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Conserved domains on  [gi|1443072518|ref|XP_025880391|]
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subtilisin-like protease SBT3.9 [Oryza sativa Japonica Group]

Protein Classification

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 ...
47-485 9.13e-126

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: 374.63  E-value: 9.13e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  47 PNGLLAKAKYGEDIIIGVIDTGITPESPSFADDGYGPPPSKWKGVCQVGPSFKAKSCNRKLIGARWYID--DDTLRSMSK 124
Cdd:cd04852    19 GGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPFSCNNKLIGARYFSDgyDAYGGFNSD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 125 DEILSPRDVVGHGTHTASTAGGNIIHNASILGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILS 204
Cdd:cd04852    99 GEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGCFGSDILAAIDQAIADGVDVIS 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 205 LSLGG----PFEDP---GTLHVVAKGIPVVYSAGNDGPIAQTVENSSPWLLTVAAATmdrsfpvvitlgnndkfvaqsfa 277
Cdd:cd04852   179 YSIGGgspdPYEDPiaiAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST----------------------- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 278 isgktssqfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtllt 357
Cdd:cd04852       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 358 lpiplvavdyeityriyqyikendgtpkvkisltqttigkvsapkvaafssrgpsyiypgvLKPDIAAPGVTVLAAAPKA 437
Cdd:cd04852   236 -------------------------------------------------------------LKPDIAAPGVDILAAWTPE 254
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 438 FMD----AGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd04852   255 GADpgdaRGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTA 306
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
559-656 1.05e-36

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


:

Pssm-ID: 465493  Cd Length: 98  Bit Score: 132.32  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 559 DLNLPSIAIP--NLRTFQATTRTVTNVGQANARYKAFLYTPAGVEMTVDPPVLVFSKEKKVQSFKVTIKATGRPiQGDYS 636
Cdd:pfam17766   1 DLNYPSIAVSfeNLNGSVTVTRTVTNVGDGPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAP-SGEYV 79
                          90       100
                  ....*....|....*....|
gi 1443072518 637 FGSLVWHDGGiHWVRIPIAV 656
Cdd:pfam17766  80 FGSLTWSDGK-HTVRSPIVV 98
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
262-388 1.07e-15

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: 73.99  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 262 VITLGNNDKFVAQSFAISGKTS----SQFGEIQFYEREDCSAENIHNT-VKGKIVFCFFGtkfdSERDYYNITKATSEKG 336
Cdd:cd02120     1 VVTLGNGKTIVGQSLYPGNLKTyplvYKSANSGDVDASLCLPGSLDPSkVKGKIVLCDRG----GNTSRVAKGDAVKAAG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 337 GIGVILPKYNTDTLLGDTLLTlPIPLVAVDYEITYRIYQYIKENdGTPKVKI 388
Cdd:cd02120    77 GAGMILANDPTDGLDVVADAH-VLPAVHVDYEDGTAILSYINST-SNPTATI 126
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
47-485 9.13e-126

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: 374.63  E-value: 9.13e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  47 PNGLLAKAKYGEDIIIGVIDTGITPESPSFADDGYGPPPSKWKGVCQVGPSFKAKSCNRKLIGARWYID--DDTLRSMSK 124
Cdd:cd04852    19 GGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPFSCNNKLIGARYFSDgyDAYGGFNSD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 125 DEILSPRDVVGHGTHTASTAGGNIIHNASILGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILS 204
Cdd:cd04852    99 GEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGCFGSDILAAIDQAIADGVDVIS 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 205 LSLGG----PFEDP---GTLHVVAKGIPVVYSAGNDGPIAQTVENSSPWLLTVAAATmdrsfpvvitlgnndkfvaqsfa 277
Cdd:cd04852   179 YSIGGgspdPYEDPiaiAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST----------------------- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 278 isgktssqfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtllt 357
Cdd:cd04852       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 358 lpiplvavdyeityriyqyikendgtpkvkisltqttigkvsapkvaafssrgpsyiypgvLKPDIAAPGVTVLAAAPKA 437
Cdd:cd04852   236 -------------------------------------------------------------LKPDIAAPGVDILAAWTPE 254
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 438 FMD----AGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd04852   255 GADpgdaRGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTA 306
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
559-656 1.05e-36

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


Pssm-ID: 465493  Cd Length: 98  Bit Score: 132.32  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 559 DLNLPSIAIP--NLRTFQATTRTVTNVGQANARYKAFLYTPAGVEMTVDPPVLVFSKEKKVQSFKVTIKATGRPiQGDYS 636
Cdd:pfam17766   1 DLNYPSIAVSfeNLNGSVTVTRTVTNVGDGPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAP-SGEYV 79
                          90       100
                  ....*....|....*....|
gi 1443072518 637 FGSLVWHDGGiHWVRIPIAV 656
Cdd:pfam17766  80 FGSLTWSDGK-HTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
57-600 1.93e-31

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 127.91  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADdgygpppskwkgvcqvgpsfkakscnrKLIGARWYIDDDTlrsmskdeilSPRDVVGH 136
Cdd:COG1404   108 GAGVTVAVIDTGVDADHPDLAG---------------------------RVVGGYDFVDGDG----------DPSDDNGH 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 137 GTHTASTAGGNiihnasilGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILSLSLGGPFEDPGT 216
Cdd:COG1404   151 GTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNGADVINLSLGGPADGYSD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 217 L------HVVAKGIPVVYSAGNDGPIAQTVenSSPwlltvAAatmdrsFPVVITlgnndkfVAqsfaisgktssqfgeiq 290
Cdd:COG1404   223 AlaaavdYAVDKGVLVVAAAGNSGSDDATV--SYP-----AA------YPNVIA-------VG----------------- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 291 fyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlpiplvAVDyeit 370
Cdd:COG1404   266 -------------------------------------------------------------------------AVD---- 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 371 yriyqyikendgtpkvkisltqttigkvSAPKVAAFSSRGPsyiypgvlKPDIAAPGVTVLAAAPKAfmdagiPYRFDSG 450
Cdd:COG1404   269 ----------------------------ANGQLASFSNYGP--------KVDVAAPGVDILSTYPGG------GYATLSG 306
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 451 TSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTAltydnngmpiqangkVPKIADPFDYGAGVVNPNMAADPGLIYDIE 530
Cdd:COG1404   307 TSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTA---------------TPLGAPGPYYGYGLLADGAAGATSAGAGLA 371
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 531 PSDYFKFFNCMGGLGSADNCTTVKGSLADLNLPSIAIPNLRTFQATTRTVTNVGQANARYKAFLYTPAGV 600
Cdd:COG1404   372 AAAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATAAGLLAAAALSTLAAVAAAVVV 441
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
57-485 3.27e-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: 103.31  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFAD--DGYGPPPSKWKGvcqvgpsfkakscnrkligaRWYIDDDTLRSmskdeilSPRDVV 134
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGnlDNDPSDDPEASV--------------------DFNNEWDDPRD-------DIDDKN 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 135 GHGTHTASTAGGNIIHNASILglaagtvrGGAPRARVAMYKTCWNGvGCSAAGQLKAIDDAIHDGVDILSLSLGGPFEDP 214
Cdd:pfam00082  54 GHGTHVAGIIAAGGNNSIGVS--------GVAPGAKILGVRVFGDG-GGTDAITAQAISWAIPQGADVINMSWGSDKTDG 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 215 GT----------LHVVAKGIPVVYSAGNDGPIAQ---TVEN--SSPWLLTVAAATmdrsfpvvitlgnndkfvaqsfais 279
Cdd:pfam00082 125 GPgswsaavdqlGGAEAAGSLFVWAAGNGSPGGNngsSVGYpaQYKNVIAVGAVD------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 280 gktssqfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlp 359
Cdd:pfam00082     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 360 iplvavdyeityriyqyikendgtpkvkisltqttigKVSAPKVAAFSSRGPSyiYPGVLKPDIAAPGVTVLAAAPKAFM 439
Cdd:pfam00082 180 -------------------------------------EASEGNLASFSSYGPT--LDGRLKPDIVAPGGNITGGNISSTL 220
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 440 DAGIP------YRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:pfam00082 221 LTTTSdppnqgYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTA 272
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
262-388 1.07e-15

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: 73.99  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 262 VITLGNNDKFVAQSFAISGKTS----SQFGEIQFYEREDCSAENIHNT-VKGKIVFCFFGtkfdSERDYYNITKATSEKG 336
Cdd:cd02120     1 VVTLGNGKTIVGQSLYPGNLKTyplvYKSANSGDVDASLCLPGSLDPSkVKGKIVLCDRG----GNTSRVAKGDAVKAAG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 337 GIGVILPKYNTDTLLGDTLLTlPIPLVAVDYEITYRIYQYIKENdGTPKVKI 388
Cdd:cd02120    77 GAGMILANDPTDGLDVVADAH-VLPAVHVDYEDGTAILSYINST-SNPTATI 126
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
402-533 1.50e-07

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: 53.87  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 402 KVAAFSSRGPsyiypgvlKPDIAAPGVTVLAAAPkafmdAGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAI 481
Cdd:TIGR03921 189 TPSSFSLPGP--------WVDLAAPGENIVSLSP-----GGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRI 255
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 482 MTTAltyDNNGmpiqANGKVPkiadpfDYGAGVVNPnMAAdpgLIYDIEPSD 533
Cdd:TIGR03921 256 EATA---DHPA----RGGRDD------YVGYGVVDP-VAA---LTGELPPED 290
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
407-464 4.50e-05

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 46.70  E-value: 4.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443072518  407 SSRGPSYIypGVLKPDIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAV 464
Cdd:NF040809   994 SSRGPTIR--NIQKPDIVAPGVNIIAPYP------GNTYATITGTSAAAAHVSGVAAL 1043
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
403-499 3.36e-04

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: 44.00  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  403 VAAFSSRGPsyIYPGVLKPDIAAPGVTVLAAAPKAFMDAGipyrfdSGTSMSCPHVSGIIAVLKslhpQWS--------- 473
Cdd:NF040809   418 VSVFSGEGD--IENGIYKPDLLAPGENIVSYLPGGTTGAL------TGTSMATPHVTGVCSLLM----QWGivegndlfl 485
                           90       100
                   ....*....|....*....|....*..
gi 1443072518  474 -PAALKSAIMTTALTYDNNGMPIQANG 499
Cdd:NF040809   486 ySQKLKALLLQNARRSPNRTYPNNSSG 512
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
423-473 5.54e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 43.03  E-value: 5.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1443072518 423 IAAPGVTVLAAAPKAfmdagiPYRFDSGTSMSCPHVSGIIAVLKSLHPQWS 473
Cdd:PTZ00262  534 LAAPGTNIYSTFPKN------SYRKLNGTSMAAPHVAAIASLILSINPSLS 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 ...
47-485 9.13e-126

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: 374.63  E-value: 9.13e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  47 PNGLLAKAKYGEDIIIGVIDTGITPESPSFADDGYGPPPSKWKGVCQVGPSFKAKSCNRKLIGARWYID--DDTLRSMSK 124
Cdd:cd04852    19 GGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPFSCNNKLIGARYFSDgyDAYGGFNSD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 125 DEILSPRDVVGHGTHTASTAGGNIIHNASILGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILS 204
Cdd:cd04852    99 GEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGCFGSDILAAIDQAIADGVDVIS 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 205 LSLGG----PFEDP---GTLHVVAKGIPVVYSAGNDGPIAQTVENSSPWLLTVAAATmdrsfpvvitlgnndkfvaqsfa 277
Cdd:cd04852   179 YSIGGgspdPYEDPiaiAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAST----------------------- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 278 isgktssqfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtllt 357
Cdd:cd04852       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 358 lpiplvavdyeityriyqyikendgtpkvkisltqttigkvsapkvaafssrgpsyiypgvLKPDIAAPGVTVLAAAPKA 437
Cdd:cd04852   236 -------------------------------------------------------------LKPDIAAPGVDILAAWTPE 254
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 438 FMD----AGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd04852   255 GADpgdaRGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTA 306
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
57-520 1.27e-42

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: 155.95  E-value: 1.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADDGYGPPpskwkgvcqvgpsfkakscnrKLIGARWYIDDD-----TLRSMSKDEILSPR 131
Cdd:cd07474     1 GKGVKVAVIDTGIDYTHPDLGGPGFPND---------------------KVKGGYDFVDDDydpmdTRPYPSPLGDASAG 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 132 DVVGHGTHTASTAGGNiihnasilGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILSLSLGGPF 211
Cdd:cd07474    60 DATGHGTHVAGIIAGN--------GVNVGTIKGVAPKADLYAYKVLGPGGSGTTDVIIAAIEQAVDDGMDVINLSLGSSV 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 212 EDPGTLHVVA------KGIPVVYSAGNDGPIAQTVEN--SSPWLLTVAAATMDRSFPvvitlgnndkfvaqsfaisgkts 283
Cdd:cd07474   132 NGPDDPDAIAinnavkAGVVVVAAAGNSGPAPYTIGSpaTAPSAITVGASTVADVAE----------------------- 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 284 sqfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlpiplv 363
Cdd:cd07474       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 364 avdyeityriyqyikendgtpkvkisltqttigkvsAPKVAAFSSRGPSyIYPGVLKPDIAAPGVTVLAAAPKafmdAGI 443
Cdd:cd07474   189 ------------------------------------ADTVGPSSSRGPP-TSDSAIKPDIVAPGVDIMSTAPG----SGT 227
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443072518 444 PYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTALTYDNNGmpiqangkvPKIADPFDYGAGVVNPNMA 520
Cdd:cd07474   228 GYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSD---------GVVYPVSRQGAGRVDALRA 295
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
559-656 1.05e-36

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


Pssm-ID: 465493  Cd Length: 98  Bit Score: 132.32  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 559 DLNLPSIAIP--NLRTFQATTRTVTNVGQANARYKAFLYTPAGVEMTVDPPVLVFSKEKKVQSFKVTIKATGRPiQGDYS 636
Cdd:pfam17766   1 DLNYPSIAVSfeNLNGSVTVTRTVTNVGDGPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAP-SGEYV 79
                          90       100
                  ....*....|....*....|
gi 1443072518 637 FGSLVWHDGGiHWVRIPIAV 656
Cdd:pfam17766  80 FGSLTWSDGK-HTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
57-600 1.93e-31

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 127.91  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADdgygpppskwkgvcqvgpsfkakscnrKLIGARWYIDDDTlrsmskdeilSPRDVVGH 136
Cdd:COG1404   108 GAGVTVAVIDTGVDADHPDLAG---------------------------RVVGGYDFVDGDG----------DPSDDNGH 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 137 GTHTASTAGGNiihnasilGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILSLSLGGPFEDPGT 216
Cdd:COG1404   151 GTHVAGIIAAN--------GNNGGGVAGVAPGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNGADVINLSLGGPADGYSD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 217 L------HVVAKGIPVVYSAGNDGPIAQTVenSSPwlltvAAatmdrsFPVVITlgnndkfVAqsfaisgktssqfgeiq 290
Cdd:COG1404   223 AlaaavdYAVDKGVLVVAAAGNSGSDDATV--SYP-----AA------YPNVIA-------VG----------------- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 291 fyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlpiplvAVDyeit 370
Cdd:COG1404   266 -------------------------------------------------------------------------AVD---- 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 371 yriyqyikendgtpkvkisltqttigkvSAPKVAAFSSRGPsyiypgvlKPDIAAPGVTVLAAAPKAfmdagiPYRFDSG 450
Cdd:COG1404   269 ----------------------------ANGQLASFSNYGP--------KVDVAAPGVDILSTYPGG------GYATLSG 306
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 451 TSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTAltydnngmpiqangkVPKIADPFDYGAGVVNPNMAADPGLIYDIE 530
Cdd:COG1404   307 TSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTA---------------TPLGAPGPYYGYGLLADGAAGATSAGAGLA 371
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 531 PSDYFKFFNCMGGLGSADNCTTVKGSLADLNLPSIAIPNLRTFQATTRTVTNVGQANARYKAFLYTPAGV 600
Cdd:COG1404   372 AAAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATAAGLLAAAALSTLAAVAAAVVV 441
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
57-485 3.27e-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: 103.31  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFAD--DGYGPPPSKWKGvcqvgpsfkakscnrkligaRWYIDDDTLRSmskdeilSPRDVV 134
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGnlDNDPSDDPEASV--------------------DFNNEWDDPRD-------DIDDKN 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 135 GHGTHTASTAGGNIIHNASILglaagtvrGGAPRARVAMYKTCWNGvGCSAAGQLKAIDDAIHDGVDILSLSLGGPFEDP 214
Cdd:pfam00082  54 GHGTHVAGIIAAGGNNSIGVS--------GVAPGAKILGVRVFGDG-GGTDAITAQAISWAIPQGADVINMSWGSDKTDG 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 215 GT----------LHVVAKGIPVVYSAGNDGPIAQ---TVEN--SSPWLLTVAAATmdrsfpvvitlgnndkfvaqsfais 279
Cdd:pfam00082 125 GPgswsaavdqlGGAEAAGSLFVWAAGNGSPGGNngsSVGYpaQYKNVIAVGAVD------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 280 gktssqfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlp 359
Cdd:pfam00082     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 360 iplvavdyeityriyqyikendgtpkvkisltqttigKVSAPKVAAFSSRGPSyiYPGVLKPDIAAPGVTVLAAAPKAFM 439
Cdd:pfam00082 180 -------------------------------------EASEGNLASFSSYGPT--LDGRLKPDIVAPGGNITGGNISSTL 220
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 440 DAGIP------YRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:pfam00082 221 LTTTSdppnqgYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTA 272
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
57-485 4.97e-24

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: 101.89  E-value: 4.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADDGygpppskwkgvcqvgpsfkakscnrkligARWYIDDDTLRSMSkdeilSPRDVVGH 136
Cdd:cd07487     1 GKGITVAVLDTGIDAPHPDFDGRI-----------------------------IRFADFVNTVNGRT-----TPYDDNGH 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 137 GTHTASTAGGNiihnasiLGLAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAI----HDGVDILSLSLGGPF- 211
Cdd:cd07487    47 GTHVAGIIAGS-------GRASNGKYKGVAPGANLVGVKVLDDSGSGSESDIIAGIDWVVenneKYNIRVVNLSLGAPPd 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 212 ----EDP---GTLHVVAKGIPVVYSAGNDGPIAQTVenSSPwlltvAAAtmdrsfPVVITLGnndkfvaqsfaisgktss 284
Cdd:cd07487   120 psygEDPlcqAVERLWDAGIVVVVAAGNSGPGPGTI--TSP-----GNS------PKVITVG------------------ 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 285 qfgeiqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlpiplvA 364
Cdd:cd07487   169 -------------------------------------------------------------------------------A 169
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 365 VDYEITYRIYqyikendgtpkvkisltqttigkvsapkVAAFSSRGPsyIYPGVLKPDIAAPGVTVLAAAPKAFMDAGIP 444
Cdd:cd07487   170 VDDNGPHDDG----------------------------ISYFSSRGP--TGDGRIKPDVVAPGENIVSCRSPGGNPGAGV 219
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1443072518 445 ---YRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd07487   220 gsgYFEMSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDTA 263
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
60-484 9.15e-20

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: 89.18  E-value: 9.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  60 IIIGVIDTGITPESPSFADDGYGPPPSKWKGVCQVGPSfkakscnrkligarwyidddtlrsmskdeilSPRDVVGHGTH 139
Cdd:cd00306     1 VTVAVIDTGVDPDHPDLDGLFGGGDGGNDDDDNENGPT-------------------------------DPDDGNGHGTH 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 140 TASTAGGNIihnasilglAAGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHD-GVDILSLSLGGPFEDPGTLH 218
Cdd:cd00306    50 VAGIIAASA---------NNGGGVGVAPGAKLIPVKVLDGDGSGSSSDIAAAIDYAAADqGADVINLSLGGPGSPPSSAL 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 219 -------VVAKGIPVVYSAGNDGPIAQTVEN---SSPWLLTVAAATmdrsfpvvitlgnndkfvaqsfaisgktssqfge 288
Cdd:cd00306   121 seaidyaLAKLGVLVVAAAGNDGPDGGTNIGypaASPNVIAVGAVD---------------------------------- 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 289 iqfyeredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlpiplvavdye 368
Cdd:cd00306       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 369 ityriyqyikeNDGTPkvkisltqttigkvsapkVAAFSSRGPsyiypgvlKPDIAAPGVTVLAAAPkafmDAGIPYRFD 448
Cdd:cd00306   167 -----------RDGTP------------------ASPSSNGGA--------GVDIAAPGGDILSSPT----TGGGGYATL 205
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1443072518 449 SGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTT 484
Cdd:cd00306   206 SGTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
50-522 1.00e-18

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


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 87.66  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  50 LLAKAKYGEDIIIGVIDTGITPESPSFaddgygpppskwkGVCqVGPSFKakscnrkLIGARWYIDDDTLRSMSKDEILS 129
Cdd:cd07489     5 LHAEGITGKGVKVAVVDTGIDYTHPAL-------------GGC-FGPGCK-------VAGGYDFVGDDYDGTNPPVPDDD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 130 PRDVVGHGTHTASTAGGNiihnASILGLAagtvrGGAPRARVAMYKTcwngVGCSAAGQ----LKAIDDAIHDGVDILSL 205
Cdd:cd07489    64 PMDCQGHGTHVAGIIAAN----PNAYGFT-----GVAPEATLGAYRV----FGCSGSTTedtiIAAFLRAYEDGADVITA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 206 SLGGPF---EDPGTLHV---VAKGIPVVYSAGNDGpiaqtvensspwlltvaaatmdrsfpvvitlgnndkfvaqsfais 279
Cdd:cd07489   131 SLGGPSgwsEDPWAVVAsriVDAGVVVTIAAGNDG--------------------------------------------- 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 280 gktssQFGeiQFYeredcsaenihntvkgkivfcffgtkfdserdyynitkATSEKGGIGVIlpkyntdtllgdtlltlp 359
Cdd:cd07489   166 -----ERG--PFY--------------------------------------ASSPASGRGVI------------------ 182
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 360 iplvavdyeityriyqyikendgtpkvkisltqtTIGKVSApkvaAFSSRGPSYIYpgVLKPDIAAPGVTVLAAAPkafm 439
Cdd:cd07489   183 ----------------------------------AVASVDS----YFSSWGPTNEL--YLKPDVAAPGGNILSTYP---- 218
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 440 DAGIPYRFDSGTSMSCPHVSGIIAVLKSL-HPQWSPAALKSAIMTTALTYDNNGmpiqANGKVPKIADPFDYGAGVVNPN 518
Cdd:cd07489   219 LAGGGYAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKPLPWSD----GTSALPDLAPVAQQGAGLVNAY 294

                  ....
gi 1443072518 519 MAAD 522
Cdd:cd07489   295 KALY 298
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
394-485 1.52e-18

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: 85.68  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 394 TIGKVS-APKVAAFSSRGPSYIYPG---------VLKPDIAAPGVTVLAAAPKAFMDAGipYRFDSGTSMSCPHVSGIIA 463
Cdd:cd07490   154 SVGAVDrDDEDAWFSSFGSSGASLVsapdsppdeYTKPDVAAPGVDVYSARQGANGDGQ--YTRLSGTSMAAPHVAGVAA 231
                          90       100
                  ....*....|....*....|..
gi 1443072518 464 VLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd07490   232 LLAAAHPDLSPEQIKDALTETA 253
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
57-485 5.65e-18

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: 85.78  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADDgygpPPSKWKgvcqVGPSFKAKSCNRKLIGARW----------YIDDDtlrsmskDE 126
Cdd:cd07475    10 GEGMVVAVIDSGVDPTHDAFRLD----DDSKAK----YSEEFEAKKKKAGIGYGKYynekvpfaynYADNN-------DD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 127 ILSPRDVVGHGTHTASTAGGNIIHNASILGlaagtVRGGAPRARVAMYK--TCWNGVGCSAAGQLKAIDDAIHDGVDILS 204
Cdd:cd07475    75 ILDEDDGSSHGMHVAGIVAGNGDEEDNGEG-----IKGVAPEAQLLAMKvfSNPEGGSTYDDAYAKAIEDAVKLGADVIN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 205 LSLGGP--FEDPGTL------HVVAKGIPVVYSAGNDGpiaqtvENSSPWLLTVAAATMDRSfpvviTLGNNdkfvaqsf 276
Cdd:cd07475   150 MSLGSTagFVDLDDPeqqaikRAREAGVVVVVAAGNDG------NSGSGTSKPLATNNPDTG-----TVGSP-------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 277 aisgktssqfgeiqfyeredcsaenihntvkgkivfcffGTKFDSerdyynITKATSEKggigvilpkyntdtllgdtll 356
Cdd:cd07475   211 ---------------------------------------ATADDV------LTVASANK--------------------- 224
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 357 tlpiplvavdyeityriyqyikendgtpkvkisltqtTIGKVSAPKVAAFSSRGPSyiyP-GVLKPDIAAPGVTVLAAAP 435
Cdd:cd07475   225 -------------------------------------KVPNPNGGQMSGFSSWGPT---PdLDLKPDITAPGGNIYSTVN 264
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443072518 436 KAfmdagiPYRFDSGTSMSCPHVSGIIAV----LKSLHPQWSPAAL----KSAIMTTA 485
Cdd:cd07475   265 DN------TYGYMSGTSMASPHVAGASALvkqrLKEKYPKLSGEELvdlvKNLLMNTA 316
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
262-388 1.07e-15

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: 73.99  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 262 VITLGNNDKFVAQSFAISGKTS----SQFGEIQFYEREDCSAENIHNT-VKGKIVFCFFGtkfdSERDYYNITKATSEKG 336
Cdd:cd02120     1 VVTLGNGKTIVGQSLYPGNLKTyplvYKSANSGDVDASLCLPGSLDPSkVKGKIVLCDRG----GNTSRVAKGDAVKAAG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 337 GIGVILPKYNTDTLLGDTLLTlPIPLVAVDYEITYRIYQYIKENdGTPKVKI 388
Cdd:cd02120    77 GAGMILANDPTDGLDVVADAH-VLPAVHVDYEDGTAILSYINST-SNPTATI 126
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
59-484 1.38e-15

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: 76.42  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  59 DIIIGVIDTGITPESPSFADDGYGpppskwkGVCQVGPsfkakscnrkliGARWYIDDDtlrsmskdeilsprdvvGHGT 138
Cdd:cd07477     1 GVKVAVIDTGIDSSHPDLKLNIVG-------GANFTGD------------DNNDYQDGN-----------------GHGT 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 139 HTASTaggniihnasILGLAAGT-VRGGAPRARVAMYKTC-WNGVGcSAAGQLKAIDDAIHDGVDILSLSLGGPFEDPGT 216
Cdd:cd07477    45 HVAGI----------IAALDNGVgVVGVAPEADLYAVKVLnDDGSG-TYSDIIAGIEWAIENGMDIINMSLGGPSDSPAL 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 217 LHVV----AKGIPVVYSAGNDGpiaqtveNSSPWLLTVAaatmdrSFPVVITLGnndkfvaqsfaisgktssqfgeiqfy 292
Cdd:cd07477   114 REAIkkayAAGILVVAAAGNSG-------NGDSSYDYPA------KYPSVIAVG-------------------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 293 eredcsaenihntvkgkivfcffgtkfdserdyynitkatsekggigvilpkyntdtllgdtlltlpiplvAVDyeityr 372
Cdd:cd07477   155 -----------------------------------------------------------------------AVD------ 157
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 373 iyqyikENDgtpkvkisltqttigkvsapKVAAFSSRGPsyiypgvlKPDIAAPGVTVLAAAPkafmdaGIPYRFDSGTS 452
Cdd:cd07477   158 ------SNN--------------------NRASFSSTGP--------EVELAAPGVDILSTYP------NNDYAYLSGTS 197
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1443072518 453 MSCPHVSGIIAVLKSLHPQWSPAALKSAIMTT 484
Cdd:cd07477   198 MATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
404-485 1.64e-14

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: 73.77  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 404 AAFSSRGPSYIypgvlkpDIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMT 483
Cdd:cd07473   190 ASFSNYGKKTV-------DLAAPGVDILSTSP------GGGYGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILS 256

                  ..
gi 1443072518 484 TA 485
Cdd:cd07473   257 SA 258
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
402-473 9.47e-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: 71.64  E-value: 9.47e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 402 KVAAFSSRGPSYiyPGVLKPDIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWS 473
Cdd:cd07481   186 VLADFSSRGPST--YGRIKPDISAPGVNIRSAVP------GGGYGSSSGTSMAAPHVAGVAALLWSANPSLI 249
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
399-485 1.54e-12

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: 68.51  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 399 SAPKVAAFSSRGPSYiyPGVLKPDIAAPGVTVLAAAPKAFMDAGIP---YRFDSGTSMSCPHVSGIIAVL---------- 465
Cdd:cd04842   197 NSDTVASFSSRGPTY--DGRIKPDLVAPGTGILSARSGGGGIGDTSdsaYTSKSGTSMATPLVAGAAALLrqyfvdgyyp 274
                          90       100
                  ....*....|....*....|
gi 1443072518 466 KSLHPqwSPAALKSAIMTTA 485
Cdd:cd04842   275 TKFNP--SAALLKALLINSA 292
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
56-465 3.25e-12

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: 69.18  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  56 YGEDIIIGVIDTGITPESPSFAD-DG-------------YGPPPSKwkgvcQVGPSFkakscnrkligARWYIDDDTLRS 121
Cdd:cd07478     2 TGKGVLVGIIDTGIDYLHPEFRNeDGttrilyiwdqtipGGPPPGG-----YYGGGE-----------YTEEIINAALAS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 122 MSKDEILSPRDVVGHGTHTASTAGGNiihnasilGLAAGTVRGGAPRARVAMYK------TCWNGVGCSAAGQLKAIDDA 195
Cdd:cd07478    66 DNPYDIVPSRDENGHGTHVAGIAAGN--------GDNNPDFKGVAPEAELIVVKlkqakkYLREFYEDVPFYQETDIMLA 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 196 I--------------------------HDGVDILSL---SLGGPfedpgtlhvvaKGIPVVYSAGNDGpIAQTVENSspw 246
Cdd:cd07478   138 IkylydkalelnkplvinislgtnfgsHDGTSLLERyidAISRL-----------RGIAVVVGAGNEG-NTQHHHSG--- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 247 lltvaaatmdrsfpvviTLGNNDKFVAQSFAISGKTSSQFGEI--QFYER-----EDCSAENIHN-----TVKGKIVFCF 314
Cdd:cd07478   203 -----------------GIVPNGETKTVELNVGEGEKGFNLEIwgDFPDRfsvsiISPSGESSGRinpgiGGSESYKFVF 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 315 FGTKFdsERDYYNITkatsEKGGIGVILPKYNTDTLLGDTLLTLPIPLVAVDYEITYRIYQYIKEN--------DGTpkV 386
Cdd:cd07478   266 EGTTV--YVYYYLPE----PYTGDQLIFIRFKNIKPGIWKIRLTGVSITDGRFDAWLPSRGLLSENtrflepdpYTT--L 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 387 KI-SLTQTTIgKVSA-----PKVAAFSSRGpsYIYPGVLKPDIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSG 460
Cdd:cd07478   338 TIpGTARSVI-TVGAynqnnNSIAIFSGRG--PTRDGRIKPDIAAPGVNILTASP------GGGYTTRSGTSVAAAIVAG 408

                  ....*
gi 1443072518 461 IIAVL 465
Cdd:cd07478   409 ACALL 413
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
422-485 5.77e-12

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


Pssm-ID: 173790 [Multi-domain]  Cd Length: 255  Bit Score: 66.39  E-value: 5.77e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443072518 422 DIAAPGVTVLAAAPKAfmDAGipYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd04077   194 DIFAPGVDILSAWIGS--DTA--TATLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
57-234 9.85e-12

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: 65.81  E-value: 9.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADDgygpppskwkgvcqvgpsfkakscnrkligarwYIDDDTLRSMSKDEILSPRDVVGH 136
Cdd:cd04848     2 GAGVKVGVIDSGIDLSHPEFAGR---------------------------------VSEASYYVAVNDAGYASNGDGDSH 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 137 GTHTASTAGGNIIHNASIlglaagtvrGGAPRARVAMYKTCWN-GVGCSAAGQLKAIDDAIHDGVDILSLSLGGPFEDPG 215
Cdd:cd04848    49 GTHVAGVIAAARDGGGMH---------GVAPDATLYSARASASaGSTFSDADIAAAYDFLAASGVRIINNSWGGNPAIDT 119
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1443072518 216 T-------------------LHVVAKGIPVVYSAGNDG 234
Cdd:cd04848   120 VsttykgsaatqgntllaalARAANAGGLFVFAAGNDG 157
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
403-471 2.33e-10

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: 61.73  E-value: 2.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 403 VAAFSSRGpSYIypgvlkpDIAAPGV-TVLAAAPKAFMDAGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQ 471
Cdd:cd07485   198 KASFSNYG-RWV-------DIAAPGVgTILSTVPKLDGDGGGNYEYLSGTSMAAPHVSGVAALVLSKFPD 259
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
394-485 5.24e-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: 60.40  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 394 TIGKVSAPK-VAAFSSRGPSYiyPGVLKPDIAAPGVtvlaaapKAFMDAGI-PYRFDSGTSMSCPHVSGIIAVLKSLHPQ 471
Cdd:cd07493   176 SVGAVDANGnKASFSSIGPTA--DGRLKPDVMALGT-------GIYVINGDgNITYANGTSFSCPLIAGLIACLWQAHPN 246
                          90
                  ....*....|....
gi 1443072518 472 WSPAALKSAIMTTA 485
Cdd:cd07493   247 WTNLQIKEAILKSA 260
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
60-270 8.03e-10

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: 60.46  E-value: 8.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  60 IIIGVIDTGITPESPSFADdgygpppskwkgvcQVGPSFKAKScnrkligarwyiDDDTLRSMSKDEILSPRDVV---GH 136
Cdd:cd07482     2 VTVAVIDSGIDPDHPDLKN--------------SISSYSKNLV------------PKGGYDGKEAGETGDINDIVdklGH 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 137 GTHTASTAGGNiihnasilglaaGTVRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILSLSLGG------- 209
Cdd:cd07482    56 GTAVAGQIAAN------------GNIKGVAPGIGIVSYRVFGSCGSAESSWIIKAIIDAADDGVDVINLSLGGyliigge 123
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443072518 210 PFEDPGTLHVVA--------KGIPVVYSAGNDG-----PIAQTVENSSPWLLTVAAATMD--RSFPVVITLGNNDK 270
Cdd:cd07482   124 YEDDDVEYNAYKkainyaksKGSIVVAAAGNDGldvsnKQELLDFLSSGDDFSVNGEVYDvpASLPNVITVSATDN 199
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
57-257 2.81e-09

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: 58.43  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  57 GEDIIIGVIDTGITPESPSFADDgygpppskwkgvcqvgpsfkakscnrKLIGARWYIDDDTlrsmskdeilSPRDVVGH 136
Cdd:cd07484    27 GSGVTVAVVDTGVDPTHPDLLKV--------------------------KFVLGYDFVDNDS----------DAMDDNGH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 137 GTHTASTAGGNIIHNASILGLaagtvrggAPRARVAMYKTcwngVGCSAAGQLKAIDDAIH----DGVDILSLSLGGPFE 212
Cdd:cd07484    71 GTHVAGIIAAATNNGTGVAGV--------APKAKIMPVKV----LDANGSGSLADIANGIRyaadKGAKVINLSLGGGLG 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1443072518 213 DPGTLHVVA----KGIPVVYSAGNDGPIAQTVENSSPWLLTVAAATMDR 257
Cdd:cd07484   139 STALQEAINyawnKGVVVVAAAGNEGVSSVSYPAAYPGAIAVAATDQDD 187
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
421-515 3.94e-09

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: 58.54  E-value: 3.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 421 PDIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAVlkslhpqWSPAALKSAIMTTALTYDNNGMPIQANGK 500
Cdd:cd07480   213 VDIAAPGVDIVSAAP------GGGYRSMSGTSMATPHVAGVAAL-------WAEALPKAGGRALAALLQARLTAARTTQF 279
                          90
                  ....*....|....*
gi 1443072518 501 VPKIADPfDYGAGVV 515
Cdd:cd07480   280 APGLDLP-DRGVGLG 293
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
407-520 8.29e-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: 57.30  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 407 SSRGPSYIYPgvLKPDIAAP-GVTVLAAApkafmDAGIPYRFdSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd05562   179 GIRLPTPEVR--QKPDVTAPdGVNGTVDG-----DGDGPPNF-FGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTA 250
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1443072518 486 LTYDNNGmpiqangkvpkiaDPFDYGAGVVNPNMA 520
Cdd:cd05562   251 LDMGEPG-------------YDNASGSGLVDADRA 272
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
422-485 1.89e-08

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: 55.76  E-value: 1.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443072518 422 DIAAPGVTVLAAAPKAfmdagiPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIMTTA 485
Cdd:cd05561   168 DFAAPGVDVWVAAPGG------GYRYVSGTSFAAPFVTAALALLLQASPLAPDDARARLAATAK 225
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
402-533 1.50e-07

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: 53.87  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 402 KVAAFSSRGPsyiypgvlKPDIAAPGVTVLAAAPkafmdAGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAI 481
Cdd:TIGR03921 189 TPSSFSLPGP--------WVDLAAPGENIVSLSP-----GGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRI 255
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443072518 482 MTTAltyDNNGmpiqANGKVPkiadpfDYGAGVVNPnMAAdpgLIYDIEPSD 533
Cdd:TIGR03921 256 EATA---DHPA----RGGRDD------YVGYGVVDP-VAA---LTGELPPED 290
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
422-485 1.89e-07

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: 53.03  E-value: 1.89e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443072518 422 DIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAVLKSLHPqWSPAALKSAIMTTA 485
Cdd:cd07484   200 DVSAPGGGILSTTP------DGDYAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTA 256
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
403-486 5.19e-07

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


Pssm-ID: 173809 [Multi-domain]  Cd Length: 291  Bit Score: 51.98  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 403 VAAFSSRGPSYIypgvlkpDIAAPGVTVLAAAPKAfmdagiPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSAIM 482
Cdd:cd07483   221 VANFSNYGKKNV-------DVFAPGERIYSTTPDN------EYETDSGTSMAAPVVSGVAALIWSYYPNLTAKEVKQIIL 287

                  ....
gi 1443072518 483 TTAL 486
Cdd:cd07483   288 ESGV 291
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
404-484 8.07e-07

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


Pssm-ID: 173820 [Multi-domain]  Cd Length: 285  Bit Score: 51.14  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 404 AAFSSRGPSYiypgvlkpDIAAPGVTVLA---------AAPKAFMDAGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSP 474
Cdd:cd07496   204 ASYSNYGPAV--------DVSAPGGDCASdvngdgypdSNTGTTSPGGSTYGFLQGTSMAAPHVAGVAALMKSVNPSLTP 275
                          90
                  ....*....|
gi 1443072518 475 AALKSAIMTT 484
Cdd:cd07496   276 AQIESLLQST 285
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
402-485 8.74e-06

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: 47.83  E-value: 8.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 402 KVAAFSSRGPS-----YIYpGVLKPDIAAPGVTVLAAApkafMDAGIpyRFDSGTSMSCPHVSGIIAVLKSLHPQ----W 472
Cdd:cd07479   165 NIARFSSRGMTtwelpGGY-GRVKPDIVTYGSGVYGSK----LKGGC--RALSGTSVASPVVAGAVALLLSTVPEkrdlI 237
                          90
                  ....*....|...
gi 1443072518 473 SPAALKSAIMTTA 485
Cdd:cd07479   238 NPASMKQALIESA 250
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
423-480 1.36e-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: 46.95  E-value: 1.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443072518 423 IAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAVLKSLHPQWSPAALKSA 480
Cdd:cd07492   165 FSADGVDIIAPAP------HGRYLTVSGNSFAAPHVTGMVALLLSEKPDIDANDLKRL 216
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
59-234 2.10e-05

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: 46.90  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  59 DIIIGVIDTGITPE----------------SPSFADDGYG-----PPPSKWKGVCQVGPSFkakSCNRKLIGARWyiddd 117
Cdd:cd07496     1 GVVVAVLDTGVLFHhpdlagvllpgydfisDPAIANDGDGrdsdpTDPGDWVTGDDVPPGG---FCGSGVSPSSW----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 118 tlrsmskdeilsprdvvgHGTHTASTAGGNiiHNASIlGLAagtvrGGAPRARVAMYKT---CwngvgcsaAGQLKAIDD 194
Cdd:cd07496    73 ------------------HGTHVAGTIAAV--TNNGV-GVA-----GVAWGARILPVRVlgkC--------GGTLSDIVD 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1443072518 195 AIH-------DGV-------DILSLSLGGPFEDPGTLH-----VVAKGIPVVYSAGNDG 234
Cdd:cd07496   119 GMRwaaglpvPGVpvnpnpaKVINLSLGGDGACSATMQnaindVRARGVLVVVAAGNEG 177
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
132-242 2.41e-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: 46.29  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 132 DVVGHGTHTAstaggniihnasilGLAAGT---VRGGAPRARVAMYKTCWNGVGCSAAGQLKAIDDAIHDGVDILSLSLG 208
Cdd:cd07479    43 DGLGHGTFVA--------------GVIASSreqCLGFAPDAEIYIFRVFTNNQVSYTSWFLDAFNYAILTKIDVLNLSIG 108
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1443072518 209 GP-FED----PGTLHVVAKGIPVVYSAGNDGPIAQTVEN 242
Cdd:cd07479   109 GPdFMDkpfvDKVWELTANNIIMVSAIGNDGPLYGTLNN 147
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
403-485 2.47e-05

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


Pssm-ID: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 46.69  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 403 VAAFSSRGPSYIypGVLKPDIAAPGVTVLAAAP--KAFMDAGIPYRFD--SGTSMSCPHVSGIIA-VLKSLH-----PQW 472
Cdd:cd07497   221 VVSWSSRGPSIA--GDPKPDLAAIGAFAWAPGRvlDSGGALDGNEAFDlfGGTSMATPMTAGSAAlVISALKekegvGEY 298
                          90
                  ....*....|...
gi 1443072518 473 SPAALKSAIMTTA 485
Cdd:cd07497   299 DPFLVRTILMSTA 311
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
407-464 4.50e-05

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 46.70  E-value: 4.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443072518  407 SSRGPSYIypGVLKPDIAAPGVTVLAAAPkafmdaGIPYRFDSGTSMSCPHVSGIIAV 464
Cdd:NF040809   994 SSRGPTIR--NIQKPDIVAPGVNIIAPYP------GNTYATITGTSAAAAHVSGVAAL 1043
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
380-484 6.03e-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: 45.03  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 380 NDGTPKVKISLTQTTIGKVSAP----KVAAFSSRGPsYIypgvlkpDIAAPGV---TVLAAAPKAFMDAGIPYRFDSGTS 452
Cdd:cd07498   139 NSGRSVSSGYAANPSVIAVAATdsndARASYSNYGN-YV-------DLVAPGVgiwTTGTGRGSAGDYPGGGYGSFSGTS 210
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1443072518 453 MSCPHVSGIIAVLKSLHPQWSPAALKSAIMTT 484
Cdd:cd07498   211 FASPVAAGVAALILSANPNLTPAEVEDILTST 242
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
407-485 1.83e-04

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


Pssm-ID: 173796 [Multi-domain]  Cd Length: 412  Bit Score: 44.20  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 407 SSRGPSYiyPGVLKPDIAAPG-----VTVLAAAPKAFMDagipyrfdsGTSMSCPHVSGIIAVLKS-LHPQ---WSPAAL 477
Cdd:cd04857   333 SSRGPTA--DGALGVSISAPGgaiasVPNWTLQGSQLMN---------GTSMSSPNACGGIALLLSgLKAEgipYTPYSV 401

                  ....*...
gi 1443072518 478 KSAIMTTA 485
Cdd:cd04857   402 RRALENTA 409
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
149-238 2.74e-04

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


Pssm-ID: 173797 [Multi-domain]  Cd Length: 239  Bit Score: 43.05  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 149 IHNASILGLAAGTVRGGAPRARVAmyKTCWNGVGCSAAGQ--------LKAIDDAIHDGVDILSLSLGGPfeDPGTL--- 217
Cdd:cd05561    37 AHGTAVASLLAGAGAQRPGLLPGA--DLYGADVFGRAGGGegasalalARALDWLAEQGVRVVNISLAGP--PNALLaaa 112
                          90       100
                  ....*....|....*....|...
gi 1443072518 218 --HVVAKGIPVVYSAGNDGPIAQ 238
Cdd:cd05561   113 vaAAAARGMVLVAAAGNDGPAAP 135
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
403-499 3.36e-04

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: 44.00  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  403 VAAFSSRGPsyIYPGVLKPDIAAPGVTVLAAAPKAFMDAGipyrfdSGTSMSCPHVSGIIAVLKslhpQWS--------- 473
Cdd:NF040809   418 VSVFSGEGD--IENGIYKPDLLAPGENIVSYLPGGTTGAL------TGTSMATPHVTGVCSLLM----QWGivegndlfl 485
                           90       100
                   ....*....|....*....|....*..
gi 1443072518  474 -PAALKSAIMTTALTYDNNGMPIQANG 499
Cdd:NF040809   486 ySQKLKALLLQNARRSPNRTYPNNSSG 512
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
423-473 5.54e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 43.03  E-value: 5.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1443072518 423 IAAPGVTVLAAAPKAfmdagiPYRFDSGTSMSCPHVSGIIAVLKSLHPQWS 473
Cdd:PTZ00262  534 LAAPGTNIYSTFPKN------SYRKLNGTSMAAPHVAAIASLILSINPSLS 578
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
60-254 5.99e-03

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: 38.86  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518  60 IIIGVIDTGITPESPSFAddgygpppskwkGVCQVGPSFKAkscnrkligarwyIDDDTlrsmskdeilSPRDVVGHGTH 139
Cdd:cd07498     1 VVVAIIDTGVDLNHPDLS------------GKPKLVPGWNF-------------VSNND----------PTSDIDGHGTA 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 140 TASTAGGNiiHNASiLGLAagtvrGGAPRARVamykTCWNGVGCSAAGQLKAIDDAIH----DGVDILSLSLGGPFEDPG 215
Cdd:cd07498    46 CAGVAAAV--GNNG-LGVA-----GVAPGAKL----MPVRIADSLGYAYWSDIAQAITwaadNGADVISNSWGGSDSTES 113
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1443072518 216 TLHVV---------AKGIPVVYSAGNDGPIAQTVENSSPWLLTVAAAT 254
Cdd:cd07498   114 ISSAIdnaatygrnGKGGVVLFAAGNSGRSVSSGYAANPSVIAVAATD 161
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
402-485 6.62e-03

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


Pssm-ID: 173813  Cd Length: 247  Bit Score: 38.99  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443072518 402 KVAAFSSRGPSYIYPGVLKPDIAAPGVTVLAAAPKAFmdagipyrFDSGTSMSCPHVSGIIAVLKSLHPQ------WSPA 475
Cdd:cd07488   166 FASDVSNAGSEINSYGRRKVLIVAPGSNYNLPDGKDD--------FVSGTSFSAPLVTGIIALLLEFYDRqykkgnNNLI 237
                          90
                  ....*....|
gi 1443072518 476 ALKSAIMTTA 485
Cdd:cd07488   238 ALRALVSSSV 247
 
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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