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Conserved domains on  [gi|6320775|ref|NP_010854|]
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proteinase B [Saccharomyces cerevisiae S288C]

Protein Classification

S8 family peptidase( domain architecture ID 10531344)

S8 family peptidase is a subtilisin-like serine protease containing a Asp/His/Ser catalytic triad that is not homologous to trypsin

CATH:  3.40.50.200
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S8
PubMed:  8439290|9070434
SCOP:  2000207

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 290-566 4.11e-147

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: 426.16  E-value: 4.11e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  290 WGLARISHRerlNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKH 369
Cdd:cd04077   1 WGLDRISQR---DLPLDGTYYYDSSTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDCNGHGTHVAGTVGGKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  370 YGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKeaqekkkGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFA 449
Cdd:cd04077  78 YGVAKKANLVAVKVLDCNGSGTLSGIIAGLEWVANDATK-------RGKPAVANMSLGGGASTALDAAVAAAVNAGVVVV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  450 VAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLL 529
Cdd:cd04077 151 VAAGNSNQDACNYSPASAPEAITVGATDSDDARASFSNYGSCVDIFAPGVDILSAWIGSDTATATLSGTSMAAPHVAGLA 230

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6320775  530 TYFLSLQPgsdseffelgqdSLTPQQLKKKLIHYSTK 566
Cdd:cd04077 231 AYLLSLGP------------DLSPAEVKARLLNLATK 255
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 182-278 1.25e-10

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


:

Pssm-ID: 428674  Cd Length: 82  Bit Score: 58.07  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    182 RYIIVFKRGAPQEEIDFHKENVQQAQLQSVenlsaedaffistkdTSLSTSEAGGIQDSFNIdnLFSGYIGYFTQEIVDL 261
Cdd:pfam05922   1 TYIVYLKEGAAAADSFSSHTEWHSSLLRSV---------------LSEESSAEAGILYSYKI--GFNGFAAKLTEEEAEK 63

                          90
                  ....*....|....*..
gi 6320775    262 IRQNPLVDFVERDSIVE 278
Cdd:pfam05922  64 LRKHPEVVSVEPDQVVK 80
 
Name Accession Description Interval E-value
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 290-566 4.11e-147

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: 426.16  E-value: 4.11e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  290 WGLARISHRerlNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKH 369
Cdd:cd04077   1 WGLDRISQR---DLPLDGTYYYDSSTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDCNGHGTHVAGTVGGKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  370 YGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKeaqekkkGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFA 449
Cdd:cd04077  78 YGVAKKANLVAVKVLDCNGSGTLSGIIAGLEWVANDATK-------RGKPAVANMSLGGGASTALDAAVAAAVNAGVVVV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  450 VAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLL 529
Cdd:cd04077 151 VAAGNSNQDACNYSPASAPEAITVGATDSDDARASFSNYGSCVDIFAPGVDILSAWIGSDTATATLSGTSMAAPHVAGLA 230

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6320775  530 TYFLSLQPgsdseffelgqdSLTPQQLKKKLIHYSTK 566
Cdd:cd04077 231 AYLLSLGP------------DLSPAEVKARLLNLATK 255
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 316-565 5.35e-77

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 252.71  E-value: 5.35e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDL-DGNGHGTHCAGTIASKH------YGVAKNANVVAVKVLRSNG 388
Cdd:COG1404 108 GAGVTVAVIDTGVDADHPDLAGRVVGGYDFVDGDGDPsDDNGHGTHVAGIIAANGnngggvAGVAPGAKLLPVRVLDDNG 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  389 SGTMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSLGG---GKSPALDLAVNAAVEVGIHFAVAAGNENQ-DACNTSP 464
Cdd:COG1404 188 SGTTSDIAAAIDWAADNGAD------------VINLSLGGpadGYSDALAAAVDYAVDKGVLVVAAAGNSGSdDATVSYP 255

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  465 ASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGLLTYFLSLQPgsdseff 544
Cdd:COG1404 256 AAYPNVIAVGAVDANGQLASFSNYGPKVDVAAPGVDILSTYPGGG--YATLSGTSMAAPHVAGAAALLLSANP------- 326

                       250       260
                ....*....|....*....|.
gi 6320775  545 elgqdSLTPQQLKKKLIHYST 565
Cdd:COG1404 327 -----DLTPAQVRAILLNTAT 342
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 316-562 4.86e-37

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: 139.90  E-value: 4.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    316 GRGVTSYVIDTGVNINHKDFEKR-------------AIWGKTIPLNDEDLDGNGHGTHCAGTIA------SKHYGVAKNA 376
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNldndpsddpeasvDFNNEWDDPRDDIDDKNGHGTHVAGIIAaggnnsIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    377 NVVAVKVLrSNGSGTMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSLGG----GKSPALDLAVNA---AVEVGIHFA 449
Cdd:pfam00082  81 KILGVRVF-GDGGGTDAITAQAISWAIPQGAD------------VINMSWGSdktdGGPGSWSAAVDQlggAEAAGSLFV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    450 VAAGNENQDACNTS----PASADKAITVGASTL--SDDRAYFSNWGKCV------DVFAPGLNILSTYIGSD-------- 509
Cdd:pfam00082 148 WAAGNGSPGGNNGSsvgyPAQYKNVIAVGAVDEasEGNLASFSSYGPTLdgrlkpDIVAPGGNITGGNISSTlltttsdp 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6320775    510 --DATATLSGTSMASPHVAGLLTYFLSLQPgsdseffelgqdSLTPQQLKKKLIH 562
Cdd:pfam00082 228 pnQGYDSMSGTSMATPHVAGAAALLKQAYP------------NLTPETLKALLVN 270
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 316-528 4.18e-26

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: 110.11  E-value: 4.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    316 GRGVTSYVIDTGVNiNHKDFEKRAIWGKT-IPLNDEDLDGNGHGTHCAGTIASKH------YGVAKNANVVAVKVL---- 384
Cdd:TIGR03921  12 GAGVTVAVIDTGVD-DHPRLPGLVLPGGDfVGSGDGTDDCDGHGTLVAGIIAGRPgegdgfSGVAPDARILPIRQTsaaf 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    385 ----RSNGSGTMSDVVKGVEYAAKahqkeaqekkkgfKGSTA-NMSL-------GGGKSPALDLAVNAAVEVGIHFAVAA 452
Cdd:TIGR03921  91 epdeGTSGVGDLGTLAKAIRRAAD-------------LGADViNISLvaclpagSGADDPELGAAVRYALDKGVVVVAAA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320775    453 GNENQDACNT---SPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGsDDATATLSGTSMASPHVAGL 528
Cdd:TIGR03921 158 GNTGGDGQKTtvvYPAWYPGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGENIVSLSPG-GDGLATTSGTSFAAPFVSGT 235
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 323-551 1.69e-13

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 73.46  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775   323 VIDTGVNINHKDFEK------RAIWGKTIPLNDED------------------LDGNGHGTHCAGTIASKH------YGV 372
Cdd:PTZ00262 322 VIDSGIDYNHPDLHDnidvnvKELHGRKGIDDDNNgnvddeyganfvnndggpMDDNYHGTHVSGIISAIGnnnigiVGV 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775   373 AKNANVVAVKVLRSNGSGTMSDVVKGVEYAAkahQKEAQEKKKGFkGSTANmslgggkSPALDLAVNAAVEVGIHFAVAA 452
Cdd:PTZ00262 402 DKRSKLIICKALDSHKLGRLGDMFKCFDYCI---SREAHMINGSF-SFDEY-------SGIFNESVKYLEEKGILFVVSA 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775   453 GNENQDA--------CNTS------PASA---DKAITVG--------ASTLSDDrAYFSNwgKCVDVFAPGLNILSTYig 507
Cdd:PTZ00262 471 SNCSHTKeskpdipkCDLDvnkvypPILSkklRNVITVSnlikdknnQYSLSPN-SFYSA--KYCQLAAPGTNIYSTF-- 545

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 6320775   508 SDDATATLSGTSMASPHVAGLLTYFLSLQPG-SDSEFFELGQDSL 551
Cdd:PTZ00262 546 PKNSYRKLNGTSMAAPHVAAIASLILSINPSlSYEEVIRILKESI 590
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 182-278 1.25e-10

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


Pssm-ID: 428674  Cd Length: 82  Bit Score: 58.07  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    182 RYIIVFKRGAPQEEIDFHKENVQQAQLQSVenlsaedaffistkdTSLSTSEAGGIQDSFNIdnLFSGYIGYFTQEIVDL 261
Cdd:pfam05922   1 TYIVYLKEGAAAADSFSSHTEWHSSLLRSV---------------LSEESSAEAGILYSYKI--GFNGFAAKLTEEEAEK 63

                          90
                  ....*....|....*..
gi 6320775    262 IRQNPLVDFVERDSIVE 278
Cdd:pfam05922  64 LRKHPEVVSVEPDQVVK 80
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 462-527 8.71e-08

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 55.56  E-value: 8.71e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320775    462 TSPASADKAITVGA-STLSDDRAYFSNWGKCV------DVFAPGLNILSTYIGSddATATLSGTSMASPHVAG 527
Cdd:NF040809  397 TVPGTASRVITVGSfNSRTDVVSVFSGEGDIEngiykpDLLAPGENIVSYLPGG--TTGALTGTSMATPHVTG 467
 
Name Accession Description Interval E-value
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 290-566 4.11e-147

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: 426.16  E-value: 4.11e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  290 WGLARISHRerlNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKH 369
Cdd:cd04077   1 WGLDRISQR---DLPLDGTYYYDSSTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDCNGHGTHVAGTVGGKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  370 YGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKeaqekkkGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFA 449
Cdd:cd04077  78 YGVAKKANLVAVKVLDCNGSGTLSGIIAGLEWVANDATK-------RGKPAVANMSLGGGASTALDAAVAAAVNAGVVVV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  450 VAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLL 529
Cdd:cd04077 151 VAAGNSNQDACNYSPASAPEAITVGATDSDDARASFSNYGSCVDIFAPGVDILSAWIGSDTATATLSGTSMAAPHVAGLA 230

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6320775  530 TYFLSLQPgsdseffelgqdSLTPQQLKKKLIHYSTK 566
Cdd:cd04077 231 AYLLSLGP------------DLSPAEVKARLLNLATK 255
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 316-565 5.35e-77

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 252.71  E-value: 5.35e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDL-DGNGHGTHCAGTIASKH------YGVAKNANVVAVKVLRSNG 388
Cdd:COG1404 108 GAGVTVAVIDTGVDADHPDLAGRVVGGYDFVDGDGDPsDDNGHGTHVAGIIAANGnngggvAGVAPGAKLLPVRVLDDNG 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  389 SGTMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSLGG---GKSPALDLAVNAAVEVGIHFAVAAGNENQ-DACNTSP 464
Cdd:COG1404 188 SGTTSDIAAAIDWAADNGAD------------VINLSLGGpadGYSDALAAAVDYAVDKGVLVVAAAGNSGSdDATVSYP 255

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  465 ASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGLLTYFLSLQPgsdseff 544
Cdd:COG1404 256 AAYPNVIAVGAVDANGQLASFSNYGPKVDVAAPGVDILSTYPGGG--YATLSGTSMAAPHVAGAAALLLSANP------- 326

                       250       260
                ....*....|....*....|.
gi 6320775  545 elgqdSLTPQQLKKKLIHYST 565
Cdd:COG1404 327 -----DLTPAQVRAILLNTAT 342
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 318-561 5.15e-59

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: 197.37  E-value: 5.15e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  318 GVTSYVIDTGVNINHKDFEKRAIWGKTI--PLNDEDLDGNGHGTHCAGTIASKHY-----GVAKNANVVAVKVLRSNGSG 390
Cdd:cd07477   1 GVKVAVIDTGIDSSHPDLKLNIVGGANFtgDDNNDYQDGNGHGTHVAGIIAALDNgvgvvGVAPEADLYAVKVLNDDGSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  391 TMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSLGGGK-SPALDLAVNAAVEVGIHFAVAAGNE-NQDACNTSPASAD 468
Cdd:cd07477  81 TYSDIIAGIEWAIENGMD------------IINMSLGGPSdSPALREAIKKAYAAGILVVAAAGNSgNGDSSYDYPAKYP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  469 KAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGLLTYFLSLQPgsdseffelgq 548
Cdd:cd07477 149 SVIAVGAVDSNNNRASFSSTGPEVELAAPGVDILSTYPNND--YAYLSGTSMATPHVAGVAALVWSKRP----------- 215

                       250
                ....*....|...
gi 6320775  549 dSLTPQQLKKKLI 561
Cdd:cd07477 216 -ELTNAQVRQALN 227
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 316-542 1.09e-56

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: 192.48  E-value: 1.09e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEK-RAIWGKTIPLNDED-LDGNGHGTHCAGTIASKH------YGVAKNANVVAVKVLRSN 387
Cdd:cd07484  27 GSGVTVAVVDTGVDPTHPDLLKvKFVLGYDFVDNDSDaMDDNGHGTHVAGIIAAATnngtgvAGVAPKAKIMPVKVLDAN 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  388 GSGTMSDVVKGVEYAAKahqkeaqekkKGFKgsTANMSLGGG-KSPALDLAVNAAVEVGIHFAVAAGNENQDACNTsPAS 466
Cdd:cd07484 107 GSGSLADIANGIRYAAD----------KGAK--VINLSLGGGlGSTALQEAINYAWNKGVVVVAAAGNEGVSSVSY-PAA 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320775  467 ADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGLLTYFLSLQPGSDSE 542
Cdd:cd07484 174 YPGAIAVAATDQDDKRASFSNYGKWVDVSAPGGGILSTTPDGD--YAYMSGTSMATPHVAGVAALLYSQGPLSASE 247
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 323-565 2.70e-55

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: 188.56  E-value: 2.70e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  323 VIDTGVNINHKDFEKRaIW--GKTIPLNDEDLDGNG----------------------HGTHCAGTIASKH------YGV 372
Cdd:cd07473   8 VIDTGVDYNHPDLKDN-MWvnPGEIPGNGIDDDGNGyvddiygwnfvnndndpmddngHGTHVAGIIGAVGnngigiAGV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  373 AKNANVVAVKVLRSNGSGTMSDVVKGVEYAakahqkeaqeKKKGFKGStaNMSLGGGK-SPALDLAVNAAVEVGIHFAVA 451
Cdd:cd07473  87 AWNVKIMPLKFLGADGSGTTSDAIKAIDYA----------VDMGAKII--NNSWGGGGpSQALRDAIARAIDAGILFVAA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  452 AGNE--NQDACNTSPASADKA--ITVGASTLSDDRAYFSNWG-KCVDVFAPGLNILSTYigSDDATATLSGTSMASPHVA 526
Cdd:cd07473 155 AGNDgtNNDKTPTYPASYDLDniISVAATDSNDALASFSNYGkKTVDLAAPGVDILSTS--PGGGYGYMSGTSMATPHVA 232

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6320775  527 GLLTYFLSLQPgsdseffelgqdSLTPQQLKKKLIHYST 565
Cdd:cd07473 233 GAAALLLSLNP------------NLTAAQIKDAILSSAD 259
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 316-561 1.57e-53

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: 183.94  E-value: 1.57e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAI----WGKTIPLNDEDLDGNGHGTHCAGTIAS-------KHYGVAKNANVVAVKVL 384
Cdd:cd07487   1 GKGITVAVLDTGIDAPHPDFDGRIIrfadFVNTVNGRTTPYDDNGHGTHVAGIIAGsgrasngKYKGVAPGANLVGVKVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  385 RSNGSGTMSDVVKGVEYAAKAHQKEaqekkkGFKGstANMSLGGGKSPA-----LDLAVNAAVEVGIHFAVAAGNENQDA 459
Cdd:cd07487  81 DDSGSGSESDIIAGIDWVVENNEKY------NIRV--VNLSLGAPPDPSygedpLCQAVERLWDAGIVVVVAAGNSGPGP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  460 CN-TSPASADKAITVGA----STLSDDRAYFSNWG---KCV---DVFAPGLNILSTY-------IGSDDATATLSGTSMA 521
Cdd:cd07487 153 GTiTSPGNSPKVITVGAvddnGPHDDGISYFSSRGptgDGRikpDVVAPGENIVSCRspggnpgAGVGSGYFEMSGTSMA 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 6320775  522 SPHVAGLLTYFLSLQPgsdseffelgqdSLTPQQLKKKLI 561
Cdd:cd07487 233 TPHVSGAIALLLQANP------------ILTPDEVKCILR 260
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 319-562 3.64e-51

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: 177.01  E-value: 3.64e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  319 VTSYVIDTGVNINHKDFEKRAIWGKT-------IPLNDEDLDGNGHGTHCAGTIASKH-----YGVAKNANVVAVKVLRS 386
Cdd:cd00306   1 VTVAVIDTGVDPDHPDLDGLFGGGDGgnddddnENGPTDPDDGNGHGTHVAGIIAASAnngggVGVAPGAKLIPVKVLDG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  387 NGSGTMSDVVKGVEYAAKAHqkeaqekkkgfKGSTANMSLGGG---KSPALDLAVNAAVE-VGIHFAVAAGNENQDACNT 462
Cdd:cd00306  81 DGSGSSSDIAAAIDYAAADQ-----------GADVINLSLGGPgspPSSALSEAIDYALAkLGVLVVAAAGNDGPDGGTN 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  463 --SPASADKAITVGASTLSDDRA-YFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLLTYFLSLQPgs 539
Cdd:cd00306 150 igYPAASPNVIAVGAVDRDGTPAsPSSNGGAGVDIAAPGGDILSSPTTGGGGYATLSGTSMAAPIVAGVAALLLSANP-- 227

                       250       260
                ....*....|....*....|...
gi 6320775  540 dseffelgqdSLTPQQLKKKLIH 562
Cdd:cd00306 228 ----------DLTPAQVKAALLS 240
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 316-561 6.88e-42

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


Pssm-ID: 173800 [Multi-domain]  Cd Length: 295  Bit Score: 153.25  E-value: 6.88e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKR----------------------AIWGKTIPLNDEDLDGNGHGTHCAGTIA------S 367
Cdd:cd07474   1 GKGVKVAVIDTGIDYTHPDLGGPgfpndkvkggydfvdddydpmdTRPYPSPLGDASAGDATGHGTHVAGIIAgngvnvG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  368 KHYGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQkeaqekkkgfkgSTANMSLGGGKSPALD---LAVNAAVEV 444
Cdd:cd07474  81 TIKGVAPKADLYAYKVLGPGGSGTTDVIIAAIEQAVDDGM------------DVINLSLGSSVNGPDDpdaIAINNAVKA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  445 GIHFAVAAGNeNQDACNT--SPASADKAITVGAST-----LSDDRAYFS-------NWGKCVDVFAPGLNILSTYIGSDD 510
Cdd:cd07474 149 GVVVVAAAGN-SGPAPYTigSPATAPSAITVGASTvadvaEADTVGPSSsrgpptsDSAIKPDIVAPGVDIMSTAPGSGT 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6320775  511 ATATLSGTSMASPHVAGLLTYFLSLQPgsdseffelgqdSLTPQQLKKKLI 561
Cdd:cd07474 228 GYARMSGTSMAAPHVAGAAALLKQAHP------------DWSPAQIKAALM 266
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 318-560 5.83e-41

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: 150.52  E-value: 5.83e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  318 GVTSYVIDTGVNINHKDFEKRAI---------------------------WGKTIPLNDEDLDGNG------HGTHCAGT 364
Cdd:cd07496   1 GVVVAVLDTGVLFHHPDLAGVLLpgydfisdpaiandgdgrdsdptdpgdWVTGDDVPPGGFCGSGvspsswHGTHVAGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  365 IASKH------YGVAKNANVVAVKVLRSNGsGTMSDVVKGVEYAAkahqkeaqekkkGFK--GSTA--------NMSLG- 427
Cdd:cd07496  81 IAAVTnngvgvAGVAWGARILPVRVLGKCG-GTLSDIVDGMRWAA------------GLPvpGVPVnpnpakviNLSLGg 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  428 -GGKSPALDLAVNAAVEVGIHFAVAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILST-- 504
Cdd:cd07496 148 dGACSATMQNAINDVRARGVLVVVAAGNEGSSASVDAPANCRGVIAVGATDLRGQRASYSNYGPAVDVSAPGGDCASDvn 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320775  505 ---YIGSDDATAT--------LSGTSMASPHVAGLLTYFLSLQPgsdseffelgqdSLTPQQLKKKL 560
Cdd:cd07496 228 gdgYPDSNTGTTSpggstygfLQGTSMAAPHVAGVAALMKSVNP------------SLTPAQIESLL 282
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 316-562 4.86e-37

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: 139.90  E-value: 4.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    316 GRGVTSYVIDTGVNINHKDFEKR-------------AIWGKTIPLNDEDLDGNGHGTHCAGTIA------SKHYGVAKNA 376
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNldndpsddpeasvDFNNEWDDPRDDIDDKNGHGTHVAGIIAaggnnsIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    377 NVVAVKVLrSNGSGTMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSLGG----GKSPALDLAVNA---AVEVGIHFA 449
Cdd:pfam00082  81 KILGVRVF-GDGGGTDAITAQAISWAIPQGAD------------VINMSWGSdktdGGPGSWSAAVDQlggAEAAGSLFV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    450 VAAGNENQDACNTS----PASADKAITVGASTL--SDDRAYFSNWGKCV------DVFAPGLNILSTYIGSD-------- 509
Cdd:pfam00082 148 WAAGNGSPGGNNGSsvgyPAQYKNVIAVGAVDEasEGNLASFSSYGPTLdgrlkpDIVAPGGNITGGNISSTlltttsdp 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6320775    510 --DATATLSGTSMASPHVAGLLTYFLSLQPgsdseffelgqdSLTPQQLKKKLIH 562
Cdd:pfam00082 228 pnQGYDSMSGTSMATPHVAGAAALLKQAYP------------NLTPETLKALLVN 270
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 319-562 1.65e-36

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: 136.70  E-value: 1.65e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  319 VTSYVIDTGVNINHKDFekrAIWGKTIP------LNDEDLDGNGHGTHCAGTIASKHY------GVAKNANVVAVKVLRS 386
Cdd:cd07498   1 VVVAIIDTGVDLNHPDL---SGKPKLVPgwnfvsNNDPTSDIDGHGTACAGVAAAVGNnglgvaGVAPGAKLMPVRIADS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  387 NGSGTMSDVVKGVEYAAkahQKEAqekkkgfkgSTANMSLGG-GKSPALDLAVNAAVE-----VGIHFAVAAGNENQDAc 460
Cdd:cd07498  78 LGYAYWSDIAQAITWAA---DNGA---------DVISNSWGGsDSTESISSAIDNAATygrngKGGVVLFAAGNSGRSV- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  461 NTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIG-------SDDATATLSGTSMASPHVAGLLTYFL 533
Cdd:cd07498 145 SSGYAANPSVIAVAATDSNDARASYSNYGNYVDLVAPGVGIWTTGTGrgsagdyPGGGYGSFSGTSFASPVAAGVAALIL 224

                       250       260
                ....*....|....*....|....*....
gi 6320775  534 SLQPgsdseffelgqdSLTPQQLKKKLIH 562
Cdd:cd07498 225 SANP------------NLTPAEVEDILTS 241
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 318-560 7.11e-34

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: 129.98  E-value: 7.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  318 GVTSYVIDTGVNINHKDFEKR-AIW-----GKTIPLNDEDlDGNGHGTHCAGTIA-----SKHYGVAKNANVVAVKVLrS 386
Cdd:cd07490   1 GVTVAVLDTGVDADHPDLAGRvAQWadfdeNRRISATEVF-DAGGHGTHVSGTIGgggakGVYIGVAPEADLLHGKVL-D 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  387 NGSGTMSDVVKGVEYAAKahqKEAqekkkgfkgSTANMSLGGGKSPA--LDLAVNA-AVEVGIHFAVAAGNENQDAcNTS 463
Cdd:cd07490  79 DGGGSLSQIIAGMEWAVE---KDA---------DVVSMSLGGTYYSEdpLEEAVEAlSNQTGALFVVSAGNEGHGT-SGS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  464 PASADKAITVGASTLSDDRAYFSNWGKCV-----------------DVFAPGLNILSTYIGS--DDATATLSGTSMASPH 524
Cdd:cd07490 146 PGSAYAALSVGAVDRDDEDAWFSSFGSSGaslvsapdsppdeytkpDVAAPGVDVYSARQGAngDGQYTRLSGTSMAAPH 225

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 6320775  525 VAGLLTYFLSLQPgsdseffelgqdSLTPQQLKKKL 560
Cdd:cd07490 226 VAGVAALLAAAHP------------DLSPEQIKDAL 249
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
 352-537 8.17e-32

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: 125.40  E-value: 8.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  352 LDGNGHGTHCAGTIASKHY--------------GVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAhqkeaqekkkgf 417
Cdd:cd04852 105 RDYDGHGTHTASTAAGNVVvnasvggfafgtasGVAPRARIAVYKVCWPDGGCFGSDILAAIDQAIAD------------ 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  418 kGSTA-NMSLGGGKSP----ALDLAVNAAVEVGIHFAVAAGNENQDAcNTSPASADKAITVGASTLSddrayfsnwgkcV 492
Cdd:cd04852 173 -GVDViSYSIGGGSPDpyedPIAIAFLHAVEAGIFVAASAGNSGPGA-STVPNVAPWVTTVAASTLK------------P 238

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6320775  493 DVFAPGLNILSTYIGSDDAT--------ATLSGTSMASPHVAGLLTYFLSLQP 537
Cdd:cd04852 239 DIAAPGVDILAAWTPEGADPgdargedfAFISGTSMASPHVAGVAALLKSAHP 291
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 316-539 7.77e-31

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: 122.71  E-value: 7.77e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHK----------------DFEKRAIWGKTIPLNDED-LDGNGHGTHCAGTIA--SKHY---GVA 373
Cdd:cd07489  12 GKGVKVAVVDTGIDYTHPalggcfgpgckvaggyDFVGDDYDGTNPPVPDDDpMDCQGHGTHVAGIIAanPNAYgftGVA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  374 KNANVVAVKVLRSNGSGTmSDVVkgVEYAAKAHQKEAQekkkgfkgsTANMSLGG--GKSP-ALDLAVNAAVEVGIHFAV 450
Cdd:cd07489  92 PEATLGAYRVFGCSGSTT-EDTI--IAAFLRAYEDGAD---------VITASLGGpsGWSEdPWAVVASRIVDAGVVVTI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  451 AAGNENQD--ACNTSPASADKAITVGAStlsddRAYFSNWGKCVD------VFAPGLNILSTYIGSDDATATLSGTSMAS 522
Cdd:cd07489 160 AAGNDGERgpFYASSPASGRGVIAVASV-----DSYFSSWGPTNElylkpdVAAPGGNILSTYPLAGGGYAVLSGTSMAT 234

                       250
                ....*....|....*..
gi 6320775  523 PHVAGLLTYFLSLQPGS 539
Cdd:cd07489 235 PYVAGAAALLIQARHGK 251
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 316-527 9.29e-30

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: 119.40  E-value: 9.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIA-----SKHYGVAKNANVVAVKVLRSNGSG 390
Cdd:cd07480   7 GAGVRVAVLDTGIDLTHPAFAGRDITTKSFVGGEDVQDGHGHGTHCAGTIFgrdvpGPRYGVARGAEIALIGKVLGDGGG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  391 TMSDVVKGVEYAAkAHQKEaqekkkgfkgsTANMSLGG--------GKSPALD---------------------LAVNAA 441
Cdd:cd07480  87 GDGGILAGIQWAV-ANGAD-----------VISMSLGAdfpglvdqGWPPGLAfsraleayrqrarlfdalmtlVAAQAA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  442 VEVGIHFAVAAGNENQDACNTSP---ASADKAITVGASTLSDDR-------AYFSNWGkcVDVFAPGLNILSTYIGSddA 511
Cdd:cd07480 155 LARGTLIVAAAGNESQRPAGIPPvgnPAACPSAMGVAAVGALGRtgnfsavANFSNGE--VDIAAPGVDIVSAAPGG--G 230

                       250
                ....*....|....*.
gi 6320775  512 TATLSGTSMASPHVAG 527
Cdd:cd07480 231 YRSMSGTSMATPHVAG 246
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 306-528 1.05e-29

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: 120.45  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  306 FNKYLYDddaGRGVTSYVIDTGVNINHKDF-----------------EKRAIWGKTIPLND----------------EDL 352
Cdd:cd07475   3 WDKGGYK---GEGMVVAVIDSGVDPTHDAFrldddskakyseefeakKKKAGIGYGKYYNEkvpfaynyadnnddilDED 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  353 DGNGHGTHCAGTIA---------SKHYGVAKNANVVAVKVLRSNGSGTM--SDVVKGVEYAAKahqkeaqekkkgFKGST 421
Cdd:cd07475  80 DGSSHGMHVAGIVAgngdeedngEGIKGVAPEAQLLAMKVFSNPEGGSTydDAYAKAIEDAVK------------LGADV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  422 ANMSLGGG-----KSPALDLAVNAAVEVGIHFAVAAGNE--------------NQDACNT-SPASADKAITVGASTLSDD 481
Cdd:cd07475 148 INMSLGSTagfvdLDDPEQQAIKRAREAGVVVVVAAGNDgnsgsgtskplatnNPDTGTVgSPATADDVLTVASANKKVP 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320775  482 R------AYFSNWGKCV------DVFAPGLNILSTYIgsDDATATLSGTSMASPHVAGL 528
Cdd:cd07475 228 NpnggqmSGFSSWGPTPdldlkpDITAPGGNIYSTVN--DNTYGYMSGTSMASPHVAGA 284
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 316-538 1.82e-28

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: 114.78  E-value: 1.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDF-EKRAIWGKTI---------PLNDEDL--DGNGHGTHCAGTIASKH-----YGVAKNANV 378
Cdd:cd07481   1 GTGIVVANIDTGVDWTHPALkNKYRGWGGGSadhdynwfdPVGNTPLpyDDNGHGTHTMGTMVGNDgdgqqIGVAPGARW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  379 VAVKVLRSNGsGTMSDVVKGVEYAAKAHQKEAQEKKKGFKGSTANMSLGG--GKSPALDLAVNAAVEVGIHFAVAAGNEN 456
Cdd:cd07481  81 IACRALDRNG-GNDADYLRCAQWMLAPTDSAGNPADPDLAPDVINNSWGGpsGDNEWLQPAVAAWRAAGIFPVFAAGNDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  457 QD--ACNTSPASADKAITVGASTLSDDRAYFSNWGKCV------DVFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGL 528
Cdd:cd07481 160 PRcsTLNAPPANYPESFAVGATDRNDVLADFSSRGPSTygrikpDISAPGVNIRSAVPGGG--YGSSSGTSMAAPHVAGV 237

                       250
                ....*....|
gi 6320775  529 LTYFLSLQPG 538
Cdd:cd07481 238 AALLWSANPS 247
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 316-560 6.03e-28

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: 113.35  E-value: 6.03e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEK-------RAIWGKTIP------LNDEDLDGNGHGTHCAGTIASK------------HY 370
Cdd:cd07485   9 GPGIIVAVVDTGVDGTHPDLQGngdgdgyDPAVNGYNFvpnvgdIDNDVSVGGGHGTHVAGTIAAVnnngggvggiagAG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  371 GVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKEAQEKKKGFKGSTANMSLgggkSPALDLAVNAA---VEVGIH 447
Cdd:cd07485  89 GVAPGVKIMSIQIFAGRYYVGDDAVAAAIVYAADNGAVILQNSWGGTGGGIYSPLL----KDAFDYFIENAggsPLDGGI 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  448 FAVAAGNENqDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLN-ILSTYI---GSDDAT-ATLSGTSMAS 522
Cdd:cd07485 165 VVFSAGNSY-TDEHRFPAAYPGVIAVAALDTNDNKASFSNYGRWVDIAAPGVGtILSTVPkldGDGGGNyEYLSGTSMAA 243

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6320775  523 PHVAGLLTYFLSLQPgsdseffelgqDSLTPQQLKKKL 560
Cdd:cd07485 244 PHVSGVAALVLSKFP-----------DVFTPEQIRKLL 270
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 316-528 4.18e-26

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: 110.11  E-value: 4.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    316 GRGVTSYVIDTGVNiNHKDFEKRAIWGKT-IPLNDEDLDGNGHGTHCAGTIASKH------YGVAKNANVVAVKVL---- 384
Cdd:TIGR03921  12 GAGVTVAVIDTGVD-DHPRLPGLVLPGGDfVGSGDGTDDCDGHGTLVAGIIAGRPgegdgfSGVAPDARILPIRQTsaaf 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    385 ----RSNGSGTMSDVVKGVEYAAKahqkeaqekkkgfKGSTA-NMSL-------GGGKSPALDLAVNAAVEVGIHFAVAA 452
Cdd:TIGR03921  91 epdeGTSGVGDLGTLAKAIRRAAD-------------LGADViNISLvaclpagSGADDPELGAAVRYALDKGVVVVAAA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320775    453 GNENQDACNT---SPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGsDDATATLSGTSMASPHVAGL 528
Cdd:TIGR03921 158 GNTGGDGQKTtvvYPAWYPGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGENIVSLSPG-GDGLATTSGTSFAAPFVSGT 235
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 316-529 1.66e-25

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: 106.25  E-value: 1.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAIWG-----KTIPLNDEDLDGNGHGTHCAGTIASKH-----YGVAKNANVVAVKVLR 385
Cdd:cd04848   2 GAGVKVGVIDSGIDLSHPEFAGRVSEAsyyvaVNDAGYASNGDGDSHGTHVAGVIAAARdgggmHGVAPDATLYSARASA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  386 SNGSGTMSDVVKGVEYAAKAH-----------QKEAQEKKKGFKGSTANmslgggKSPALDLAVNAAVEVGIHFAVAAGN 454
Cdd:cd04848  82 SAGSTFSDADIAAAYDFLAASgvriinnswggNPAIDTVSTTYKGSAAT------QGNTLLAALARAANAGGLFVFAAGN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  455 ENQD----ACNTSPASADKA----ITVGASTLSDDRAYFS---------NWGkcvdVFAPGLNILSTYIGSDDATATLSG 517
Cdd:cd04848 156 DGQAnpslAAAALPYLEPELeggwIAVVAVDPNGTIASYSysnrcgvaaNWC----LAAPGENIYSTDPDGGNGYGRVSG 231

                       250
                ....*....|..
gi 6320775  518 TSMASPHVAGLL 529
Cdd:cd04848 232 TSFAAPHVSGAA 243
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 318-560 3.03e-24

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: 101.26  E-value: 3.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  318 GVTSYVIDTGVNINHKDFEKRA------IWGKTIPLNDEDLDGNGHGTHCAGTIASKhygvAKNANVVAVKVLRSNGSGT 391
Cdd:cd07492   1 GVRVAVIDSGVDTDHPDLGNLAldgevtIDLEIIVVSAEGGDKDGHGTACAGIIKKY----APEAEIGSIKILGEDGRCN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  392 MSDVVKGVEYAAkahqkeaqekKKGFKgsTANMSLGGG---KSPALDLAVNAAVEVGIHFAVAAGNENQDAcnTSPASAD 468
Cdd:cd07492  77 SFVLEKALRACV----------ENDIR--IVNLSLGGPgdrDFPLLKELLEYAYKAGGIIVAAAPNNNDIG--TPPASFP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  469 KAITVGASTLSDDRayfSNWGKCVDVFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGLLTYFLSLQPGsdseffelgq 548
Cdd:cd07492 143 NVIGVKSDTADDPK---SFWYIYVEFSADGVDIIAPAPHGR--YLTVSGNSFAAPHVTGMVALLLSEKPD---------- 207

                       250
                ....*....|..
gi 6320775  549 dsLTPQQLKKKL 560
Cdd:cd07492 208 --IDANDLKRLL 217
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 319-535 3.15e-24

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: 103.21  E-value: 3.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  319 VTSYVIDTGVNINHKDFeKRAIW--GKTIPLNDEDLDGNG---------------------------------------- 356
Cdd:cd07483   3 VIVAVLDSGVDIDHEDL-KGKLWinKKEIPGNGIDDDNNGyiddvngwnflgqydprrivgddpydltekgygnndvngp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  357 -----HGTHCAGTIASKHY---GVAKNANVVAVKVLR--SNGSGTMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSL 426
Cdd:cd07483  82 isdadHGTHVAGIIAAVRDngiGIDGVADNVKIMPLRivPNGDERDKDIANAIRYAVDNGAK------------VINMSF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  427 GGGKSP---ALDLAVNAAVEVGIHFAVAAGNENQDACNT----------SPASADKAITVGASTLSDDR---AYFSNWGK 490
Cdd:cd07483 150 GKSFSPnkeWVDDAIKYAESKGVLIVHAAGNDGLDLDITpnfpndydknGGEPANNFITVGASSKKYENnlvANFSNYGK 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6320775  491 -CVDVFAPGLNILSTYigSDDATATLSGTSMASPHVAGL----LTYFLSL 535
Cdd:cd07483 230 kNVDVFAPGERIYSTT--PDNEYETDSGTSMAAPVVSGVaaliWSYYPNL 277
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 316-530 7.21e-23

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: 99.33  E-value: 7.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAIWG---------KTIPLNDEDLDGNGHGTHCAGTIASKHY---------GVAKNAN 377
Cdd:cd04842   6 GKGQIVGVADTGLDTNHCFFYDPNFNKtnlfhrkivRYDSLSDTKDDVDGHGTHVAGIIAGKGNdsssislykGVAPKAK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  378 VVAVKVlrSNGSGTMSDVVKGVEYAAKAHQKEAQekkkgfkgsTANMSLGGGKSP-------ALDLAVNAAVEvgIHFAV 450
Cdd:cd04842  86 LYFQDI--GDTSGNLSSPPDLNKLFSPMYDAGAR---------ISSNSWGSPVNNgytllarAYDQFAYNNPD--ILFVF 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  451 AAGNENQDACNT--SPASADKAITVGAST---------------LSDDRAYFSNWGKCV------DVFAPGLNILSTYIG 507
Cdd:cd04842 153 SAGNDGNDGSNTigSPATAKNVLTVGASNnpsvsngegglgqsdNSDTVASFSSRGPTYdgrikpDLVAPGTGILSARSG 232

                       250       260       270
                ....*....|....*....|....*....|
gi 6320775  508 -------SDDATATLSGTSMASPHVAGLLT 530
Cdd:cd04842 233 gggigdtSDSAYTSKSGTSMATPLVAGAAA 262
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 319-529 2.40e-21

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: 94.74  E-value: 2.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  319 VTSYVIDTGVNINH-----------KDFEKRAIWGKTIPLNDEDL----DGNGHGTHCAGTIAS--KHYGVAKNANVVAV 381
Cdd:cd07482   2 VTVAVIDSGIDPDHpdlknsissysKNLVPKGGYDGKEAGETGDIndivDKLGHGTAVAGQIAAngNIKGVAPGIGIVSY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  382 KVLRSNGSGTMSDVVKGVEYAAKAHQKeaqekkkgfkgsTANMSLGG----GKSPALDL--------AVNAAVEVGIHFA 449
Cdd:cd07482  82 RVFGSCGSAESSWIIKAIIDAADDGVD------------VINLSLGGyliiGGEYEDDDveynaykkAINYAKSKGSIVV 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  450 VAAGNENQDACNTS---------------------PASADKAITVGASTLSDDRAYFSNWGKC-VDVFAPG--------- 498
Cdd:cd07482 150 AAAGNDGLDVSNKQelldflssgddfsvngevydvPASLPNVITVSATDNNGNLSSFSNYGNSrIDLAAPGgdfllldqy 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 6320775  499 -------------LNILSTYIGSDDATATlsGTSMASPHVAGLL 529
Cdd:cd07482 230 gkekwvnnglmtkEQILTTAPEGGYAYMY--GTSLAAPKVSGAL 271
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
 323-529 2.39e-17

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: 81.95  E-value: 2.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  323 VIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNgHGTHCAGTIASK---HYGVAKNANVVAVKVLRSNGS---GTMSDVV 396
Cdd:cd05561   5 MIDTGIDTAHPALSAVVIARLFFAGPGAPAPSA-HGTAVASLLAGAgaqRPGLLPGADLYGADVFGRAGGgegASALALA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  397 KGVEYAAKAhqkeaqekkkgfKGSTANMSLGGGKSPALDLAVNAAVEVGIHFAVAAGNENQDACNTSPASADKAITVGAs 476
Cdd:cd05561  84 RALDWLAEQ------------GVRVVNISLAGPPNALLAAAVAAAAARGMVLVAAAGNDGPAAPPLYPAAYPGVIAVTA- 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6320775  477 TLSDDRAY-FSNWGKCVDVFAPGLNILSTyiGSDDATATLSGTSMASPHVAGLL 529
Cdd:cd05561 151 VDARGRLYrEANRGAHVDFAAPGVDVWVA--APGGGYRYVSGTSFAAPFVTAAL 202
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 316-527 1.33e-16

Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.


Pssm-ID: 173789 [Multi-domain]  Cd Length: 297  Bit Score: 80.68  E-value: 1.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLD-------GNGHGTHCAGTIASK--HY----GVAKNANVVAVK 382
Cdd:cd04059  38 GKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDptpryddDNSHGTRCAGEIAAVgnNGicgvGVAPGAKLGGIR 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  383 VLrsngSGTMSDVVKgveyaAKAHQKEAQekkkgfKGSTANMSLG----GGKSPALDLAVNAAVEVGIH---------FA 449
Cdd:cd04059 118 ML----DGDVTDVVE-----AESLGLNPD------YIDIYSNSWGpdddGKTVDGPGPLAQRALENGVTngrngkgsiFV 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  450 VAAGN--ENQDACNTSPASADK-AITVGASTLSDDRAYFSNWGKCVDVFAPG-------LNILSTYI-GSDDATATLSGT 518
Cdd:cd04059 183 WAAGNggNLGDNCNCDGYNNSIyTISVSAVTANGVRASYSEVGSSVLASAPSggsgnpeASIVTTDLgGNCNCTSSHNGT 262


                ....*....
gi 6320775  519 SMASPHVAG 527
Cdd:cd04059 263 SAAAPLAAG 271
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 323-551 1.69e-13

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 73.46  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775   323 VIDTGVNINHKDFEK------RAIWGKTIPLNDED------------------LDGNGHGTHCAGTIASKH------YGV 372
Cdd:PTZ00262 322 VIDSGIDYNHPDLHDnidvnvKELHGRKGIDDDNNgnvddeyganfvnndggpMDDNYHGTHVSGIISAIGnnnigiVGV 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775   373 AKNANVVAVKVLRSNGSGTMSDVVKGVEYAAkahQKEAQEKKKGFkGSTANmslgggkSPALDLAVNAAVEVGIHFAVAA 452
Cdd:PTZ00262 402 DKRSKLIICKALDSHKLGRLGDMFKCFDYCI---SREAHMINGSF-SFDEY-------SGIFNESVKYLEEKGILFVVSA 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775   453 GNENQDA--------CNTS------PASA---DKAITVG--------ASTLSDDrAYFSNwgKCVDVFAPGLNILSTYig 507
Cdd:PTZ00262 471 SNCSHTKeskpdipkCDLDvnkvypPILSkklRNVITVSnlikdknnQYSLSPN-SFYSA--KYCQLAAPGTNIYSTF-- 545

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 6320775   508 SDDATATLSGTSMASPHVAGLLTYFLSLQPG-SDSEFFELGQDSL 551
Cdd:PTZ00262 546 PKNSYRKLNGTSMAAPHVAAIASLILSINPSlSYEEVIRILKESI 590
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 315-562 9.78e-13

Peptidase S8 family domain, uncharacterized subfamily 11; 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: 173792  Cd Length: 277  Bit Score: 68.88  E-value: 9.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  315 AGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDgngHGTHCAGTIASKH--YGVAKNANVVAVKVLRSNGSGTM 392
Cdd:cd04843  14 SGQGVTFVDIEQGWNLNHEDLVGNGITLISGLTDQADSD---HGTAVLGIIVAKDngIGVTGIAHGAQAAVVSSTRVSNT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  393 SDVVKgveyAAKAH-------QKEAQEKKKGFKGSTANMSLgggkSPALDLAVNAAVEVGIHFAVAAGNENQD------- 458
Cdd:cd04843  91 ADAIL----DAADYlspgdviLLEMQTGGPNNGYPPLPVEY----EQANFDAIRTATDLGIIVVEAAGNGGQDldapvyn 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  459 -ACNTSPASADK----AITVGA--STLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDA--------TATLSGTSMASP 523
Cdd:cd04843 163 rGPILNRFSPDFrdsgAIMVGAgsSTTGHTRLAFSNYGSRVDVYGWGENVTTTGYGDLQDlggenqdyTDSFSGTSSASP 242

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6320775  524 HVAGLLtyfLSLQpgsdSEFFELGQDSLTPQQLKKKLIH 562
Cdd:cd04843 243 IVAGAA---ASIQ----GIAKQKGGTPLTPIEMRELLTA 274
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 318-557 1.00e-11

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


Pssm-ID: 173818 [Multi-domain]  Cd Length: 261  Bit Score: 65.79  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  318 GVTSYVIDTGVNINHKDFEKRAIWGK---------TIPLNDEDLDGNGHGTHC----AGTIASKHYGVAKNANVVavkVL 384
Cdd:cd07493   1 GITIAVIDAGFPKVHEAFAFKHLFKNlrilgeydfVDNSNNTNYTDDDHGTAVlstmAGYTPGVMVGTAPNASYY---LA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  385 RSNGSGTMSDV-----VKGVEYAAKAhqkeaqekkkgfkGST-ANMSLG----------------GGKSPALDLAVNAAV 442
Cdd:cd07493  78 RTEDVASETPVeednwVAAAEWADSL-------------GVDiISSSLGyttfdnptysytyadmDGKTSFISRAANIAA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  443 EVGIHFAVAAGNENQDACN--TSPASADKAITVGASTLSDDRAYFSNWGKCVD------VFAPGLNIlsTYIGSDDATAT 514
Cdd:cd07493 145 SKGMLVVNSAGNEGSTQWKgiGAPADAENVLSVGAVDANGNKASFSSIGPTADgrlkpdVMALGTGI--YVINGDGNITY 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 6320775  515 LSGTSMASPHVAGLLTYFLSLQPgsdseffelgqdSLTPQQLK 557
Cdd:cd07493 223 ANGTSFSCPLIAGLIACLWQAHP------------NWTNLQIK 253
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 316-528 1.06e-11

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: 67.26  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFEKR-------AIWGKTIP----------------------LNDEDL-------DGNGHGT 359
Cdd:cd07478   3 GKGVLVGIIDTGIDYLHPEFRNEdgttrilYIWDQTIPggpppggyygggeyteeiinaaLASDNPydivpsrDENGHGT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  360 HCAGTIA------SKHYGVAKNANVVAVKVLRSNGSGT----------MSDVVKGVEYAAKAhqkeAQEKKKGFkgsTAN 423
Cdd:cd07478  83 HVAGIAAgngdnnPDFKGVAPEAELIVVKLKQAKKYLRefyedvpfyqETDIMLAIKYLYDK----ALELNKPL---VIN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  424 MSLG------GGKSPaLDLAVNAAVEV-GIHFAVAAGNE--------------------------NQDACN--------- 461
Cdd:cd07478 156 ISLGtnfgshDGTSL-LERYIDAISRLrGIAVVVGAGNEgntqhhhsggivpngetktvelnvgeGEKGFNleiwgdfpd 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775      --------------------------------------------------------------------------------
Cdd:cd07478 235 rfsvsiispsgessgrinpgiggsesykfvfegttvyvyyylpepytgdqlifirfknikpgiwkirltgvsitdgrfda 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  462 -----------------------TSPASADKAITVGA-STLSDDRAYFS-------NWGKcVDVFAPGLNILSTYIGSDd 510
Cdd:cd07478 315 wlpsrgllsentrflepdpyttlTIPGTARSVITVGAyNQNNNSIAIFSgrgptrdGRIK-PDIAAPGVNILTASPGGG- 392

                       410
                ....*....|....*...
gi 6320775  511 aTATLSGTSMASPHVAGL 528
Cdd:cd07478 393 -YTTRSGTSVAAAIVAGA 409
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 316-566 1.99e-11

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: 64.78  E-value: 1.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKDFekRAIWGKTIPLNDEDL-DGNGHGTHCAGTIASKH---YGVAKNANVVAVKVLRSNGSGT 391
Cdd:cd07479   7 GAGVKVAVFDTGLAKDHPHF--RNVKERTNWTNEKTLdDGLGHGTFVAGVIASSReqcLGFAPDAEIYIFRVFTNNQVSY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  392 MSDVVKGVEYAAKAhqkeaqekkkgfKGSTANMSLGGGK---SPALDlAVNAAVEVGIHFAVAAGNENQ--DACNtSPAS 466
Cdd:cd07479  85 TSWFLDAFNYAILT------------KIDVLNLSIGGPDfmdKPFVD-KVWELTANNIIMVSAIGNDGPlyGTLN-NPAD 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  467 ADKAITVGASTLSDDRAYFSNWGKCV------------DVFAPGLNILSTYIgsDDATATLSGTSMASPHVAGLLTYFLS 534
Cdd:cd07479 151 QMDVIGVGGIDFDDNIARFSSRGMTTwelpggygrvkpDIVTYGSGVYGSKL--KGGCRALSGTSVASPVVAGAVALLLS 228

                       250       260       270
                ....*....|....*....|....*....|..
gi 6320775  535 LQPGSdseffelgQDSLTPQQLKKKLIHYSTK 566
Cdd:cd07479 229 TVPEK--------RDLINPASMKQALIESATR 252
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 323-542 6.82e-11

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: 63.48  E-value: 6.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  323 VIDTGVNINHKDFEKR-AIWGKTIPLNDEDLDGNGHGTHCAGTIAskhYGVAKNAN---------VVAVKVLRSNGSGT- 391
Cdd:cd04847   5 VLDSGINRGHPLLAPAlAEDDLDSDEPGWTADDLGHGTAVAGLAL---YGDLTLPGnglprpgcrLESVRVLPPNGENDp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  392 ---MSDVVKGVEYAAKAHqkeaQEKKKGFkgstaNMSLG-------GGKSP---ALDlavNAAVEVGIHFAVAAGN---- 454
Cdd:cd04847  82 elyGDITLRAIRRAVIQN----PDIVRVF-----NLSLGsplpiddGRPSSwaaALD---QLAAEYDVLFVVSAGNlgdd 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  455 -------ENQDACNTSPASADKAITVGAST---LSDDRAYFSN-------------WGK--CV--DVFAPGLNIL----- 502
Cdd:cd04847 150 daadgppRIQDDEIEDPADSVNALTVGAITsddDITDRARYSAvgpapagattssgPGSpgPIkpDVVAFGGNLAydpsg 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6320775  503 -----------STYIGSDDATATLSGTSMASPHVAGLLTYFLSLQPGSDSE 542
Cdd:cd04847 230 naadgdlslltTLSSPSGGGFVTVGGTSFAAPLAARLAAGLFAELPELSPE 280
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 182-278 1.25e-10

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


Pssm-ID: 428674  Cd Length: 82  Bit Score: 58.07  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775    182 RYIIVFKRGAPQEEIDFHKENVQQAQLQSVenlsaedaffistkdTSLSTSEAGGIQDSFNIdnLFSGYIGYFTQEIVDL 261
Cdd:pfam05922   1 TYIVYLKEGAAAADSFSSHTEWHSSLLRSV---------------LSEESSAEAGILYSYKI--GFNGFAAKLTEEEAEK 63

                          90
                  ....*....|....*..
gi 6320775    262 IRQNPLVDFVERDSIVE 278
Cdd:pfam05922  64 LRKHPEVVSVEPDQVVK 80
Peptidases_S8_thiazoline_oxidase_subtilisin-like_p cd07476
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ...
 319-536 5.10e-10

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


Pssm-ID: 173802 [Multi-domain]  Cd Length: 267  Bit Score: 60.81  E-value: 5.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  319 VTSYVIDTGVNINHKDFEKRAI------WGKTIPlndeDLDGNGHGTHCAGTIASKH----YGVAKNANVVAVKVLRSNG 388
Cdd:cd07476  12 ITIAILDGPVDRTHPCFRGANLtplftyAAAACQ----DGGASAHGTHVASLIFGQPcssvEGIAPLCRGLNIPIFAEDR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  389 SG-TMSDVVKGVEYAAK--AHqkeaqekkkgfkgsTANMSLG-----GGKSPALDLAVNAAVEVGIHFAVAAGNeNQDAC 460
Cdd:cd07476  88 RGcSQLDLARAINLALEqgAH--------------IINISGGrltqtGEADPILANAVAMCQQNNVLIVAAAGN-EGCAC 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320775  461 NTSPASADKAITVGASTLSDDRAYFSNWGKCVD---VFAPGLNILSTYIGSDdaTATLSGTSMASPHVAGLLTYFLSLQ 536
Cdd:cd07476 153 LHVPAALPSVLAVGAMDDDGLPLKFSNWGADYRkkgILAPGENILGAALGGE--VVRRSGTSFAAAIVAGIAALLLSLQ 229
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 316-570 5.56e-10

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


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 60.95  E-value: 5.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNiNHKDFEKRAIWGKTIPL---NDEDLDGNGHGT-HCAGTIAskhygVAKNANVVAVKVlrsnGSGT 391
Cdd:cd07494  20 GRGVRVAMVDTGFY-AHPFFESRGYQVRVVLApgaTDPACDENGHGTgESANLFA-----IAPGAQFIGVKL----GGPD 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  392 MSDVVKGVEYAAkAHQKEAQEKKKGFK----GSTANMSLGGGKSpALDLAVNAAVEVGIHFAVAAGNENQdacnTSPASA 467
Cdd:cd07494  90 LVNSVGAFKKAI-SLSPDIISNSWGYDlrspGTSWSRSLPNALK-ALAATLQDAVARGIVVVFSAGNGGW----SFPAQH 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  468 DKAITVGASTLSDD---------RAYFSNW--GKCV-DVFA-PGLNILSTYI---------------------GSDDATA 513
Cdd:cd07494 164 PEVIAAGGVFVDEDgarrassyaSGFRSKIypGRQVpDVCGlVGMLPHAAYLmlpvppgsqldrscaafpdgtPPNDGWG 243

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320775  514 TLSGTSMASPHVAGLLTYFLSLQPGsdseffelgqdsLTPQQlKKKLIHYSTKDILF 570
Cdd:cd07494 244 VFSGTSAAAPQVAGVCALMLQANPG------------LSPER-ARSLLNKTARDVTK 287
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 316-527 6.45e-08

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


Pssm-ID: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 54.78  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  316 GRGVTSYVIDTGVNINHKD------FEKRA---IWGKTIPLNDED-------LDGNGHGTHCAGTIASKHY--------- 370
Cdd:cd07497   1 GEGVVIAIVDTGVDYSHPDldiygnFSWKLkfdYKAYLLPGMDKWggfyvimYDFFSHGTSCASVAAGRGKmeynlygyt 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  371 ------GVAKNANVVAVKVLRSN----GSGTMSDV----VKGVEYAAKAHQKEAQEKKKGFKGSTANmslggGKSPALD- 435
Cdd:cd07497  81 gkflirGIAPDAKIAAVKALWFGdviyAWLWTAGFdpvdRKLSWIYTGGPRVDVISNSWGISNFAYT-----GYAPGLDi 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  436 --LAVNAAV-EVGIHFAVAAGNENQD-ACNTSPASADKAITVGASTL---------------SDDRAYFSNWGKCV---- 492
Cdd:cd07497 156 ssLVIDALVtYTGVPIVSAAGNGGPGyGTITAPGAASLAISVGAATNfdyrpfylfgylpggSGDVVSWSSRGPSIagdp 235

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6320775  493 --DV-------FAPGLNILSTYIGSDDATATL-SGTSMASPHVAG 527
Cdd:cd07497 236 kpDLaaigafaWAPGRVLDSGGALDGNEAFDLfGGTSMATPMTAG 280
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 462-527 8.71e-08

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 55.56  E-value: 8.71e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320775    462 TSPASADKAITVGA-STLSDDRAYFSNWGKCV------DVFAPGLNILSTYIGSddATATLSGTSMASPHVAG 527
Cdd:NF040809  397 TVPGTASRVITVGSfNSRTDVVSVFSGEGDIEngiykpDLLAPGENIVSYLPGG--TTGALTGTSMATPHVTG 467
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
 323-528 5.39e-07

Peptidase S8 family domain, uncharacterized subfamily 7; 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: 173816  Cd Length: 247  Bit Score: 51.18  E-value: 5.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  323 VIDTGVNINHKDFEKRAIWGKTIPLNDEDLDG--------NGHGTHCAGTI-----ASKHYgVAKnanvvaVKVLRSNGS 389
Cdd:cd07491   9 LIDDGVDILDSDLQGKIIGGKSFSPYEGDGNKvspyyvsaDGHGTAMARMIcricpSAKLY-VIK------LEDRPSPDS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  390 G----TMSDVVKGVEYAAkahQKEAQ--------EKKKGFKGSTANmslgggkspaLDLAVNAAVEVGIHFAVAAGNENQ 457
Cdd:cd07491  82 NkrsiTPQSAAKAIEAAV---EKKVDiismswtiKKPEDNDNDINE----------LENAIKEALDRGILLFCSASDQGA 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320775  458 DACNTSPASA--DKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNI---LSTYIGSDDATATlsGTSMASPHVAGL 528
Cdd:cd07491 149 FTGDTYPPPAarDRIFRIGAADEDGGADAPVGDEDRVDYILPGENVearDRPPLSNSFVTHT--GSSVATALAAGL 222
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 436-560 8.22e-07

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


Pssm-ID: 173798 [Multi-domain]  Cd Length: 275  Bit Score: 51.14  E-value: 8.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  436 LAVNAAV-EVGIHFAVAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVD--VFAPGLNILSTYIG--SDD 510
Cdd:cd05562 113 QAVDEVVaSPGVLYFSSAGNDGQSGSIFGHAAAPGAIAVGAVDYGNTPAFGSDPAPGGTpsSFDPVGIRLPTPEVrqKPD 192

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320775  511 ATAT----------------LSGTSMASPHVAGLLTYFLSLQPGsdseffelgqdsLTPQQLKKKL 560
Cdd:cd05562 193 VTAPdgvngtvdgdgdgppnFFGTSAAAPHAAGVAALVLSANPG------------LTPADIRDAL 246
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 353-534 4.34e-06

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: 49.59  E-value: 4.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  353 DGNGHGTHCAGtIASKHY-------GVAKNANVVAVKV----LRSNGSGTmsDVVKGVEYAAKahqkeaqekkkgFKGST 421
Cdd:cd04857 183 DSGAHGTHVAG-IAAAHFpeepernGVAPGAQIVSIKIgdtrLGSMETGT--ALVRAMIAAIE------------TKCDL 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  422 ANMSLGGG-----KSPALDLAVNAAVEVGIHFAVAAGNeNQDACNT--SP-ASADKAITVGA--------------STLS 479
Cdd:cd04857 248 INMSYGEAthwpnSGRIIELMNEAVNKHGVIFVSSAGN-NGPALSTvgAPgGTTSSVIGVGAyvspemmaaeyslrEKLP 326

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320775  480 DDRAYFSNWGKC------VDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLLTYFLS 534
Cdd:cd04857 327 GNQYTWSSRGPTadgalgVSISAPGGAIASVPNWTLQGSQLMNGTSMSSPNACGGIALLLS 387
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 450-551 1.15e-03

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


Pssm-ID: 173813  Cd Length: 247  Bit Score: 40.92  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320775  450 VAAGNENQDACN----TSPASADKAITVGASTLSDDR---AYFSNW--------GKCVDVFAPGLNIlSTYIGSDDataT 514
Cdd:cd07488 128 FSAGNQGKEKEKfggiSIPTLAYNSIVVGSTDRNGDRffaSDVSNAgseinsygRRKVLIVAPGSNY-NLPDGKDD---F 203

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6320775  515 LSGTSMASPHVAGLLTYFLSLQPgsdsEFFELGQDSL 551
Cdd:cd07488 204 VSGTSFSAPLVTGIIALLLEFYD----RQYKKGNNNL 236
 
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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