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Conserved domains on  [gi|219763042|emb|CAW48082|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

S8 family peptidase( domain architecture ID 15916511)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
113-569 4.61e-116

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: 352.29  E-value: 4.61e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 113 KLHTTKSWDFVGLPLTAKRHL----KAERDVIIGVLDTGITPDSESFLDHGLGPPPAKWKGSCGPYKNFTG--CNNKIIG 186
Cdd:cd04852    2 QLHTTRSPDFLGLPGAWGGSLlgaaNAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPfsCNNKLIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 187 AKYFKH-----DGNVPAGEVRSPIDIDGHGTHTSSTVAGVLVANASLYGIANGTARGAVPSARLAMYKVCWARSGCADMD 261
Cdd:cd04852   82 ARYFSDgydayGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGCFGSD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 262 ILAGFEAAIHDGVEIISISIGGPIADYSSDSISVGSFHAMRKGILTVASAGNDGPSSGTVTNHEPWILTVAASgidrTfk 341
Cdd:cd04852  162 ILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAS----T-- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 342 skidlgngksfsgmgismfspkaksyplvsgvdaakntddkylarycfsdsldrkkvkgkvmvcrmggggvestiksygg 421
Cdd:cd04852      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 422 agaiivsdqyldnaqifmapatsvnssvgdiiyryinstrsasaviqktrqvtipapfvasfssrgpnpgsirlLKPDIA 501
Cdd:cd04852  236 --------------------------------------------------------------------------LKPDIA 241
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219763042 502 APGIDILAAFTlkrSLTGLDGDTQFSKFTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSA 569
Cdd:cd04852  242 APGVDILAAWT---PEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTA 306
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
645-743 3.05e-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: 131.55  E-value: 3.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  645 LNYPTIQLTLRSAKTStlAVFRRRVTNVGPPSSVYTATVRAPKGVEITVEPQSLSFSKASQKRSFKVVVKAKQMTPGKIV 724
Cdd:pfam17766   2 LNYPSIAVSFENLNGS--VTVTRTVTNVGDGPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAPSGEYV 79
                          90
                  ....*....|....*....
gi 219763042  725 SGLLVWKSPRHSVRSPIVI 743
Cdd:pfam17766  80 FGSLTWSDGKHTVRSPIVV 98
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
346-467 1.98e-21

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: 90.55  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 346 LGNGKSFsgMGISMFSPKAKSYPLVSGVDAAKNTDdkylARYCFSDSLDRKKVKGKVMVCRMGGGG----VESTIKSYGG 421
Cdd:cd02120    4 LGNGKTI--VGQSLYPGNLKTYPLVYKSANSGDVD----ASLCLPGSLDPSKVKGKIVLCDRGGNTsrvaKGDAVKAAGG 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 219763042 422 AGAIIV---SDQYLDNAQIFMAPATSVNSSVGDIIYRYINSTRSASAVI 467
Cdd:cd02120   78 AGMILAndpTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
38-115 4.58e-19

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


:

Pssm-ID: 428674  Cd Length: 82  Bit Score: 81.96  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042   38 YIIYLGDR---PDNTEETIKTHINLLSSLNISQEEAKERKVYSYTKAFNAFAAKLSPHEAKKMMEMEEVVSVSRNQYRKL 114
Cdd:pfam05922   2 YIVYLKEGaaaADSFSSHTEWHSSLLRSVLSEESSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVKL 81

                  .
gi 219763042  115 H 115
Cdd:pfam05922  82 H 82
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
113-569 4.61e-116

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: 352.29  E-value: 4.61e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 113 KLHTTKSWDFVGLPLTAKRHL----KAERDVIIGVLDTGITPDSESFLDHGLGPPPAKWKGSCGPYKNFTG--CNNKIIG 186
Cdd:cd04852    2 QLHTTRSPDFLGLPGAWGGSLlgaaNAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPfsCNNKLIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 187 AKYFKH-----DGNVPAGEVRSPIDIDGHGTHTSSTVAGVLVANASLYGIANGTARGAVPSARLAMYKVCWARSGCADMD 261
Cdd:cd04852   82 ARYFSDgydayGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGCFGSD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 262 ILAGFEAAIHDGVEIISISIGGPIADYSSDSISVGSFHAMRKGILTVASAGNDGPSSGTVTNHEPWILTVAASgidrTfk 341
Cdd:cd04852  162 ILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAS----T-- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 342 skidlgngksfsgmgismfspkaksyplvsgvdaakntddkylarycfsdsldrkkvkgkvmvcrmggggvestiksygg 421
Cdd:cd04852      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 422 agaiivsdqyldnaqifmapatsvnssvgdiiyryinstrsasaviqktrqvtipapfvasfssrgpnpgsirlLKPDIA 501
Cdd:cd04852  236 --------------------------------------------------------------------------LKPDIA 241
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219763042 502 APGIDILAAFTlkrSLTGLDGDTQFSKFTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSA 569
Cdd:cd04852  242 APGVDILAAWT---PEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTA 306
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
645-743 3.05e-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: 131.55  E-value: 3.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  645 LNYPTIQLTLRSAKTStlAVFRRRVTNVGPPSSVYTATVRAPKGVEITVEPQSLSFSKASQKRSFKVVVKAKQMTPGKIV 724
Cdd:pfam17766   2 LNYPSIAVSFENLNGS--VTVTRTVTNVGDGPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAPSGEYV 79
                          90
                  ....*....|....*....
gi 219763042  725 SGLLVWKSPRHSVRSPIVI 743
Cdd:pfam17766  80 FGSLTWSDGKHTVRSPIVV 98
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
137-689 4.58e-25

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 109.03  E-value: 4.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 137 RDVIIGVLDTGITPDSESFldhglgpppakwKGSCGPYKNFTGCNNkiigakyfkhdgnvpagevrSPIDIDGHGTHTSS 216
Cdd:COG1404  109 AGVTVAVIDTGVDADHPDL------------AGRVVGGYDFVDGDG--------------------DPSDDNGHGTHVAG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 217 TVAGVLVANASLYGIAngtargavPSARLAMYKVCWARSGCADMDILAGFEAAIHDGveiisisiggpiADYSSDSISVG 296
Cdd:COG1404  157 IIAANGNNGGGVAGVA--------PGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNG------------ADVINLSLGGP 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 297 SF-----------HAMRKGILTVASAGNDGPSSGTVtnhepwiltvaasgidrtfkskidlgngksfsgmgismfspkak 365
Cdd:COG1404  217 ADgysdalaaavdYAVDKGVLVVAAAGNSGSDDATV-------------------------------------------- 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 366 SYPlvsgvdaakntddkylARYcfsdsldrkkvkgkvmvcrmggggvestiksyggAGAIIVSdqyldnaqifmapATSV 445
Cdd:COG1404  253 SYP----------------AAY----------------------------------PNVIAVG-------------AVDA 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 446 NSSvgdiiyryinstrsasaviqktrqvtipapfVASFSSRGPnpgsirllKPDIAAPGIDILAaftlkrslTGLDGDTQ 525
Cdd:COG1404  270 NGQ-------------------------------LASFSNYGP--------KVDVAAPGVDILS--------TYPGGGYA 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 526 FskftiLSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAKPISrrvnkDAEFAYGGGQINPRRAASPGLVYDMDD 605
Cdd:COG1404  303 T-----LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLG-----APGPYYGYGLLADGAAGATSAGAGLAA 372
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 606 ISYVQFLCGEGYNATTLAPLVGTRSVSCSSIVPGLGHDSLNYPTIQLTLRSAKTSTLAVFRRRVTNVGPPSSVYTATVRA 685
Cdd:COG1404  373 AAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATAAGLLAAAALSTLAAVAAAVVVTTGTSTEALVA 452

                 ....
gi 219763042 686 PKGV 689
Cdd:COG1404  453 VGGT 456
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
137-585 4.76e-23

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: 99.84  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  137 RDVIIGVLDTGITPDsesfldHglgpppakwkgscgPYKNFTGCNNKIIGAKYFKHDGNVPAGEVRSPIDIDGHGTHtss 216
Cdd:pfam00082   2 KGVVVAVLDTGIDPN------H--------------PDLSGNLDNDPSDDPEASVDFNNEWDDPRDDIDDKNGHGTH--- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  217 tVAGVLVANASLYGIANGTArgavPSARLAMYKVCWArSGCADMDILAGFEAAIHDGVEIISIS--IGGPIADYSSDSIS 294
Cdd:pfam00082  59 -VAGIIAAGGNNSIGVSGVA----PGAKILGVRVFGD-GGGTDAITAQAISWAIPQGADVINMSwgSDKTDGGPGSWSAA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  295 VGSF-HAMRKGILTVASAGNDGPSsgtvtnhepwiltvaasgidrtfkskidlgngksfsgmgismfspkaksyplvsgv 373
Cdd:pfam00082 133 VDQLgGAEAAGSLFVWAAGNGSPG-------------------------------------------------------- 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  374 daaKNTDDKYLArycfsdsldrkkvkgkvmvcrmggggvestiksyggagaiivsdqyldnaqifmaPATSVNS-SVGdi 452
Cdd:pfam00082 157 ---GNNGSSVGY-------------------------------------------------------PAQYKNViAVG-- 176
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  453 iyryinSTRSASAviqktrqvtipaPFVASFSSRGPNpgSIRLLKPDIAAPGIDILAAFTLkRSLTGLDGDTQFSKFTIL 532
Cdd:pfam00082 177 ------AVDEASE------------GNLASFSSYGPT--LDGRLKPDIVAPGGNITGGNIS-STLLTTTSDPPNQGYDSM 235
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 219763042  533 SGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAKPISRRVNkDAEFAYG 585
Cdd:pfam00082 236 SGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGL-DRLFGYG 287
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
346-467 1.98e-21

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: 90.55  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 346 LGNGKSFsgMGISMFSPKAKSYPLVSGVDAAKNTDdkylARYCFSDSLDRKKVKGKVMVCRMGGGG----VESTIKSYGG 421
Cdd:cd02120    4 LGNGKTI--VGQSLYPGNLKTYPLVYKSANSGDVD----ASLCLPGSLDPSKVKGKIVLCDRGGNTsrvaKGDAVKAAGG 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 219763042 422 AGAIIV---SDQYLDNAQIFMAPATSVNSSVGDIIYRYINSTRSASAVI 467
Cdd:cd02120   78 AGMILAndpTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
38-115 4.58e-19

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


Pssm-ID: 428674  Cd Length: 82  Bit Score: 81.96  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042   38 YIIYLGDR---PDNTEETIKTHINLLSSLNISQEEAKERKVYSYTKAFNAFAAKLSPHEAKKMMEMEEVVSVSRNQYRKL 114
Cdd:pfam05922   2 YIVYLKEGaaaADSFSSHTEWHSSLLRSVLSEESSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVKL 81

                  .
gi 219763042  115 H 115
Cdd:pfam05922  82 H 82
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
473-594 2.53e-12

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: 68.89  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  473 VTIPA--PFVASFSSRGPN--PGSIRLLKP--DIAAPGIDILAAftlkrsltGLDGDtqfsKFTILSGTSMACPHVAGVA 546
Cdd:TIGR03921 169 VVYPAwyPGVLAVGSIDRDgtPSSFSLPGPwvDLAAPGENIVSL--------SPGGD----GLATTSGTSFAAPFVSGTA 236
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 219763042  547 AYVKSFHPDWTPAAIKSAIITSAKPISRRVNKDaefAYGGGQINPRRA 594
Cdd:TIGR03921 237 ALVRSRFPDLTAAQVRRRIEATADHPARGGRDD---YVGYGVVDPVAA 281
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
137-592 5.27e-06

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 50.16  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  137 RDVIIGVLDTGITPDSESFL-DHGLGPPPAKWKGScgpyKNFTGCNNKIIGAKYFKHDGNVPAGEVRSPIDID--GHGTH 213
Cdd:NF040809  652 RGVLIAIADTGIDYLHPDFIyPDGTSKILYLWDQT----KEGNPPEGFYIGTEYTREDINRAIAENDSSLSQDevGHGTM 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  214 TSSTVAGVLVANASLYGIAngtargavPSARLAMYKVCWARSGCADMDILAGFEAAIHDGVEII------SISIGGPIAD 287
Cdd:NF040809  728 LSGICAGLGNVNSEYAGVA--------EDAELIVIKLGKIDGFYNNAMLYAATQYAYKKARELNrpliinISVGSNSLAG 799
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  288 YSSDSISVGSFHAmrKGILTVASAGNDG----------PSSGTVTNHEPWILTVAASGIDRTFKSKIDLGNGKSFSGMGI 357
Cdd:NF040809  800 FTNRTNAEKAYFT--RGLCIVAGAGNEGntqthasgkiSAVGESVDVELEIEEDEENLQIEIWMDRPDRINVIIISPTGE 877
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  358 SMFSPKAKSYPLVSGVDAAKNTddKYLARYCFSDS--------LDRKKVKGKVMVCRMGGGGVESTIksyggagaiivSD 429
Cdd:NF040809  878 ESKDVGLSNYDEVSGIFDLENT--EYLIRYSYPTSysgqqftnVNLKNAKKGIWKIRLTGVYINSGI-----------YN 944
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  430 QYLDNaQIFMAPATSVNSSvgDIIYRyINSTRSASAVIQKTRQVTIPAPFVASfSSRGPNPGSIrlLKPDIAAPGIDILA 509
Cdd:NF040809  945 MYLPN-RVFLKPGTKFRES--DPFYT-INYPAVQDDIITVGAYDTINNSIWPT-SSRGPTIRNI--QKPDIVAPGVNIIA 1017
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  510 AFTlkrsltgldgdtqFSKFTILSGTSMACPHVAGVAA------YVKSFHPDwtpAAIKSAIITSAKPISRRVNKDA--E 581
Cdd:NF040809 1018 PYP-------------GNTYATITGTSAAAAHVSGVAAlylqytLVERRYPN---QAFTQKIKTFMQAGATRSTNIEypN 1081
                         490
                  ....*....|.
gi 219763042  582 FAYGGGQINPR 592
Cdd:NF040809 1082 TTSGYGLLNIR 1092
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
500-555 2.46e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.57  E-value: 2.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 219763042 500 IAAPGIDILAAFTlkrsltgldgdtqFSKFTILSGTSMACPHVAGVAAYVKSFHPD 555
Cdd:PTZ00262 534 LAAPGTNIYSTFP-------------KNSYRKLNGTSMAAPHVAAIASLILSINPS 576
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
480-585 2.83e-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: 44.38  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  480 VASFSSRGPNPGSIrlLKPDIAAPGIDILAAftlkrsltgLDGDTQFSkftiLSGTSMACPHVAGVAAY------VKSFH 553
Cdd:NF040809  418 VSVFSGEGDIENGI--YKPDLLAPGENIVSY---------LPGGTTGA----LTGTSMATPHVTGVCSLlmqwgiVEGND 482
                          90       100       110
                  ....*....|....*....|....*....|..
gi 219763042  554 PDWTPAAIKSAIITSAKPISRRVNKDAEFAYG 585
Cdd:NF040809  483 LFLYSQKLKALLLQNARRSPNRTYPNNSSGYG 514
 
Name Accession Description Interval E-value
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
113-569 4.61e-116

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: 352.29  E-value: 4.61e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 113 KLHTTKSWDFVGLPLTAKRHL----KAERDVIIGVLDTGITPDSESFLDHGLGPPPAKWKGSCGPYKNFTG--CNNKIIG 186
Cdd:cd04852    2 QLHTTRSPDFLGLPGAWGGSLlgaaNAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDFNPfsCNNKLIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 187 AKYFKH-----DGNVPAGEVRSPIDIDGHGTHTSSTVAGVLVANASLYGIANGTARGAVPSARLAMYKVCWARSGCADMD 261
Cdd:cd04852   82 ARYFSDgydayGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVAPRARIAVYKVCWPDGGCFGSD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 262 ILAGFEAAIHDGVEIISISIGGPIADYSSDSISVGSFHAMRKGILTVASAGNDGPSSGTVTNHEPWILTVAASgidrTfk 341
Cdd:cd04852  162 ILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAASAGNSGPGASTVPNVAPWVTTVAAS----T-- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 342 skidlgngksfsgmgismfspkaksyplvsgvdaakntddkylarycfsdsldrkkvkgkvmvcrmggggvestiksygg 421
Cdd:cd04852      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 422 agaiivsdqyldnaqifmapatsvnssvgdiiyryinstrsasaviqktrqvtipapfvasfssrgpnpgsirlLKPDIA 501
Cdd:cd04852  236 --------------------------------------------------------------------------LKPDIA 241
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219763042 502 APGIDILAAFTlkrSLTGLDGDTQFSKFTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSA 569
Cdd:cd04852  242 APGVDILAAWT---PEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTA 306
fn3_6 pfam17766
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ...
645-743 3.05e-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: 131.55  E-value: 3.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  645 LNYPTIQLTLRSAKTStlAVFRRRVTNVGPPSSVYTATVRAPKGVEITVEPQSLSFSKASQKRSFKVVVKAKQMTPGKIV 724
Cdd:pfam17766   2 LNYPSIAVSFENLNGS--VTVTRTVTNVGDGPSTYTASVTAPPGVSVTVSPSTLVFTKVGEKKSFTVTFTATKAPSGEYV 79
                          90
                  ....*....|....*....
gi 219763042  725 SGLLVWKSPRHSVRSPIVI 743
Cdd:pfam17766  80 FGSLTWSDGKHTVRSPIVV 98
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
138-594 1.33e-34

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: 133.61  E-value: 1.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 138 DVIIGVLDTGIT---PDSEsfldhGLGPPPAKWKGScgpyKNFTGCNNKIIGAKYFKHDGNVPAGEVRspidiDGHGTHt 214
Cdd:cd07474    3 GVKVAVIDTGIDythPDLG-----GPGFPNDKVKGG----YDFVDDDYDPMDTRPYPSPLGDASAGDA-----TGHGTH- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 215 sstVAGVLVANASLYGIANGTArgavPSARLAMYKVCWARSGCADMDILAGFEAAIHDGVEI---ISISIGGPIADYSSD 291
Cdd:cd07474   68 ---VAGIIAGNGVNVGTIKGVA----PKADLYAYKVLGPGGSGTTDVIIAAIEQAVDDGMDVinlSLGSSVNGPDDPDAI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 292 SISvgsfHAMRKGILTVASAGNDGPSSGTV--TNHEPWILTVAASgidrtfkskidlgngksfsgmgismfspkaksypl 369
Cdd:cd07474  141 AIN----NAVKAGVVVVAAAGNSGPAPYTIgsPATAPSAITVGAS----------------------------------- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 370 vsgvdaakntddkylarycfsdsldrkkvkgkvmvcrmggggvestiksyggagaiivsdqyldnaqifmapatsvnssv 449
Cdd:cd07474      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 450 gdiiyryinstrsasaviqkTRQVTIPAPFVASFSSRGPnPGSIRLLKPDIAAPGIDILAAFTlkrsltgldgdTQFSKF 529
Cdd:cd07474  182 --------------------TVADVAEADTVGPSSSRGP-PTSDSAIKPDIVAPGVDIMSTAP-----------GSGTGY 229
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219763042 530 TILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAKPI-SRRVNKDAEFAYGGGQINPRRA 594
Cdd:cd07474  230 ARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLyDSDGVVYPVSRQGAGRVDALRA 295
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
137-689 4.58e-25

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 109.03  E-value: 4.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 137 RDVIIGVLDTGITPDSESFldhglgpppakwKGSCGPYKNFTGCNNkiigakyfkhdgnvpagevrSPIDIDGHGTHTSS 216
Cdd:COG1404  109 AGVTVAVIDTGVDADHPDL------------AGRVVGGYDFVDGDG--------------------DPSDDNGHGTHVAG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 217 TVAGVLVANASLYGIAngtargavPSARLAMYKVCWARSGCADMDILAGFEAAIHDGveiisisiggpiADYSSDSISVG 296
Cdd:COG1404  157 IIAANGNNGGGVAGVA--------PGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNG------------ADVINLSLGGP 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 297 SF-----------HAMRKGILTVASAGNDGPSSGTVtnhepwiltvaasgidrtfkskidlgngksfsgmgismfspkak 365
Cdd:COG1404  217 ADgysdalaaavdYAVDKGVLVVAAAGNSGSDDATV-------------------------------------------- 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 366 SYPlvsgvdaakntddkylARYcfsdsldrkkvkgkvmvcrmggggvestiksyggAGAIIVSdqyldnaqifmapATSV 445
Cdd:COG1404  253 SYP----------------AAY----------------------------------PNVIAVG-------------AVDA 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 446 NSSvgdiiyryinstrsasaviqktrqvtipapfVASFSSRGPnpgsirllKPDIAAPGIDILAaftlkrslTGLDGDTQ 525
Cdd:COG1404  270 NGQ-------------------------------LASFSNYGP--------KVDVAAPGVDILS--------TYPGGGYA 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 526 FskftiLSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAKPISrrvnkDAEFAYGGGQINPRRAASPGLVYDMDD 605
Cdd:COG1404  303 T-----LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLG-----APGPYYGYGLLADGAAGATSAGAGLAA 372
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 606 ISYVQFLCGEGYNATTLAPLVGTRSVSCSSIVPGLGHDSLNYPTIQLTLRSAKTSTLAVFRRRVTNVGPPSSVYTATVRA 685
Cdd:COG1404  373 AAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATAAGLLAAAALSTLAAVAAAVVVTTGTSTEALVA 452

                 ....
gi 219763042 686 PKGV 689
Cdd:COG1404  453 VGGT 456
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
137-585 4.76e-23

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: 99.84  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  137 RDVIIGVLDTGITPDsesfldHglgpppakwkgscgPYKNFTGCNNKIIGAKYFKHDGNVPAGEVRSPIDIDGHGTHtss 216
Cdd:pfam00082   2 KGVVVAVLDTGIDPN------H--------------PDLSGNLDNDPSDDPEASVDFNNEWDDPRDDIDDKNGHGTH--- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  217 tVAGVLVANASLYGIANGTArgavPSARLAMYKVCWArSGCADMDILAGFEAAIHDGVEIISIS--IGGPIADYSSDSIS 294
Cdd:pfam00082  59 -VAGIIAAGGNNSIGVSGVA----PGAKILGVRVFGD-GGGTDAITAQAISWAIPQGADVINMSwgSDKTDGGPGSWSAA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  295 VGSF-HAMRKGILTVASAGNDGPSsgtvtnhepwiltvaasgidrtfkskidlgngksfsgmgismfspkaksyplvsgv 373
Cdd:pfam00082 133 VDQLgGAEAAGSLFVWAAGNGSPG-------------------------------------------------------- 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  374 daaKNTDDKYLArycfsdsldrkkvkgkvmvcrmggggvestiksyggagaiivsdqyldnaqifmaPATSVNS-SVGdi 452
Cdd:pfam00082 157 ---GNNGSSVGY-------------------------------------------------------PAQYKNViAVG-- 176
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  453 iyryinSTRSASAviqktrqvtipaPFVASFSSRGPNpgSIRLLKPDIAAPGIDILAAFTLkRSLTGLDGDTQFSKFTIL 532
Cdd:pfam00082 177 ------AVDEASE------------GNLASFSSYGPT--LDGRLKPDIVAPGGNITGGNIS-STLLTTTSDPPNQGYDSM 235
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 219763042  533 SGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAKPISRRVNkDAEFAYG 585
Cdd:pfam00082 236 SGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGL-DRLFGYG 287
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
346-467 1.98e-21

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: 90.55  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 346 LGNGKSFsgMGISMFSPKAKSYPLVSGVDAAKNTDdkylARYCFSDSLDRKKVKGKVMVCRMGGGG----VESTIKSYGG 421
Cdd:cd02120    4 LGNGKTI--VGQSLYPGNLKTYPLVYKSANSGDVD----ASLCLPGSLDPSKVKGKIVLCDRGGNTsrvaKGDAVKAAGG 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 219763042 422 AGAIIV---SDQYLDNAQIFMAPATSVNSSVGDIIYRYINSTRSASAVI 467
Cdd:cd02120   78 AGMILAndpTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
137-569 3.93e-20

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: 90.72  E-value: 3.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 137 RDVIIGVLDTGITPDSESFLDHGlgpppakwkgscgpyKNFTGCNNKIIGAKYfkhdgnvpagevrsPIDIDGHGTHTSS 216
Cdd:cd07487    2 KGITVAVLDTGIDAPHPDFDGRI---------------IRFADFVNTVNGRTT--------------PYDDNGHGTHVAG 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 217 TVAGVLVAnaslygiANGTARGAVPSARLAMYKVCWARSGCADMDILAGFEAAIH-------DGVeiisisiggpiadys 289
Cdd:cd07487   53 IIAGSGRA-------SNGKYKGVAPGANLVGVKVLDDSGSGSESDIIAGIDWVVEnnekyniRVV--------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 290 sdSISVGSFH---------------AMRKGILTVASAGNDGPSSGTVTN--HEPWILTVAASgidrtfkskidlgngksf 352
Cdd:cd07487  111 --NLSLGAPPdpsygedplcqaverLWDAGIVVVVAAGNSGPGPGTITSpgNSPKVITVGAV------------------ 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 353 sgmgismfspkaksyplvsgvdaaknTDDKYLARYcfsdsldrkkvkgkvmvcrmggggvestiksyggagaiivsdqyl 432
Cdd:cd07487  171 --------------------------DDNGPHDDG--------------------------------------------- 179
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 433 dnaqifmapatsvnssvgdiiyryinstrsasaviqktrqvtipapfVASFSSRGPNPgsIRLLKPDIAAPGIDILAAft 512
Cdd:cd07487  180 -----------------------------------------------ISYFSSRGPTG--DGRIKPDVVAPGENIVSC-- 208
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219763042 513 lkRSLTGLDGDTQFSKFTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSA 569
Cdd:cd07487  209 --RSPGGNPGAGVGSGYFEMSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDTA 263
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
38-115 4.58e-19

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


Pssm-ID: 428674  Cd Length: 82  Bit Score: 81.96  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042   38 YIIYLGDR---PDNTEETIKTHINLLSSLNISQEEAKERKVYSYTKAFNAFAAKLSPHEAKKMMEMEEVVSVSRNQYRKL 114
Cdd:pfam05922   2 YIVYLKEGaaaADSFSSHTEWHSSLLRSVLSEESSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVKL 81

                  .
gi 219763042  115 H 115
Cdd:pfam05922  82 H 82
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
139-595 1.78e-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: 86.89  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 139 VIIGVLDTGItpdseSFLDHGLGpppakwkGSCGPyknftGCnnKIIGAKYFKHDGNVPAGEVR---SPIDIDGHGTHts 215
Cdd:cd07489   15 VKVAVVDTGI-----DYTHPALG-------GCFGP-----GC--KVAGGYDFVGDDYDGTNPPVpddDPMDCQGHGTH-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 216 stVAGVLVANASLYGIAngtarGAVPSARLAMYKVcWARSGCADMD-ILAGFEAAIHDGVEiisisiggpiadyssdsis 294
Cdd:cd07489   74 --VAGIIAANPNAYGFT-----GVAPEATLGAYRV-FGCSGSTTEDtIIAAFLRAYEDGAD------------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 295 vgsfhamrkgILTVASAGNDGPSSgtvtnhEPWilTVAASGIdrtfkskidlgngksfsgmgismfspkaksyplvsgVD 374
Cdd:cd07489  127 ----------VITASLGGPSGWSE------DPW--AVVASRI------------------------------------VD 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 375 AakntddkylarycfsdsldrkkvkGKVMVCRMGgggvestikSYGGAGaiivsdqyldnaqIFMAPATSvnssvgdiiy 454
Cdd:cd07489  153 A------------------------GVVVTIAAG---------NDGERG-------------PFYASSPA---------- 176
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 455 ryinSTRSASAViqktrqvtipAPFVASFSSRGP-NPGSirlLKPDIAAPGIDILAAFtlkrsLTGLDGdtqfskFTILS 533
Cdd:cd07489  177 ----SGRGVIAV----------ASVDSYFSSWGPtNELY---LKPDVAAPGGNILSTY-----PLAGGG------YAVLS 228
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219763042 534 GTSMACPHVAGVAA-YVKSFHPDWTPAAIKSAIITSAKPI--SRRVNKDAEFAY----GGGQINPRRAA 595
Cdd:cd07489  229 GTSMATPYVAGAAAlLIQARHGKLSPAELRDLLASTAKPLpwSDGTSALPDLAPvaqqGAGLVNAYKAL 297
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
137-585 2.12e-18

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


Pssm-ID: 173804 [Multi-domain]  Cd Length: 455  Bit Score: 88.83  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 137 RDVIIGVLDTGI--------TPDS----ESFLDHGLGPPPAKwkgscGPYKNFTGCNNKIIGAKYfkhDGNVPAGEVRSP 204
Cdd:cd07478    4 KGVLVGIIDTGIdylhpefrNEDGttriLYIWDQTIPGGPPP-----GGYYGGGEYTEEIINAAL---ASDNPYDIVPSR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 205 iDIDGHGTHtsstVAGVLVANaslyGIANGTARGAVPSARLAMYKVCWARSGCADMDILAGF--EAAIHDGVEIISisig 282
Cdd:cd07478   76 -DENGHGTH----VAGIAAGN----GDNNPDFKGVAPEAELIVVKLKQAKKYLREFYEDVPFyqETDIMLAIKYLY---- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 283 gpiaDYSSDS-------ISVGS----------------FHAMRKGILTVASAGNDGPSSGTVTNhepwilTVAASGIDRT 339
Cdd:cd07478  143 ----DKALELnkplvinISLGTnfgshdgtslleryidAISRLRGIAVVVGAGNEGNTQHHHSG------GIVPNGETKT 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 340 FKSKIDLGNgKSFSG---------MGISMFSPkaksyplvSGvDAAKNTDDKYLARYCFSDSLDRKKVKgkvmvcrmggg 410
Cdd:cd07478  213 VELNVGEGE-KGFNLeiwgdfpdrFSVSIISP--------SG-ESSGRINPGIGGSESYKFVFEGTTVY----------- 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 411 gVE-STIKSYGGAGAIIVSDQYLDNA--QIFMAPATSVNSSVgDI---IYRYINS-TRSASAVIQKTrqVTIPAP----- 478
Cdd:cd07478  272 -VYyYLPEPYTGDQLIFIRFKNIKPGiwKIRLTGVSITDGRF-DAwlpSRGLLSEnTRFLEPDPYTT--LTIPGTarsvi 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 479 ----------FVASFSSRGPNPGsiRLLKPDIAAPGIDILAAftlkrsltGLDGDtqfskFTILSGTSMACPHVAGVAA- 547
Cdd:cd07478  348 tvgaynqnnnSIAIFSGRGPTRD--GRIKPDIAAPGVNILTA--------SPGGG-----YTTRSGTSVAAAIVAGACAl 412
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 219763042 548 -----YVKSFHPDWTPAAIKSAIITSAKPISRRVNKDAEFAYG 585
Cdd:cd07478  413 llqwgIVRGNDPYLYGEKIKTYLIRGARRRPGDEYPNPEWGYG 455
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
139-570 4.00e-17

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: 81.83  E-value: 4.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 139 VIIGVLDTGITPDSESFLDhglgpppakwkgscgpyknftgcnnKIIGAKYFKHDGNVPAGEvrsPIDIDGHGTHTSSTV 218
Cdd:cd07490    2 VTVAVLDTGVDADHPDLAG-------------------------RVAQWADFDENRRISATE---VFDAGGHGTHVSGTI 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 219 AGvlvanaslyGIANGTARGAVPSARLAMYKVCWArSGCADMDILAGFEAAIHDGveiisisiggpiADYSSDSI----- 293
Cdd:cd07490   54 GG---------GGAKGVYIGVAPEADLLHGKVLDD-GGGSLSQIIAGMEWAVEKD------------ADVVSMSLggtyy 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 294 SVGSFHAM------RKGILTVASAGNDGPssGTVTnhepwiltvaasgidrtfkskidlgngksfsgmgismfSPkAKSY 367
Cdd:cd07490  112 SEDPLEEAvealsnQTGALFVVSAGNEGH--GTSG--------------------------------------SP-GSAY 150
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 368 PLVSgvdaakntddkylarycfsdsldrkkvkgkvmvcrmggggvestiksyggAGAIivsDQYLDNAQIfmapatsvnS 447
Cdd:cd07490  151 AALS--------------------------------------------------VGAV---DRDDEDAWF---------S 168
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 448 SVGDIIyryinstrsasaviqktrqvtipapfvASFSSRGPNPGSiRLLKPDIAAPGIDILAAftlkrsLTGLDGDTQFs 527
Cdd:cd07490  169 SFGSSG---------------------------ASLVSAPDSPPD-EYTKPDVAAPGVDVYSA------RQGANGDGQY- 213
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 219763042 528 kfTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAK 570
Cdd:cd07490  214 --TRLSGTSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
139-568 2.02e-16

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: 79.55  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 139 VIIGVLDTGITPDSESFLDHGLGPPPAKwkgscgpyknftgcnnkiigakyfkhDGNVPAGEVRSPIDIDGHGTHTSSTV 218
Cdd:cd00306    1 VTVAVIDTGVDPDHPDLDGLFGGGDGGN--------------------------DDDDNENGPTDPDDGNGHGTHVAGII 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 219 AGVlvanaslygIANGTARGAVPSARLAMYKVCWARSGCADMDILAGFEAAIHDgveiisisiggPIAD------YSSDS 292
Cdd:cd00306   55 AAS---------ANNGGGVGVAPGAKLIPVKVLDGDGSGSSSDIAAAIDYAAAD-----------QGADvinlslGGPGS 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 293 ISVGSFHAM------RKGILTVASAGNDGPSSGTVTN---HEPWILTVAASGIDRTFKSkidlgngksfsgmgismfspk 363
Cdd:cd00306  115 PPSSALSEAidyalaKLGVLVVAAAGNDGPDGGTNIGypaASPNVIAVGAVDRDGTPAS--------------------- 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 364 aksyplvsgvdaakntddkylarycfsdsldrkkvkgkvmvcrmggggvestiksyggagaiivsdqyldnaqifmapat 443
Cdd:cd00306      --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 444 svnssvgdiiyryinstrsasaviqktrqvtipapfvaSFSSRGPnpgsirllKPDIAAPGIDILAAFTLKRsltgldgd 523
Cdd:cd00306  174 --------------------------------------PSSNGGA--------GVDIAAPGGDILSSPTTGG-------- 199
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 219763042 524 tqfSKFTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITS 568
Cdd:cd00306  200 ---GGYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
481-570 1.83e-15

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: 76.85  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 481 ASFSSRGPNpgsirllKPDIAAPGIDILAaftlkrslTGLDGDTQFskftiLSGTSMACPHVAGVAAYVKSFHPDWTPAA 560
Cdd:cd07473  190 ASFSNYGKK-------TVDLAAPGVDILS--------TSPGGGYGY-----MSGTSMATPHVAGAAALLLSLNPNLTAAQ 249
                         90
                 ....*....|
gi 219763042 561 IKSAIITSAK 570
Cdd:cd07473  250 IKDAILSSAD 259
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
481-568 2.40e-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: 76.03  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 481 ASFSSRGPNPgsirllkpDIAAPGIDILAaftlkrslTGLDGDtqfskFTILSGTSMACPHVAGVAAYVKSFHPDWTPAA 560
Cdd:cd07477  163 ASFSSTGPEV--------ELAAPGVDILS--------TYPNND-----YAYLSGTSMATPHVAGVAALVWSKRPELTNAQ 221

                 ....*...
gi 219763042 561 IKSAIITS 568
Cdd:cd07477  222 VRQALNKT 229
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
440-570 9.72e-15

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


Pssm-ID: 173791 [Multi-domain]  Cd Length: 293  Bit Score: 75.44  E-value: 9.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 440 APATSVNS-SVGdiiyryiNSTRSASAVIQKTRQVTIPAPFVASFSSRGPN-PGSIrllKPDIAAPGIDILAAftlkRSL 517
Cdd:cd04842  167 SPATAKNVlTVG-------ASNNPSVSNGEGGLGQSDNSDTVASFSSRGPTyDGRI---KPDLVAPGTGILSA----RSG 232
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219763042 518 TGLDGDTQFSKFTILSGTSMACPHVAGVAA----------YVKSFHPdwTPAAIKSAIITSAK 570
Cdd:cd04842  233 GGGIGDTSDSAYTSKSGTSMATPLVAGAAAllrqyfvdgyYPTKFNP--SAALLKALLINSAR 293
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
499-569 1.64e-14

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: 74.09  E-value: 1.64e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219763042 499 DIAAPGIDILAAftlkrsltGLDGDTQFskfTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSA 569
Cdd:cd04077  194 DIFAPGVDILSA--------WIGSDTAT---ATLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
479-554 2.04e-13

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: 70.87  E-value: 2.04e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219763042 479 FVASFSSRGPNPGSIRllKPDIAAPGIDILAAFTlkrsltgldGDTqfskFTILSGTSMACPHVAGVAAYVKSFHP 554
Cdd:cd07481  186 VLADFSSRGPSTYGRI--KPDISAPGVNIRSAVP---------GGG----YGSSSGTSMAAPHVAGVAALLWSANP 246
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
463-596 1.43e-12

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: 69.60  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 463 ASAviqKTRQVTIPAPFVASFSSRGPNPgSIRLlKPDIAAPGIDILAaftlkrslTGLDGdtqfsKFTILSGTSMACPHV 542
Cdd:cd07475  220 ASA---NKKVPNPNGGQMSGFSSWGPTP-DLDL-KPDITAPGGNIYS--------TVNDN-----TYGYMSGTSMASPHV 281
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219763042 543 AGVAA----YVKSFHPDWTPA----AIKSAIITSAKPISRRVNKDAEFA---YGGGQINPRRAAS 596
Cdd:cd07475  282 AGASAlvkqRLKEKYPKLSGEelvdLVKNLLMNTATPPLDSEDTKTYYSprrQGAGLIDVAKAIA 346
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
481-573 1.77e-12

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


Pssm-ID: 173810 [Multi-domain]  Cd Length: 260  Bit Score: 68.06  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 481 ASFSSRGPNPgsirllkpDIAAPGIDILAaftlkrslTGLDGDtqfskFTILSGTSMACPHVAGVAAYVKSFHPdWTPAA 560
Cdd:cd07484  190 ASFSNYGKWV--------DVSAPGGGILS--------TTPDGD-----YAYMSGTSMATPHVAGVAALLYSQGP-LSASE 247
                         90
                 ....*....|...
gi 219763042 561 IKSAIITSAKPIS 573
Cdd:cd07484  248 VRDALKKTADDIG 260
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
473-594 2.53e-12

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: 68.89  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  473 VTIPA--PFVASFSSRGPN--PGSIRLLKP--DIAAPGIDILAAftlkrsltGLDGDtqfsKFTILSGTSMACPHVAGVA 546
Cdd:TIGR03921 169 VVYPAwyPGVLAVGSIDRDgtPSSFSLPGPwvDLAAPGENIVSL--------SPGGD----GLATTSGTSFAAPFVSGTA 236
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 219763042  547 AYVKSFHPDWTPAAIKSAIITSAKPISRRVNKDaefAYGGGQINPRRA 594
Cdd:TIGR03921 237 ALVRSRFPDLTAAQVRRRIEATADHPARGGRDD---YVGYGVVDPVAA 281
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
422-594 6.41e-10

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


Pssm-ID: 173798 [Multi-domain]  Cd Length: 275  Bit Score: 60.77  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 422 AGA-IIVSDQYLDNAQIF----MAPATSVNSSVGDIIYryI----NSTRSASAV---------------IQKTRQVTIPA 477
Cdd:cd05562   89 AGAdIIVDDIGYLNEPFFqdgpIAQAVDEVVASPGVLY--FssagNDGQSGSIFghaaapgaiavgavdYGNTPAFGSDP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 478 PFVASFSSRGPN----PGSIRLLKPDIAAP-GIDilaaftlkrSLTGLDGDTqFSKFTilsGTSMACPHVAGVAAYVKSF 552
Cdd:cd05562  167 APGGTPSSFDPVgirlPTPEVRQKPDVTAPdGVN---------GTVDGDGDG-PPNFF---GTSAAAPHAAGVAALVLSA 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 219763042 553 HPDWTPAAIKSAIITSAKPISrrvNKDAEFAYGGGQINPRRA 594
Cdd:cd05562  234 NPGLTPADIRDALRSTALDMG---EPGYDNASGSGLVDADRA 272
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
481-565 6.77e-10

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: 60.77  E-value: 6.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 481 ASFSSRGPnpgsirllKPDIAAPGIDILAAFTLKRSLTGLDGDTQFSKFTI--LSGTSMACPHVAGVAAYVKSFHPDWTP 558
Cdd:cd07496  204 ASYSNYGP--------AVDVSAPGGDCASDVNGDGYPDSNTGTTSPGGSTYgfLQGTSMAAPHVAGVAALMKSVNPSLTP 275

                 ....*..
gi 219763042 559 AAIKSAI 565
Cdd:cd07496  276 AQIESLL 282
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
480-569 1.52e-09

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: 59.24  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 480 VASFSSRGPNPGSiRLlKPDIAAPGIDIlaaftlkrsltglDGDTQFSKFTILSGTSMACPHVAGVAAYVKSFHPDWTPA 559
Cdd:cd07493  186 KASFSSIGPTADG-RL-KPDVMALGTGI-------------YVINGDGNITYANGTSFSCPLIAGLIACLWQAHPNWTNL 250
                         90
                 ....*....|
gi 219763042 560 AIKSAIITSA 569
Cdd:cd07493  251 QIKEAILKSA 260
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
139-342 7.40e-09

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: 57.33  E-value: 7.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 139 VIIGVLDTGITPDSESFldhglgpppakwkgscgpyknftgcNNKIIGAKYFKhdgNVPAGEVRSPIDIDGHGTHtsstV 218
Cdd:cd04848    5 VKVGVIDSGIDLSHPEF-------------------------AGRVSEASYYV---AVNDAGYASNGDGDSHGTH----V 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 219 AGVLVANASLYGIAnGTArgavPSARLAMYKVCWARSGCADM-DILAGFEAAIHDGV------------EIISISIGGPI 285
Cdd:cd04848   53 AGVIAAARDGGGMH-GVA----PDATLYSARASASAGSTFSDaDIAAAYDFLAASGVriinnswggnpaIDTVSTTYKGS 127
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219763042 286 ADYSSDSISVGSFHAMRKGILTVASAGNDGPSSGTVTNH---------EPWILTVAASGIDRTFKS 342
Cdd:cd04848  128 AATQGNTLLAALARAANAGGLFVFAAGNDGQANPSLAAAalpylepelEGGWIAVVAVDPNGTIAS 193
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
479-570 1.25e-08

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: 56.99  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 479 FVASFSsrgpNPGSIRLlkpDIAAPGIDILAAftlkrsltgldgdTQFSKFTILSGTSMACPHVAGVAAYVKSFHPDWTP 558
Cdd:cd07483  220 LVANFS----NYGKKNV---DVFAPGERIYST-------------TPDNEYETDSGTSMAAPVVSGVAALIWSYYPNLTA 279
                         90
                 ....*....|..
gi 219763042 559 AAIKSAIITSAK 570
Cdd:cd07483  280 KEVKQIILESGV 291
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
480-547 2.43e-08

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: 56.23  E-value: 2.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219763042 480 VASFSSRGPNPGSirllKPDIAAPGIDILAAftlkrsLTGldgdtqfSKFTILSGTSMACPHVAGVAA 547
Cdd:cd07480  199 TGNFSAVANFSNG----EVDIAAPGVDIVSA------APG-------GGYRSMSGTSMATPHVAGVAA 249
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
480-568 3.19e-08

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


Pssm-ID: 173811 [Multi-domain]  Cd Length: 273  Bit Score: 55.57  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 480 VASFSSRGpnpgsirlLKPDIAAPGIDILAAFTLKRSLTGlDGDTQFskftiLSGTSMACPHVAGVAAYVKSFHPDW-TP 558
Cdd:cd07485  198 KASFSNYG--------RWVDIAAPGVGTILSTVPKLDGDG-GGNYEY-----LSGTSMAAPHVSGVAALVLSKFPDVfTP 263
                         90
                 ....*....|
gi 219763042 559 AAIKSAIITS 568
Cdd:cd07485  264 EQIRKLLEES 273
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
139-315 6.40e-08

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


Pssm-ID: 173808 [Multi-domain]  Cd Length: 294  Bit Score: 54.68  E-value: 6.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 139 VIIGVLDTGITPDSESFldhglgpppakwKGSCGPYKNFtgcnnkIIGAKYFKHDGNVPAGEVRSPIDIDGHGTHtsstV 218
Cdd:cd07482    2 VTVAVIDSGIDPDHPDL------------KNSISSYSKN------LVPKGGYDGKEAGETGDINDIVDKLGHGTA----V 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 219 AGVLVANASLYGIAngtargavPSARLAMYKVCWARSGCADMDILAGFEAAIHDGVEIISISIGGPIADYSSDSISVGSF 298
Cdd:cd07482   60 AGQIAANGNIKGVA--------PGIGIVSYRVFGSCGSAESSWIIKAIIDAADDGVDVINLSLGGYLIIGGEYEDDDVEY 131
                        170       180
                 ....*....|....*....|....*
gi 219763042 299 HAMR--------KGILTVASAGNDG 315
Cdd:cd07482  132 NAYKkainyaksKGSIVVAAAGNDG 156
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
481-568 7.11e-08

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: 54.27  E-value: 7.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 481 ASFSSRGPNPgsirllkpDIAAPGIDILAAFTLKRSLTGLDGDtQFSKFtilSGTSMACPHVAGVAAYVKSFHPDWTPAA 560
Cdd:cd07498  167 ASYSNYGNYV--------DLVAPGVGIWTTGTGRGSAGDYPGG-GYGSF---SGTSFASPVAAGVAALILSANPNLTPAE 234

                 ....*...
gi 219763042 561 IKSAIITS 568
Cdd:cd07498  235 VEDILTST 242
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
416-570 8.04e-08

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


Pssm-ID: 173793 [Multi-domain]  Cd Length: 291  Bit Score: 54.62  E-value: 8.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 416 IKSYGGAGAIIVSDQYLDNAQIFMA-PATSVNS-SVGDIIYRYINSTRSasaviqktRQVTIPAPFVASFSSRGPN-PGS 492
Cdd:cd04847  140 VVSAGNLGDDDAADGPPRIQDDEIEdPADSVNAlTVGAITSDDDITDRA--------RYSAVGPAPAGATTSSGPGsPGP 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 493 IrllKPDIAAPGIDILAAFTLKRSLTGLDGDTQFS-----KFTILSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIIT 567
Cdd:cd04847  212 I---KPDVVAFGGNLAYDPSGNAADGDLSLLTTLSspsggGFVTVGGTSFAAPLAARLAAGLFAELPELSPETIRALLIH 288

                 ...
gi 219763042 568 SAK 570
Cdd:cd04847  289 SAE 291
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
480-551 5.51e-07

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: 52.09  E-value: 5.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219763042 480 VASFSSRGPNPgsIRLLKPDIAAPGIdilAAFTLKRSLTGLDGDTQFSKFTILSGTSMACPHVAGVAAYVKS 551
Cdd:cd07497  221 VVSWSSRGPSI--AGDPKPDLAAIGA---FAWAPGRVLDSGGALDGNEAFDLFGGTSMATPMTAGSAALVIS 287
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
480-573 2.49e-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: 49.76  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 480 VASFSSRGPN----PGSIRLLKPDIAAPGIDILAaftlkrslTGLDGDTQfskftILSGTSMACPHVAGVAAYVKSFHPD 555
Cdd:cd07479  166 IARFSSRGMTtwelPGGYGRVKPDIVTYGSGVYG--------SKLKGGCR-----ALSGTSVASPVVAGAVALLLSTVPE 232
                         90       100
                 ....*....|....*....|..
gi 219763042 556 ----WTPAAIKSAIITSAKPIS 573
Cdd:cd07479  233 krdlINPASMKQALIESATRLP 254
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
137-592 5.27e-06

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 50.16  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  137 RDVIIGVLDTGITPDSESFL-DHGLGPPPAKWKGScgpyKNFTGCNNKIIGAKYFKHDGNVPAGEVRSPIDID--GHGTH 213
Cdd:NF040809  652 RGVLIAIADTGIDYLHPDFIyPDGTSKILYLWDQT----KEGNPPEGFYIGTEYTREDINRAIAENDSSLSQDevGHGTM 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  214 TSSTVAGVLVANASLYGIAngtargavPSARLAMYKVCWARSGCADMDILAGFEAAIHDGVEII------SISIGGPIAD 287
Cdd:NF040809  728 LSGICAGLGNVNSEYAGVA--------EDAELIVIKLGKIDGFYNNAMLYAATQYAYKKARELNrpliinISVGSNSLAG 799
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  288 YSSDSISVGSFHAmrKGILTVASAGNDG----------PSSGTVTNHEPWILTVAASGIDRTFKSKIDLGNGKSFSGMGI 357
Cdd:NF040809  800 FTNRTNAEKAYFT--RGLCIVAGAGNEGntqthasgkiSAVGESVDVELEIEEDEENLQIEIWMDRPDRINVIIISPTGE 877
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  358 SMFSPKAKSYPLVSGVDAAKNTddKYLARYCFSDS--------LDRKKVKGKVMVCRMGGGGVESTIksyggagaiivSD 429
Cdd:NF040809  878 ESKDVGLSNYDEVSGIFDLENT--EYLIRYSYPTSysgqqftnVNLKNAKKGIWKIRLTGVYINSGI-----------YN 944
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  430 QYLDNaQIFMAPATSVNSSvgDIIYRyINSTRSASAVIQKTRQVTIPAPFVASfSSRGPNPGSIrlLKPDIAAPGIDILA 509
Cdd:NF040809  945 MYLPN-RVFLKPGTKFRES--DPFYT-INYPAVQDDIITVGAYDTINNSIWPT-SSRGPTIRNI--QKPDIVAPGVNIIA 1017
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  510 AFTlkrsltgldgdtqFSKFTILSGTSMACPHVAGVAA------YVKSFHPDwtpAAIKSAIITSAKPISRRVNKDA--E 581
Cdd:NF040809 1018 PYP-------------GNTYATITGTSAAAAHVSGVAAlylqytLVERRYPN---QAFTQKIKTFMQAGATRSTNIEypN 1081
                         490
                  ....*....|.
gi 219763042  582 FAYGGGQINPR 592
Cdd:NF040809 1082 TTSGYGLLNIR 1092
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
499-585 1.86e-04

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


Pssm-ID: 173797 [Multi-domain]  Cd Length: 239  Bit Score: 43.82  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 499 DIAAPGIDILAAftlkrsltglDGDtqfSKFTILSGTSMACPHVAGVAAYVKSFHPDWtPAAIKSAIITSAKPISRRvNK 578
Cdd:cd05561  168 DFAAPGVDVWVA----------APG---GGYRYVSGTSFAAPFVTAALALLLQASPLA-PDDARARLAATAKDLGPP-GR 232

                 ....*..
gi 219763042 579 DAEFAYG 585
Cdd:cd05561  233 DPVFGYG 239
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
500-555 2.46e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.57  E-value: 2.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 219763042 500 IAAPGIDILAAFTlkrsltgldgdtqFSKFTILSGTSMACPHVAGVAAYVKSFHPD 555
Cdd:PTZ00262 534 LAAPGTNIYSTFP-------------KNSYRKLNGTSMAAPHVAAIASLILSINPS 576
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
480-585 2.83e-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: 44.38  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042  480 VASFSSRGPNPGSIrlLKPDIAAPGIDILAAftlkrsltgLDGDTQFSkftiLSGTSMACPHVAGVAAY------VKSFH 553
Cdd:NF040809  418 VSVFSGEGDIENGI--YKPDLLAPGENIVSY---------LPGGTTGA----LTGTSMATPHVTGVCSLlmqwgiVEGND 482
                          90       100       110
                  ....*....|....*....|....*....|..
gi 219763042  554 PDWTPAAIKSAIITSAKPISRRVNKDAEFAYG 585
Cdd:NF040809  483 LFLYSQKLKALLLQNARRSPNRTYPNNSSGYG 514
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
194-387 6.10e-04

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


Pssm-ID: 173822 [Multi-domain]  Cd Length: 242  Bit Score: 42.33  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 194 GNVPAGEVRSP----IDIDGHGThtssTVAGVLVANASL-YGIAngtarGAVPSARLAMYKVCWARSGCADMDILAGFEA 268
Cdd:cd07498   22 KLVPGWNFVSNndptSDIDGHGT----ACAGVAAAVGNNgLGVA-----GVAPGAKLMPVRIADSLGYAYWSDIAQAITW 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 269 AIHDGVEIISISIGGPIADYSSDSISVGSFHAMR--KGILTVASAGNDGPSSGTVTNHEPWILTVAASGidrtfkskiDL 346
Cdd:cd07498   93 AADNGADVISNSWGGSDSTESISSAIDNAATYGRngKGGVVLFAAGNSGRSVSSGYAANPSVIAVAATD---------SN 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 219763042 347 GNGKSFSGMG--ISMFSPKAKSYPLVSGVDAAKNTDDKYLARY 387
Cdd:cd07498  164 DARASYSNYGnyVDLVAPGVGIWTTGTGRGSAGDYPGGGYGSF 206
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
206-358 1.61e-03

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


Pssm-ID: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 41.30  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 206 DIDGHGTHTSSTVAGVLVANASLYGIANGTA-RGAVPSARLAMYKVCWARSGCADMDILAGFEaaiHDGVEIISISIGGP 284
Cdd:cd07497   54 DFFSHGTSCASVAAGRGKMEYNLYGYTGKFLiRGIAPDAKIAAVKALWFGDVIYAWLWTAGFD---PVDRKLSWIYTGGP 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 285 IADYSSDSISVGSFH------------------AMRKGILTVASAGNDGPSSGTVTN--HEPWILTVAASgIDRTFKSKI 344
Cdd:cd07497  131 RVDVISNSWGISNFAytgyapgldisslvidalVTYTGVPIVSAAGNGGPGYGTITApgAASLAISVGAA-TNFDYRPFY 209
                        170
                 ....*....|....
gi 219763042 345 DLGNGKSFSGMGIS 358
Cdd:cd07497  210 LFGYLPGGSGDVVS 223
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
500-570 2.15e-03

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: 40.40  E-value: 2.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219763042 500 IAAPGIDILAaftlkrslTGLDGDTQFSkftilSGTSMACPHVAGVAAYVKSFHPDWTPAAIKSAIITSAK 570
Cdd:cd07492  165 FSADGVDIIA--------PAPHGRYLTV-----SGNSFAAPHVTGMVALLLSEKPDIDANDLKRLLQRLAV 222
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
484-572 2.23e-03

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


Pssm-ID: 173796 [Multi-domain]  Cd Length: 412  Bit Score: 41.12  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219763042 484 SSRGPNP-GSirlLKPDIAAPG--IDILAAFTLKRSltgldgdtqfskfTILSGTSMACPHVAGVAAYV----KSFHPDW 556
Cdd:cd04857  333 SSRGPTAdGA---LGVSISAPGgaIASVPNWTLQGS-------------QLMNGTSMSSPNACGGIALLlsglKAEGIPY 396
                         90
                 ....*....|....*.
gi 219763042 557 TPAAIKSAIITSAKPI 572
Cdd:cd04857  397 TPYSVRRALENTAKKL 412
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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