cdd:COG1404 213 LGGpadGYSDALAAAVD----YAVDKGVLVVAAAGNSGSDDATVSYpaAYPNVIAVGA---------------------- 266
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 357 slfkgealpdkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilantaangee 436
Cdd:COG1404     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 437 lvadahllpattvgekagdiirhyvtTDPNPTasisilgtvvgvkpspvVAAFSSRGPnsitpnilKPDLIAPGVNILAA 516
Cdd:COG1404 267 --------------------------VDANGQ-----------------LASFSNYGP--------KVDVAAPGVDILST 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 517 WTGAAgptglasdsrrveFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTayktykdgkplldiATGKPSTP 596
Cdd:COG1404 296 YPGGG-------------YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNT--------------ATPLGAPG 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 597 FDHGAGHVSPTTATNPGLIYDLTTEDylgflcALNYTSPQIRSVSRRNYTCDPSKSYSVADLNYPSFAVNVDGVGAYKYT 676
Cdd:COG1404 349 PYYGYGLLADGAAGATSAGAGLAAAA------GAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATAAG 422
                       490       500       510
                ....*....|....*....|....*....|.
gi 18425181 677 RTVTSVGGAGTYSVKVTSETTGVKISVEPAV 707
Cdd:COG1404 423 LLAAAALSTLAAVAAAVVVTTGTSTEALVAV 453
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
131-576 8.66e-28

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: 113.06  E-value: 8.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 131 SDVVVGVLDTGVWpesksysdegfGPIPSSWkggceagtnftaslcNRKLIGARFfargyestmgpIDESKESRSPRDDD 210
Cdd:cd07487   2 KGITVAVLDTGID-----------APHPDFD---------------GRIIRFADF-----------VNTVNGRTTPYDDN 44
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 211 GHGTHTSSTAAGSvvegasllGYAS-GTARGMAPRARVAVYKVcwL---GGCFSSDILAAIDKAIAD----NVNVLSMSL 282
Cdd:cd07487  45 GHGTHVAGIIAGS--------GRASnGKYKGVAPGANLVGVKV--LddsGSGSESDIIAGIDWVVENnekyNIRVVNLSL 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 283 GGGMSDYYRDGVAIGAF-AAMERGILVSCSAGNAGPSSsslsnvapwiTTVGAgtldrdfpalailgngknftgvslfkg 361
Cdd:cd07487 115 GAPPDPSYGEDPLCQAVeRLWDAGIVVVVAAGNSGPGP----------GTITS--------------------------- 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 362 ealpdkllPfiyaGNAsnatngnlcmtgtlipEKVkgkivmcdrginarvqkgdvvkaaggvgmIlantaangeelvada 441
Cdd:cd07487 158 --------P----GNS----------------PKV-----------------------------I--------------- 165
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 442 hllpatTVGekagdiirhyvTTDPNPTASISIlgtvvgvkpspvvAAFSSRGPNSitPNILKPDLIAPGVNILAAWTGAA 521
Cdd:cd07487 166 ------TVG-----------AVDDNGPHDDGI-------------SYFSSRGPTG--DGRIKPDVVAPGENIVSCRSPGG 213
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18425181 522 GPTGLASDSRRVEfniiSGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAY 576
Cdd:cd07487 214 NPGAGVGSGYFEM----SGTSMATPHVSGAIALLLQANPILTPDEVKCILRDTAT 264
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
131-578 4.99e-24

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: 102.92  E-value: 4.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   131 SDVVVGVLDTGVwpeskSYSDEGFgpipsswKGGCEAGTNFTASLCNRkligarffaRGYESTMGPIDEskesrspRDDD 210
Cdd:pfam00082   2 KGVVVAVLDTGI-----DPNHPDL-------SGNLDNDPSDDPEASVD---------FNNEWDDPRDDI-------DDKN 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   211 GHGTHTSSTAAGSVVEGASLLGyasgtargMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGggmSDYY 290
Cdd:pfam00082  54 GHGTHVAGIIAAGGNNSIGVSG--------VAPGAKILGVRVFGDGGGTDAITAQAISWAIPQGADVINMSWG---SDKT 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   291 RDGV-----AIGAFA-AMERGILVSCSAGNAGPSSSSLSNVapwittvgagtldrDFPALAilgngKNFTGVslfkgeal 364
Cdd:pfam00082 123 DGGPgswsaAVDQLGgAEAAGSLFVWAAGNGSPGGNNGSSV--------------GYPAQY-----KNVIAV-------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   365 pdkllpfiyaGNASNATNGNLcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilantaangeelvadahll 444
Cdd:pfam00082 176 ----------GAVDEASEGNL----------------------------------------------------------- 186
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   445 pattvgekagdiirhyvttdpnptasisilgtvvgvkpspvvAAFSSRGPNSITPniLKPDLIAPGVNIlAAWTGAAGPT 524
Cdd:pfam00082 187 ------------------------------------------ASFSSYGPTLDGR--LKPDIVAPGGNI-TGGNISSTLL 221
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18425181   525 GLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKT 578
Cdd:pfam00082 222 TTTSDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDL 275
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
206-576 4.74e-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: 99.16  E-value: 4.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 206 PRDDDGHGTHTSSTAAGsvvegasllGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGg 285
Cdd:cd07490  39 VFDAGGHGTHVSGTIGG---------GGAKGVYIGVAPEADLLHGKVLDDGGGSLSQIIAGMEWAVEKDADVVSMSLGG- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 286 msDYYRDGVAIGAFAAMER--GILVSCSAGNAGPSSSSLSNVAPWITTVGAgtLDRDfpalailGNGKNFTgvSLFKGEA 363
Cdd:cd07490 109 --TYYSEDPLEEAVEALSNqtGALFVVSAGNEGHGTSGSPGSAYAALSVGA--VDRD-------DEDAWFS--SFGSSGA 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 364 LPDKllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilantaangeelvadahl 443
Cdd:cd07490 176 SLVS---------------------------------------------------------------------------- 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 444 lpattvgekagdiirhyvttdpnptasisilgtvvgvkpspvvaafssrGPNSITPNILKPDLIAPGVNILAAWTGAAGP 523
Cdd:cd07490 180 -------------------------------------------------APDSPPDEYTKPDVAAPGVDVYSARQGANGD 210
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 18425181 524 TGLASdsrrvefniISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAY 576
Cdd:cd07490 211 GQYTR---------LSGTSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
31-106 1.06e-21

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: 89.66  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181    31 TYIVHMAK-SQMPSSFDLHSNWYDSSLRSI-----SDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYE 104
Cdd:pfam05922   1 TYIVYLKEgAAAADSFSSHTEWHSSLLRSVlseesSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80

                  ..
gi 18425181   105 LH 106
Cdd:pfam05922  81 LH 82
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
205-574 1.60e-19

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: 87.97  E-value: 1.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 205 SPRDDDGHGTHTSSTAAGS-----VVegasllgyasgtarGMAPRARVAVYKVCWLGGC-FSSDILAAIDKAIADNVNVL 278
Cdd:cd07477  35 DYQDGNGHGTHVAGIIAALdngvgVV--------------GVAPEADLYAVKVLNDDGSgTYSDIIAGIEWAIENGMDII 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 279 SMSLGGGM-SDYYRDGVAigafAAMERGILVSCSAGNAGPSSSSLsnvapwittvgagtldrDFPAlailgngknftgvs 357
Cdd:cd07477 101 NMSLGGPSdSPALREAIK----KAYAAGILVVAAAGNSGNGDSSY-----------------DYPA-------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 358 lfkgeALPDkllpfiyagnasnatngnlcmtgtlipekvkgkiVMCdrginarvqkgdvvkaaggVGmilANTAANgeel 437
Cdd:cd07477 146 -----KYPS----------------------------------VIA-------------------VG---AVDSNN---- 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 438 vadahllpattvgekagdiirhyvttdpnptasisilgtvvgvkpspVVAAFSSRGPNsitpnilkPDLIAPGVNILAAW 517
Cdd:cd07477 161 -----------------------------------------------NRASFSSTGPE--------VELAAPGVDILSTY 185
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18425181 518 TGAagptglasdsrrvEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTT 574
Cdd:cd07477 186 PNN-------------DYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
198-602 2.97e-19

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: 90.02  E-value: 2.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 198 DESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYasgtaRGMAPRARVAVYKV---CWLGGCFSSDILAAIDKAIADN 274
Cdd:cd07475  70 DNNDDILDEDDGSSHGMHVAGIVAGNGDEEDNGEGI-----KGVAPEAQLLAMKVfsnPEGGSTYDDAYAKAIEDAVKLG 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 275 VNVLSMSLGGGMSDYYRDGVAIGAFA-AMERGILVSCSAGNAGPSSSslsnvapwittvgagtldrdfpalailgngknf 353
Cdd:cd07475 145 ADVINMSLGSTAGFVDLDDPEQQAIKrAREAGVVVVVAAGNDGNSGS--------------------------------- 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 354 tgvslfkGEALPDKLLPFIYAGNASNATNGNlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilANTAAN 433
Cdd:cd07475 192 -------GTSKPLATNNPDTGTVGSPATADD-------------------------------------------VLTVAS 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 434 GEELVadahllpattvgekagdiirhyvttdPNPTAsisilgtvvgvkpsPVVAAFSSRGPnsiTPNI-LKPDLIAPGVN 512
Cdd:cd07475 222 ANKKV--------------------------PNPNG--------------GQMSGFSSWGP---TPDLdLKPDITAPGGN 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 513 ILAAwtgaagptgLASDsrrvEFNIISGTSMSCPHVSGLAAL----LKSVHPEWSPA----AIRSALMTTAyktykdgKP 584
Cdd:cd07475 259 IYST---------VNDN----TYGYMSGTSMASPHVAGASALvkqrLKEKYPKLSGEelvdLVKNLLMNTA-------TP 318
                       410
                ....*....|....*....
gi 18425181 585 LLDIA-TGKPSTPFDHGAG 602
Cdd:cd07475 319 PLDSEdTKTYYSPRRQGAG 337
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
133-574 2.19e-18

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: 85.33  E-value: 2.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 133 VVVGVLDTGVWPESksysdegfgPIPSSWKGGCEAGTNFTaslcnrkligarffargyestmgpiDESKESRSPRDDDGH 212
Cdd:cd00306   1 VTVAVIDTGVDPDH---------PDLDGLFGGGDGGNDDD-------------------------DNENGPTDPDDGNGH 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 213 GTHTSSTAAGSvvegasllgYASGTARGMAPRARVAVYKVCW-LGGCFSSDILAAIDKAIADN-VNVLSMSLGGGMSDYY 290
Cdd:cd00306  47 GTHVAGIIAAS---------ANNGGGVGVAPGAKLIPVKVLDgDGSGSSSDIAAAIDYAAADQgADVINLSLGGPGSPPS 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 291 RDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSN---VAPWITTVGAgtldrdfpalailgngknftgvslfkgealpdk 367
Cdd:cd00306 118 SALSEAIDYALAKLGVLVVAAAGNDGPDGGTNIGypaASPNVIAVGA--------------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 368 llpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilantaangeelvadahllpat 447
Cdd:cd00306     --------------------------------------------------------------------------------
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 448 tvgekagdiirhyVTTDPNPTASisilgtvvgvkpspvvaaFSSRGPnsitpnilKPDLIAPGVNILAAWTGAAGptgla 527
Cdd:cd00306 165 -------------VDRDGTPASP------------------SSNGGA--------GVDIAAPGGDILSSPTTGGG----- 200
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 18425181 528 sdsrrvEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTT 574
Cdd:cd00306 201 ------GYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
183-579 3.59e-18

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: 88.06  E-value: 3.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 183 ARFFARGYESTMGPIDESKESRSP------RDDDGHGTHTSSTAAGSvvegasllGYASGTARGMAPRARVAV------- 249
Cdd:cd07478  45 PGGYYGGGEYTEEIINAALASDNPydivpsRDENGHGTHVAGIAAGN--------GDNNPDFKGVAPEAELIVvklkqak 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 250 -YKVCWLGG--CF-SSDILAAID--KAIADNVN---VLSMSLGGGMSDyyRDGV-----AIGAFAAMeRGILVSCSAGNA 315
Cdd:cd07478 117 kYLREFYEDvpFYqETDIMLAIKylYDKALELNkplVINISLGTNFGS--HDGTsllerYIDAISRL-RGIAVVVGAGNE 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 316 GPSSSSLSNvapwitTVGAGTLDRDFPaLAILGNGKNFTgVSLFKgeALPDKL-----------LPFIYAGNaSNATNGN 384
Cdd:cd07478 194 GNTQHHHSG------GIVPNGETKTVE-LNVGEGEKGFN-LEIWG--DFPDRFsvsiispsgesSGRINPGI-GGSESYK 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 385 LCMTGTLI------PEKVKGK--IVMCDRGInarvqkgdvvkaAGGVGMILAnTAANGEELVADAHLLPATTVGEKagdi 456
Cdd:cd07478 263 FVFEGTTVyvyyylPEPYTGDqlIFIRFKNI------------KPGIWKIRL-TGVSITDGRFDAWLPSRGLLSEN---- 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 457 IRHyvtTDPNPTASISILGTVVGVKpspVVAA----------FSSRGPNsiTPNILKPDLIAPGVNILAAwtgaaGPTGl 526
Cdd:cd07478 326 TRF---LEPDPYTTLTIPGTARSVI---TVGAynqnnnsiaiFSGRGPT--RDGRIKPDIAAPGVNILTA-----SPGG- 391
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 18425181 527 asdsrrvEFNIISGTSMSCPHVSGLAALLKsvhpEWSPAAIRSALMTTAY-KTY 579
Cdd:cd07478 392 -------GYTTRSGTSVAAAIVAGACALLL----QWGIVRGNDPYLYGEKiKTY 434
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
131-575 4.07e-17

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: 81.86  E-value: 4.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 131 SDVVVGVLDTGVwpeskSYSDEGFgpIPSSWKGGCEAGTNftaslcnrkligaRFFARGYestmGPIDE------SKESR 204
Cdd:cd07473   2 GDVVVAVIDTGV-----DYNHPDL--KDNMWVNPGEIPGN-------------GIDDDGN----GYVDDiygwnfVNNDN 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 205 SPRDDDGHGTHTSSTAAGSVvegasllGYASGTArGMAPRARVAVYKVcwLGGC---FSSDILAAIDKAIADNVNVLSMS 281
Cdd:cd07473  58 DPMDDNGHGTHVAGIIGAVG-------NNGIGIA-GVAWNVKIMPLKF--LGADgsgTTSDAIKAIDYAVDMGAKIINNS 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 282 LGG-GMSDYYRDGVAigafAAMERGILVSCSAGNAG---------PSSSSLSNvapwITTVGAgtldrdfpalailgngk 351
Cdd:cd07473 128 WGGgGPSQALRDAIA----RAIDAGILFVAAAGNDGtnndktptyPASYDLDN----IISVAA----------------- 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 352 nftgvslfkgealpdkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaaggvgmilanta 431
Cdd:cd07473     --------------------------------------------------------------------------------
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 432 angeelvadahllpattvgekagdiirhyvtTDPNPTAsisilgtvvgvkpspvvAAFSSRGPNSItpnilkpDLIAPGV 511
Cdd:cd07473 183 -------------------------------TDSNDAL-----------------ASFSNYGKKTV-------DLAAPGV 207
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18425181 512 NILAAWTGAAgptglasdsrrveFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:cd07473 208 DILSTSPGGG-------------YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSA 258
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
485-575 1.03e-14

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: 74.72  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 485 VVAAFSSRGPnsITPNILKPDLIAPGVNILAAWTGaagptglasdsrrVEFNIISGTSMSCPHVSGLAALLKSVHPEWSP 564
Cdd:cd07481 186 VLADFSSRGP--STYGRIKPDISAPGVNIRSAVPG-------------GGYGSSSGTSMAAPHVAGVAALLWSANPSLIG 250
                        90
                ....*....|...
gi 18425181 565 A--AIRSALMTTA 575
Cdd:cd07481 251 DvdATEAILTETA 263
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
483-575 3.48e-14

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: 73.90  E-value: 3.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 483 SPVVAAFSSRGPNsiTPNILKPDLIAPGVNILAAWTGAAGPTGLASDSrrveFNIISGTSMSCPHVSGLAALL------- 555
Cdd:cd04842 198 SDTVASFSSRGPT--YDGRIKPDLVAPGTGILSARSGGGGIGDTSDSA----YTSKSGTSMATPLVAGAAALLrqyfvdg 271
                        90       100
                ....*....|....*....|...
gi 18425181 556 ---KSVHPewSPAAIRSALMTTA 575
Cdd:cd04842 272 yypTKFNP--SAALLKALLINSA 292
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
133-604 5.14e-14

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: 73.79  E-value: 5.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 133 VVVGVLDTGVWpesksYSDE----GFGPipsswkgGC--EAGTNFtaslcnrklIGARFFARGyesTMGPIDEskesrsP 206
Cdd:cd07489  15 VKVAVVDTGID-----YTHPalggCFGP-------GCkvAGGYDF---------VGDDYDGTN---PPVPDDD------P 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 207 RDDDGHGTHTSSTAAGSvvegASLLGYAsgtarGMAPRARVAVYKVCWLGGCFSSD-ILAAIDKAIADNVNVLSMSLGGG 285
Cdd:cd07489  65 MDCQGHGTHVAGIIAAN----PNAYGFT-----GVAPEATLGAYRVFGCSGSTTEDtIIAAFLRAYEDGADVITASLGGP 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 286 mSDYYRDGVAIGAFAAMERGILVSCSAGNAGpsssslsnvapwittvgagtldrdfpalailgngknftgvslfkgealp 365
Cdd:cd07489 136 -SGWSEDPWAVVASRIVDAGVVVTIAAGNDG------------------------------------------------- 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 366 dkllpfiyagnasnatngnlcmtgtlipekvkgkivmcdrginarvqkgdvvkaagGVGMILANTAANGEELVAdahllp 445
Cdd:cd07489 166 --------------------------------------------------------ERGPFYASSPASGRGVIA------ 183
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 446 attvgekagdiirhyvttdpnpTASISilgtvvgvkpspvvAAFSSRGP-NSItpnILKPDLIAPGVNILAAWtgaagPT 524
Cdd:cd07489 184 ----------------------VASVD--------------SYFSSWGPtNEL---YLKPDVAAPGGNILSTY-----PL 219
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 525 GLASdsrrveFNIISGTSMSCPHVSGLAALLKSV-HPEWSPAAIRSALMTTAyktykdgKPLL----DIATGKPSTPFDH 599
Cdd:cd07489 220 AGGG------YAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTA-------KPLPwsdgTSALPDLAPVAQQ 286

                ....*
gi 18425181 600 GAGHV 604
Cdd:cd07489 287 GAGLV 291
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
205-602 8.94e-14

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: 72.79  E-value: 8.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 205 SPRDDDGHGTHTSSTAAGSVVEGasllgyasgTARGMAPRARVAVYKVCW-LGGCFSSDILAAIDKAIADNVNVLSMSLG 283
Cdd:cd07480  41 DVQDGHGHGTHCAGTIFGRDVPG---------PRYGVARGAEIALIGKVLgDGGGGDGGILAGIQWAVANGADVISMSLG 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 284 GgmsdyyrdgvaigafaamergilvscsagnagpsssslsnvapwittvgagtldrDFPALAILGNgknftgvslFKGEA 363
Cdd:cd07480 112 A-------------------------------------------------------DFPGLVDQGW---------PPGLA 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 364 LPDKLLPfiYAGNASNATNGnlcmtgtlipekvkgkivMCDRGINARVQKGDVVKAAGGvgmilantaangeelvadahl 443
Cdd:cd07480 128 FSRALEA--YRQRARLFDAL------------------MTLVAAQAALARGTLIVAAAG--------------------- 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 444 lpattvGEKAGDIIRHYVTtdpNPTASISILGtVVGVKPSPVVAAFSSRGPNSITpnilKPDLIAPGVNILAAWTGaagp 523
Cdd:cd07480 167 ------NESQRPAGIPPVG---NPAACPSAMG-VAAVGALGRTGNFSAVANFSNG----EVDIAAPGVDIVSAAPG---- 228
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18425181 524 TGLASdsrrvefniISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKTYKDGkplldIATGKPSTPFDHGAG 602
Cdd:cd07480 229 GGYRS---------MSGTSMATPHVAGVAALWAEALPKAGGRALAALLQARLTAARTTQ-----FAPGLDLPDRGVGLG 293
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
505-575 1.16e-13

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: 71.39  E-value: 1.16e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18425181 505 DLIAPGVNILAAWTGaagptglaSDSrrvEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:cd04077 194 DIFAPGVDILSAWIG--------SDT---ATATLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
380-457 3.66e-13

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


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 65.61  E-value: 3.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   380 ATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILAN--------TAANGEELVADAHLLPATTVGE 451
Cdd:pfam02225   6 LAPGCYAGDGIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNnveglggpPGAGGNELYPDGIYIPAVGVSR 85

                  ....*.
gi 18425181   452 KAGDII 457
Cdd:pfam02225  86 ADGEAL 91
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
206-339 2.83e-11

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


Pssm-ID: 173810 [Multi-domain]  Cd Length: 260  Bit Score: 64.59  E-value: 2.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 206 PRDDDGHGTHTSSTAAGSVVEGaslLGYAsgtarGMAPRARVAVYKVcwL---GGCFSSDILAAIDKAIADNVNVLSMSL 282
Cdd:cd07484  64 AMDDNGHGTHVAGIIAAATNNG---TGVA-----GVAPKAKIMPVKV--LdanGSGSLADIANGIRYAADKGAKVINLSL 133
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18425181 283 GGGM-SDYYRDGVAIgafaAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDR 339
Cdd:cd07484 134 GGGLgSTALQEAINY----AWNKGVVVVAAAGNEGVSSVSYPAAYPGAIAVAATDQDD 187
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
505-575 2.38e-10

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: 61.89  E-value: 2.38e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18425181 505 DLIAPGVNILAAWTGAAgptglasdsrrveFNIISGTSMSCPHVSGLAALLKSVHPeWSPAAIRSALMTTA 575
Cdd:cd07484 200 DVSAPGGGILSTTPDGD-------------YAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTA 256
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
461-575 2.65e-10

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


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 62.73  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181   461 VTTDPNPTASISILgTVVGVKPSPVVAAFSSRGPnsitpnilKPDLIAPGVNILAAWTGAAGPTglasdsrrvefnIISG 540
Cdd:TIGR03921 166 KTTVVYPAWYPGVL-AVGSIDRDGTPSSFSLPGP--------WVDLAAPGENIVSLSPGGDGLA------------TTSG 224
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 18425181   541 TSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:TIGR03921 225 TSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATA 259
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
420-575 4.68e-10

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: 60.78  E-value: 4.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 420 AGGVGMILANTAANgeelvadahllpattvgekAGDIIRHYVTTdpnPTASISILgTVVGVKPSPVVAAFSSRGPNSitP 499
Cdd:cd07493 143 AASKGMLVVNSAGN-------------------EGSTQWKGIGA---PADAENVL-SVGAVDANGNKASFSSIGPTA--D 197
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18425181 500 NILKPDLIAPGVNILAawtgaagptglasDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:cd07493 198 GRLKPDVMALGTGIYV-------------INGDGNITYANGTSFSCPLIAGLIACLWQAHPNWTNLQIKEAILKSA 260
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
430-575 1.66e-09

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: 59.61  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 430 TAANGEELVADAHLLPATTVGEKAGD--IIRHYVTTDPNPTASISILGTVVGVKPSPVVAAFSSRGPNSI---TPNIL-K 503
Cdd:cd05562 111 IAQAVDEVVASPGVLYFSSAGNDGQSgsIFGHAAAPGAIAVGAVDYGNTPAFGSDPAPGGTPSSFDPVGIrlpTPEVRqK 190
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18425181 504 PDLIAPgvnilaawTGAAGPTGLASDsrrvEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:cd05562 191 PDVTAP--------DGVNGTVDGDGD----GPPNFFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTA 250
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
476-574 4.22e-09

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: 58.46  E-value: 4.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 476 TVVGVKPSPVVAAFSSRGPnsitpnilKPDLIAPGVNILA-AWTGAAGPTGLASDS-RRVEFNIISGTSMSCPHVSGLAA 553
Cdd:cd07496 193 AVGATDLRGQRASYSNYGP--------AVDVSAPGGDCASdVNGDGYPDSNTGTTSpGGSTYGFLQGTSMAAPHVAGVAA 264
                        90       100
                ....*....|....*....|.
gi 18425181 554 LLKSVHPEWSPAAIRSALMTT 574
Cdd:cd07496 265 LMKSVNPSLTPAQIESLLQST 285
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
198-316 2.17e-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: 2.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 198 DESKESRSPRDDD---GHGTHTSSTAAgsvvegasllgyASGTARGMAPRARVAVYKVC-WLGGCFSSDILAAIDKAIAD 273
Cdd:cd07482  38 KEAGETGDINDIVdklGHGTAVAGQIA------------ANGNIKGVAPGIGIVSYRVFgSCGSAESSWIIKAIIDAADD 105
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18425181 274 NVNVLSMSLGG---GMSDYYRDGVAIGAFA-----AMERGILVSCSAGNAG 316
Cdd:cd07482 106 GVDVINLSLGGyliIGGEYEDDDVEYNAYKkainyAKSKGSIVVAAAGNDG 156
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
487-574 1.40e-07

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: 53.12  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 487 AAFSSRGPNSitpnilkpDLIAPGVNIlaaWTGAAGPtGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAA 566
Cdd:cd07498 167 ASYSNYGNYV--------DLVAPGVGI---WTTGTGR-GSAGDYPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAE 234

                ....*...
gi 18425181 567 IRSALMTT 574
Cdd:cd07498 235 VEDILTST 242
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
490-554 1.42e-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: 55.17  E-value: 1.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18425181   490 SSRGPNSItpNILKPDLIAPGVNILAAWTGAAGPTglasdsrrvefniISGTSMSCPHVSGLAAL 554
Cdd:NF040809  994 SSRGPTIR--NIQKPDIVAPGVNIIAPYPGNTYAT-------------ITGTSAAAAHVSGVAAL 1043
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
237-337 7.94e-07

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


Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 51.93  E-value: 7.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 237 TARGMAPRARVAVYKVcwlGGCFSSDILAAIDKAIADN---VNVLSMSLGGG---MSDYYRDGV--AIGAFAAmeRGILV 308
Cdd:cd04056  82 YAGAIAPGANITLYFA---PGTVTNGPLLAFLAAVLDNpnlPSVISISYGEPeqsLPPAYAQRVcnLFAQAAA--QGITV 156
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18425181 309 SCSAGNAGPSSSSLSNVA-----------PWITTVGAGTL 337
Cdd:cd04056 157 LAASGDSGAGGCGGDGSGtgfsvsfpassPYVTAVGGTTL 196
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
131-326 1.00e-06

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


Pssm-ID: 173794 [Multi-domain]  Cd Length: 267  Bit Score: 50.79  E-value: 1.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 131 SDVVVGVLDTGVWPESKSYSDegfgpipsswkggceagtnftaslcnrKLIGARFFARGYESTmgpideskeSRSPRDDD 210
Cdd:cd04848   3 AGVKVGVIDSGIDLSHPEFAG---------------------------RVSEASYYVAVNDAG---------YASNGDGD 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 211 GHGTHTSSTAAGSVVEGAsllgyasgtARGMAPRARVAVYKVCWLGGC--FSSDILAAIDKAIADNVNVLSMSLGGGMSD 288
Cdd:cd04848  47 SHGTHVAGVIAAARDGGG---------MHGVAPDATLYSARASASAGStfSDADIAAAYDFLAASGVRIINNSWGGNPAI 117
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18425181 289 -----------YYRDGVAIGAFAAM-ERGILVSCSAGNAGPSSSSLSNVA 326
Cdd:cd04848 118 dtvsttykgsaATQGNTLLAALARAaNAGGLFVFAAGNDGQANPSLAAAA 167
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
485-555 1.31e-06

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 52.09  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18425181   485 VVAAFSSRGpnSITPNILKPDLIAPGVNILAAWTGaaGPTGlasdsrrvefnIISGTSMSCPHVSGLAALL 555
Cdd:NF040809  417 VVSVFSGEG--DIENGIYKPDLLAPGENIVSYLPG--GTTG-----------ALTGTSMATPHVTGVCSLL 472
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
486-575 1.43e-06

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


Pssm-ID: 173809 [Multi-domain]  Cd Length: 291  Bit Score: 50.82  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 486 VAAFSSRGPNSItpnilkpDLIAPGVNILAAWTGAagptglasdsrrvEFNIISGTSMSCPHVSGLAALLKSVHPEWSPA 565
Cdd:cd07483 221 VANFSNYGKKNV-------DVFAPGERIYSTTPDN-------------EYETDSGTSMAAPVVSGVAALIWSYYPNLTAK 280
                        90
                ....*....|
gi 18425181 566 AIRSALMTTA 575
Cdd:cd07483 281 EVKQIILESG 290
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
486-574 1.87e-06

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


Pssm-ID: 173811 [Multi-domain]  Cd Length: 273  Bit Score: 50.18  E-value: 1.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 486 VAAFSSRGPNSitpnilkpDLIAPGVN-ILAAWTGAAGPTGlasdsrrVEFNIISGTSMSCPHVSGLAALLKSVHP-EWS 563
Cdd:cd07485 198 KASFSNYGRWV--------DIAAPGVGtILSTVPKLDGDGG-------GNYEYLSGTSMAAPHVSGVAALVLSKFPdVFT 262
                        90
                ....*....|.
gi 18425181 564 PAAIRSALMTT 574
Cdd:cd07485 263 PEQIRKLLEES 273
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
486-575 3.35e-06

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: 49.78  E-value: 3.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 486 VAAFSSRGPNSItpNILKPDLIAPGVnilAAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALL------KSVH 559
Cdd:cd07497 221 VVSWSSRGPSIA--GDPKPDLAAIGA---FAWAPGRVLDSGGALDGNEAFDLFGGTSMATPMTAGSAALVisalkeKEGV 295
                        90
                ....*....|....*.
gi 18425181 560 PEWSPAAIRSALMTTA 575
Cdd:cd07497 296 GEYDPFLVRTILMSTA 311
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
479-572 4.15e-06

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


Pssm-ID: 173793 [Multi-domain]  Cd Length: 291  Bit Score: 49.22  E-value: 4.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 479 GVKPSPVVAAFSSRGPNSitPNILKPDLIAPGVNIL-----AAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAA 553
Cdd:cd04847 191 SAVGPAPAGATTSSGPGS--PGPIKPDVVAFGGNLAydpsgNAADGDLSLLTTLSSPSGGGFVTVGGTSFAAPLAARLAA 268
                        90
                ....*....|....*....
gi 18425181 554 LLKSVHPEWSPAAIRsALM 572
Cdd:cd04847 269 GLFAELPELSPETIR-ALL 286
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
506-575 5.02e-06

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


Pssm-ID: 173794 [Multi-domain]  Cd Length: 267  Bit Score: 48.86  E-value: 5.02e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 506 LIAPGVNILAawTGAAGPTGlasdsrrveFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:cd04848 208 LAAPGENIYS--TDPDGGNG---------YGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTA 266
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
373-471 3.44e-05

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. 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. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 44.04  E-value: 3.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 373 YAGNASNATNGNLCMTGTLIPEK--VKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELVADAHL------L 444
Cdd:cd00538  20 SSPVGVVAGPLVGCGYGTTDDSGadVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGDDPGPQMGSVGLestdpsI 99
                        90       100
                ....*....|....*....|....*..
gi 18425181 445 PATTVGEKAGDIIRHYVTTDPNPTASI 471
Cdd:cd00538 100 PTVGISYADGEALLSLLEAGKTVTVDL 126
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
506-575 6.01e-05

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


Pssm-ID: 173817 [Multi-domain]  Cd Length: 222  Bit Score: 45.02  E-value: 6.01e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 506 LIAPGVNILAAWTGaagptglaSDSRRVefniiSGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTA 575
Cdd:cd07492 165 FSADGVDIIAPAPH--------GRYLTV-----SGNSFAAPHVTGMVALLLSEKPDIDANDLKRLLQRLA 221
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
466-577 7.08e-05

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


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 45.14  E-value: 7.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 466 NPTASISILGtVVGVKPSPVVAAFSSRGPNSIT-PN---ILKPDLIAPGVNIlaawTGAAGPTGLASdsrrvefniISGT 541
Cdd:cd07479 147 NPADQMDVIG-VGGIDFDDNIARFSSRGMTTWElPGgygRVKPDIVTYGSGV----YGSKLKGGCRA---------LSGT 212
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18425181 542 SMSCPHVSGLAALLKSVHPE----WSPAAIRSALMTTAYK 577
Cdd:cd07479 213 SVASPVVAGAVALLLSTVPEkrdlINPASMKQALIESATR 252
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
206-334 9.49e-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: 44.64  E-value: 9.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 206 PRDDDGHGTHTSSTAAGSvveGASLLGYAsgtarGMAPRARV-AVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGG 284
Cdd:cd07498  36 TSDIDGHGTACAGVAAAV---GNNGLGVA-----GVAPGAKLmPVRIADSLGYAYWSDIAQAITWAADNGADVISNSWGG 107
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18425181 285 GMS------------DYYRDGvaigafaameRGILVSCSAGNAGPSSSSLSNVAPWITTVGA 334
Cdd:cd07498 108 SDStesissaidnaaTYGRNG----------KGGVVLFAAGNSGRSVSSGYAANPSVIAVAA 159
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
540-577 4.70e-04

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


Pssm-ID: 173796 [Multi-domain]  Cd Length: 412  Bit Score: 43.43  E-value: 4.70e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 18425181 540 GTSMSCPHVSGLAAL----LKSVHPEWSPAAIRSALMTTAYK 577
Cdd:cd04857 370 GTSMSSPNACGGIALllsgLKAEGIPYTPYSVRRALENTAKK 411
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
212-319 5.34e-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: 42.28  E-value: 5.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 212 HGTHTSSTAAGSVVEGASLLGYASGTARgmaprarVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYR 291
Cdd:cd05561  38 HGTAVASLLAGAGAQRPGLLPGADLYGA-------DVFGRAGGGEGASALALARALDWLAEQGVRVVNISLAGPPNALLA 110
                        90       100
                ....*....|....*....|....*...
gi 18425181 292 DGVAigafAAMERGILVSCSAGNAGPSS 319
Cdd:cd05561 111 AAVA----AAAARGMVLVAAAGNDGPAA 134
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
396-431 1.02e-03

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. 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: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 39.62  E-value: 1.02e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18425181 396 VKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTA 431
Cdd:cd04816  42 VKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNS 77
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
505-575 1.08e-03

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: 1.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18425181 505 DLIAPGVNILAAwTGAAGPTglasdsrrvefnIISGTSMSCPHVSGLAALLKSVHPEWsPAAIRSALMTTA 575
Cdd:cd05561 168 DFAAPGVDVWVA-APGGGYR------------YVSGTSFAAPFVTAALALLLQASPLA-PDDARARLAATA 224
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
208-340 1.38e-03

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


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 41.29  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 208 DDDGHGTHTSSTAAGSvvegasllgyaSGTARGMAPRARVAVYKVCWLGG-CFSSDILAAIDKAIADNVNVLSMSLGGgm 286
Cdd:cd07479  43 DGLGHGTFVAGVIASS-----------REQCLGFAPDAEIYIFRVFTNNQvSYTSWFLDAFNYAILTKIDVLNLSIGG-- 109
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18425181 287 SDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDRD 340
Cdd:cd07479 110 PDFMDKPFVDKVWELTANNIIMVSAIGNDGPLYGTLNNPADQMDVIGVGGIDFD 163
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
133-350 1.64e-03

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: 41.30  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 133 VVVGVLDTGVwpeskSYSDEGFGPIPSSWKGgceAGTNFTAslcnrKLIGARFFARGYESTMgpideskesrspRDDDGH 212
Cdd:cd07497   4 VVIAIVDTGV-----DYSHPDLDIYGNFSWK---LKFDYKA-----YLLPGMDKWGGFYVIM------------YDFFSH 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 213 GTHTSSTAAGSVVEGASLLGYASGTA-RGMAPRARVA----------VYKVCWLGGCFSSDILAAIDKAIADNVNVLSMS 281
Cdd:cd07497  59 GTSCASVAAGRGKMEYNLYGYTGKFLiRGIAPDAKIAavkalwfgdvIYAWLWTAGFDPVDRKLSWIYTGGPRVDVISNS 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18425181 282 LggGMSDYYRDGVAIGA--------FAAMERGILVSCSAGNAGPSSSSLSN--VAPWITTVGAGTlDRDFPALAILGNG 350
Cdd:cd07497 139 W--GISNFAYTGYAPGLdisslvidALVTYTGVPIVSAAGNGGPGYGTITApgAASLAISVGAAT-NFDYRPFYLFGYL 214
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
491-563 2.56e-03

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 41.11  E-value: 2.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18425181  491 SRGPNSITPNILkPDLIAPGVNILaawtgaagptglaSDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWS 563
Cdd:PTZ00262 520 SLSPNSFYSAKY-CQLAAPGTNIY-------------STFPKNSYRKLNGTSMAAPHVAAIASLILSINPSLS 578
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
209-334 2.89e-03

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: 40.37  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 209 DDGHGTHTSSTAAGsvvegasllgYASGTARGMAPRARVavykvcWLggcFSSDI------------LAAIDKAIADNVN 276
Cdd:cd07493  46 DDDHGTAVLSTMAG----------YTPGVMVGTAPNASY------YL---ARTEDvasetpveednwVAAAEWADSLGVD 106
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18425181 277 VLSMSLGGGMSDYYR--------DG----VAIGAFAAMERGILVSCSAGNAGPSSS---SLSNVAPWITTVGA 334
Cdd:cd07493 107 IISSSLGYTTFDNPTysytyadmDGktsfISRAANIAASKGMLVVNSAGNEGSTQWkgiGAPADAENVLSVGA 179
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
537-601 3.05e-03

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


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 40.54  E-value: 3.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18425181 537 IISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAyktykdgkplLDIATGKPSTPFDHGA 601
Cdd:cd07494 244 VFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTA----------RDVTKGASAQGTSAGP 298
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
361-471 5.10e-03

PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. 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. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.


Pssm-ID: 240122 [Multi-domain]  Cd Length: 118  Bit Score: 37.69  E-value: 5.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 361 GEALPDKLLPFIYAGNAsNATNGNLCMTGTLiPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELV-- 438
Cdd:cd04818   6 GPALTNVTADVVLAGAA-PASNTDGCTAFTN-AAAFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVANNVAGGAPITmg 83
                        90       100       110
                ....*....|....*....|....*....|....*
gi 18425181 439 --ADAHLLPATTVGEKAGDIIRHYVTTDPNPTASI 471
Cdd:cd04818  84 gdDPDITIPAVMISQADGDALKAALAAGGTVTVTL 118
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
185-316 8.85e-03

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


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 39.00  E-value: 8.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425181 185 FFARGYESTMGPIDESKESRspRDDDGHGThtsstaagsvVEGASLLGyasgtargMAPRARVAVYKvcwLGGCFSSDIL 264
Cdd:cd07494  38 FESRGYQVRVVLAPGATDPA--CDENGHGT----------GESANLFA--------IAPGAQFIGVK---LGGPDLVNSV 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18425181 265 AAIDKAIADNVNVLSMSLG-----GGMSDYYRDGVAIGAFA-----AMERGILVSCSAGNAG 316
Cdd:cd07494  95 GAFKKAISLSPDIISNSWGydlrsPGTSWSRSLPNALKALAatlqdAVARGIVVVFSAGNGG 156
 
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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