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Conserved domains on  [gi|887218382|ref|NP_001297469|]
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tripeptidyl-peptidase 2 isoform 2 [Mus musculus]

Protein Classification

tripeptidyl-peptidase 2( domain architecture ID 10141292)

tripeptidyl-peptidase 2 is an S8 family peptidase that catalyzes the release of N-terminal tripeptides from polypeptides

CATH:  3.40.50.200
EC:  3.4.14.10
Gene Symbol:  TPP2
Gene Ontology:  GO:0008236|GO:0006508|GO:0008240
MEROPS:  S8
PubMed:  8439290|9070434

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 14-489 0e+00

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: 853.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   14 GLLPKKETGASSFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEII-GL 92
Cdd:cd04857     1 GLLPKKETGALRFLQKYPEYDGRGVLIAILDTGVDPGAPGLQVTTDGKPKIIDIIDCTGSGDVDTSTVVTPDDGGIIgGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   93 SGRVLKIPANWTNPLGKYHIGIKNGYDfypkalkeriqkerkekiwdpihrvalaeacrkqeefdianngssqanklike 172
Cdd:cd04857    81 TGRKLKIPASWKNPSGKYHVGIKNAYD----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  173 elqsqvellnsfEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLSKCAVLRNYKEAQEYSSFGTAEMLNYSVNIYDDG 252
Cdd:cd04857   108 ------------EKKYEDPGPVYDCVVFHDGEHWRAVIDTSETGDLDSCTVLTNYREEREYATFGEQDLLNYSVNIYDDG 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  253 NLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEA 332
Cdd:cd04857   176 NLLSIVTDSGAHGTHVAGIAAAHFPEEPERNGVAPGAQIVSIKIGDTRLGSMETGTALVRAMIAAIETKCDLINMSYGEA 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  333 THWPNSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSR 412
Cdd:cd04857   256 THWPNSGRIIELMNEAVNKHGVIFVSSAGNNGPALSTVGAPGGTTSSVIGVGAYVSPEMMAAEYSLREKLPGNQYTWSSR 335

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 887218382  413 GPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKA 489
Cdd:cd04857   336 GPTADGALGVSISAPGGAIASVPNWTLQGSQLMNGTSMSSPNACGGIALLLSGLKAEGIPYTPYSVRRALENTAKKL 412
TPPII pfam12580
Tripeptidyl peptidase II; This domain family is found in bacteria and eukaryotes, and is ...
 777-963 1.08e-95

Tripeptidyl peptidase II; This domain family is found in bacteria and eukaryotes, and is approximately 190 amino acids in length. The family is found in association with pfam00082. Tripeptidyl peptidase II (TPPII) is a crucial component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. It is an amino peptidase belonging to the subtilase family removing tripeptides from the free N terminus of oligopeptides.


:

Pssm-ID: 463636  Cd Length: 187  Bit Score: 303.73  E-value: 1.08e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   777 SSLKYEDLAPCITLKSWVQTLRPVNAKTRPL-GSRDVLPNNRQLYEMVLTYSFHQPKSGEVTPSCPLLCELLYESEFDSQ 855
Cdd:pfam12580    1 SPLRSEELKPSASLKTLRQPLRPTESKIRPLsGPRDVLPDGRQIYELVLTYNFKLSKATEVTPRLPLLSDLLYESEFESQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   856 LWIIFDQNKRQMGSGDAYPHQYslKLEKGDYTIRLQIRHEQISDLDRLKDLPFIVSHRLSNTLSLDIHENHSLALLGKKK 935
Cdd:pfam12580   81 LWMLFDSNKQLVAFGDAYPKKY--KLEKGDYTLRLQVRHENRSLLEKLKDLPLLLDQKLKSPISLDVYSSHIDALTGGKK 158

                          170       180
                   ....*....|....*....|....*...
gi 887218382   936 SSSLTLPPKYNQPFFVTSLPDDKIPKGA 963
Cdd:pfam12580  159 SSSSKLPPGQRKPFYIAPLPDDKLPKDA 186
 
Name Accession Description Interval E-value
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 14-489 0e+00

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: 853.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   14 GLLPKKETGASSFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEII-GL 92
Cdd:cd04857     1 GLLPKKETGALRFLQKYPEYDGRGVLIAILDTGVDPGAPGLQVTTDGKPKIIDIIDCTGSGDVDTSTVVTPDDGGIIgGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   93 SGRVLKIPANWTNPLGKYHIGIKNGYDfypkalkeriqkerkekiwdpihrvalaeacrkqeefdianngssqanklike 172
Cdd:cd04857    81 TGRKLKIPASWKNPSGKYHVGIKNAYD----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  173 elqsqvellnsfEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLSKCAVLRNYKEAQEYSSFGTAEMLNYSVNIYDDG 252
Cdd:cd04857   108 ------------EKKYEDPGPVYDCVVFHDGEHWRAVIDTSETGDLDSCTVLTNYREEREYATFGEQDLLNYSVNIYDDG 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  253 NLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEA 332
Cdd:cd04857   176 NLLSIVTDSGAHGTHVAGIAAAHFPEEPERNGVAPGAQIVSIKIGDTRLGSMETGTALVRAMIAAIETKCDLINMSYGEA 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  333 THWPNSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSR 412
Cdd:cd04857   256 THWPNSGRIIELMNEAVNKHGVIFVSSAGNNGPALSTVGAPGGTTSSVIGVGAYVSPEMMAAEYSLREKLPGNQYTWSSR 335

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 887218382  413 GPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKA 489
Cdd:cd04857   336 GPTADGALGVSISAPGGAIASVPNWTLQGSQLMNGTSMSSPNACGGIALLLSGLKAEGIPYTPYSVRRALENTAKKL 412
TPPII pfam12580
Tripeptidyl peptidase II; This domain family is found in bacteria and eukaryotes, and is ...
 777-963 1.08e-95

Tripeptidyl peptidase II; This domain family is found in bacteria and eukaryotes, and is approximately 190 amino acids in length. The family is found in association with pfam00082. Tripeptidyl peptidase II (TPPII) is a crucial component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. It is an amino peptidase belonging to the subtilase family removing tripeptides from the free N terminus of oligopeptides.


Pssm-ID: 463636  Cd Length: 187  Bit Score: 303.73  E-value: 1.08e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   777 SSLKYEDLAPCITLKSWVQTLRPVNAKTRPL-GSRDVLPNNRQLYEMVLTYSFHQPKSGEVTPSCPLLCELLYESEFDSQ 855
Cdd:pfam12580    1 SPLRSEELKPSASLKTLRQPLRPTESKIRPLsGPRDVLPDGRQIYELVLTYNFKLSKATEVTPRLPLLSDLLYESEFESQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   856 LWIIFDQNKRQMGSGDAYPHQYslKLEKGDYTIRLQIRHEQISDLDRLKDLPFIVSHRLSNTLSLDIHENHSLALLGKKK 935
Cdd:pfam12580   81 LWMLFDSNKQLVAFGDAYPKKY--KLEKGDYTLRLQVRHENRSLLEKLKDLPLLLDQKLKSPISLDVYSSHIDALTGGKK 158

                          170       180
                   ....*....|....*....|....*...
gi 887218382   936 SSSLTLPPKYNQPFFVTSLPDDKIPKGA 963
Cdd:pfam12580  159 SSSSKLPPGQRKPFYIAPLPDDKLPKDA 186
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 239-500 8.96e-53

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: 186.90  E-value: 8.96e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   239 AEMLNYSVNIYDDGNllSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKI-GDTRLSTMETgtglIRAMIEV 317
Cdd:pfam00082   32 PEASVDFNNEWDDPR--DDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGAKILGVRVfGDGGGTDAIT----AQAISWA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   318 INHKCDLVNYSYGEATHWPNSGRICEVINEAVW--KHNTIYVSSAGNNGP---CLSTVGCPgGTTSSVIGVGAYvspdmm 392
Cdd:pfam00082  106 IPQGADVINMSWGSDKTDGGPGSWSAAVDQLGGaeAAGSLFVWAAGNGSPggnNGSSVGYP-AQYKNVIAVGAV------ 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   393 vaeyslREKLPANQYTWSSRGPSADGALGVSISAPGGAIASV----------PNWTLRGTQLMNGTSMSSPNACGGIALV 462
Cdd:pfam00082  179 ------DEASEGNLASFSSYGPTLDGRLKPDIVAPGGNITGGnisstlltttSDPPNQGYDSMSGTSMATPHVAGAAALL 252

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 887218382   463 LSGLKannvDYTVHSVRRALENTA-IKADNIEVFAQGHG 500
Cdd:pfam00082  253 KQAYP----NLTPETLKALLVNTAtDLGDAGLDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 256-532 1.04e-41

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 159.88  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  256 SIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTmeTGTGLIRAMIEVINHKCDLVNYSYGeATHW 335
Cdd:COG1404   142 GDPSDDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDDNGSG--TTSDIAAAIDWAADNGADVINLSLG-GPAD 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  336 PNSGRICEVINEAvWKHNTIYVSSAGNNGPCLSTVGCPgGTTSSVIGVGAyVSPDMMVAEYslreklpanqytwSSRGPS 415
Cdd:COG1404   219 GYSDALAAAVDYA-VDKGVLVVAAAGNSGSDDATVSYP-AAYPNVIAVGA-VDANGQLASF-------------SNYGPK 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  416 adgalgVSISAPGGAIAS-VPNwtlRGTQLMNGTSMSSPNACGGIALVLSglkaNNVDYTVHSVRRALENTAIKADNIEV 494
Cdd:COG1404   283 ------VDVAAPGVDILStYPG---GGYATLSGTSMAAPHVAGAAALLLS----ANPDLTPAQVRAILLNTATPLGAPGP 349

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 887218382  495 FaQGHGIIQVDKAYDYLIQNTSFANRLGFTVTVGNNRG 532
Cdd:COG1404   350 Y-YGYGLLADGAAGATSAGAGLAAAAGAAGAAAAATAA 386
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 243-364 1.71e-05

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 49.39  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  243 NYSVNIYDDGNLLSIVTSGGAHGTHVASIAAghfpeepernGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKC 322
Cdd:NF040809  137 NEDINEAINGNKYIPISTTSMHGTHVAGIAA----------SIANEASIIVVRVGRRQTDTFSKSTEFMRAIKFILDKAL 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 887218382  323 DL-----VNYSYG--EATHWPNSgRICEVINE--AVWKHNTiyVSSAGNNG 364
Cdd:NF040809  207 ELkmpvaINISYGsnEGSHRGLS-LFEQYIDDmcLFWKNNI--VVAAGNNA 254
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 380-511 3.62e-03

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: 41.69  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  380 VIGVGAYvspDMMvaeyslreklpaNQYTW--SSRGPSADGALGVSISAPG-GAIASVPNWTLrGTqlMNGTSMSSPNAC 456
Cdd:NF040809  977 IITVGAY---DTI------------NNSIWptSSRGPTIRNIQKPDIVAPGvNIIAPYPGNTY-AT--ITGTSAAAAHVS 1038

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 887218382  457 GGIALVLSGLKANNvDYT----VHSVRRALENTAIKADNIEV--FAQGHGIIQVDKAYDYL 511
Cdd:NF040809 1039 GVAALYLQYTLVER-RYPnqafTQKIKTFMQAGATRSTNIEYpnTTSGYGLLNIRGMFDQL 1098
 
Name Accession Description Interval E-value
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
 14-489 0e+00

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: 853.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   14 GLLPKKETGASSFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEII-GL 92
Cdd:cd04857     1 GLLPKKETGALRFLQKYPEYDGRGVLIAILDTGVDPGAPGLQVTTDGKPKIIDIIDCTGSGDVDTSTVVTPDDGGIIgGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   93 SGRVLKIPANWTNPLGKYHIGIKNGYDfypkalkeriqkerkekiwdpihrvalaeacrkqeefdianngssqanklike 172
Cdd:cd04857    81 TGRKLKIPASWKNPSGKYHVGIKNAYD----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  173 elqsqvellnsfEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLSKCAVLRNYKEAQEYSSFGTAEMLNYSVNIYDDG 252
Cdd:cd04857   108 ------------EKKYEDPGPVYDCVVFHDGEHWRAVIDTSETGDLDSCTVLTNYREEREYATFGEQDLLNYSVNIYDDG 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  253 NLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEA 332
Cdd:cd04857   176 NLLSIVTDSGAHGTHVAGIAAAHFPEEPERNGVAPGAQIVSIKIGDTRLGSMETGTALVRAMIAAIETKCDLINMSYGEA 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  333 THWPNSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSR 412
Cdd:cd04857   256 THWPNSGRIIELMNEAVNKHGVIFVSSAGNNGPALSTVGAPGGTTSSVIGVGAYVSPEMMAAEYSLREKLPGNQYTWSSR 335

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 887218382  413 GPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKA 489
Cdd:cd04857   336 GPTADGALGVSISAPGGAIASVPNWTLQGSQLMNGTSMSSPNACGGIALLLSGLKAEGIPYTPYSVRRALENTAKKL 412
TPPII pfam12580
Tripeptidyl peptidase II; This domain family is found in bacteria and eukaryotes, and is ...
 777-963 1.08e-95

Tripeptidyl peptidase II; This domain family is found in bacteria and eukaryotes, and is approximately 190 amino acids in length. The family is found in association with pfam00082. Tripeptidyl peptidase II (TPPII) is a crucial component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. It is an amino peptidase belonging to the subtilase family removing tripeptides from the free N terminus of oligopeptides.


Pssm-ID: 463636  Cd Length: 187  Bit Score: 303.73  E-value: 1.08e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   777 SSLKYEDLAPCITLKSWVQTLRPVNAKTRPL-GSRDVLPNNRQLYEMVLTYSFHQPKSGEVTPSCPLLCELLYESEFDSQ 855
Cdd:pfam12580    1 SPLRSEELKPSASLKTLRQPLRPTESKIRPLsGPRDVLPDGRQIYELVLTYNFKLSKATEVTPRLPLLSDLLYESEFESQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   856 LWIIFDQNKRQMGSGDAYPHQYslKLEKGDYTIRLQIRHEQISDLDRLKDLPFIVSHRLSNTLSLDIHENHSLALLGKKK 935
Cdd:pfam12580   81 LWMLFDSNKQLVAFGDAYPKKY--KLEKGDYTLRLQVRHENRSLLEKLKDLPLLLDQKLKSPISLDVYSSHIDALTGGKK 158

                          170       180
                   ....*....|....*....|....*...
gi 887218382   936 SSSLTLPPKYNQPFFVTSLPDDKIPKGA 963
Cdd:pfam12580  159 SSSSKLPPGQRKPFYIAPLPDDKLPKDA 186
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 239-500 8.96e-53

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: 186.90  E-value: 8.96e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   239 AEMLNYSVNIYDDGNllSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKI-GDTRLSTMETgtglIRAMIEV 317
Cdd:pfam00082   32 PEASVDFNNEWDDPR--DDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGAKILGVRVfGDGGGTDAIT----AQAISWA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   318 INHKCDLVNYSYGEATHWPNSGRICEVINEAVW--KHNTIYVSSAGNNGP---CLSTVGCPgGTTSSVIGVGAYvspdmm 392
Cdd:pfam00082  106 IPQGADVINMSWGSDKTDGGPGSWSAAVDQLGGaeAAGSLFVWAAGNGSPggnNGSSVGYP-AQYKNVIAVGAV------ 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382   393 vaeyslREKLPANQYTWSSRGPSADGALGVSISAPGGAIASV----------PNWTLRGTQLMNGTSMSSPNACGGIALV 462
Cdd:pfam00082  179 ------DEASEGNLASFSSYGPTLDGRLKPDIVAPGGNITGGnisstlltttSDPPNQGYDSMSGTSMATPHVAGAAALL 252

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 887218382   463 LSGLKannvDYTVHSVRRALENTA-IKADNIEVFAQGHG 500
Cdd:pfam00082  253 KQAYP----NLTPETLKALLVNTAtDLGDAGLDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 256-532 1.04e-41

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 159.88  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  256 SIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTmeTGTGLIRAMIEVINHKCDLVNYSYGeATHW 335
Cdd:COG1404   142 GDPSDDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDDNGSG--TTSDIAAAIDWAADNGADVINLSLG-GPAD 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  336 PNSGRICEVINEAvWKHNTIYVSSAGNNGPCLSTVGCPgGTTSSVIGVGAyVSPDMMVAEYslreklpanqytwSSRGPS 415
Cdd:COG1404   219 GYSDALAAAVDYA-VDKGVLVVAAAGNSGSDDATVSYP-AAYPNVIAVGA-VDANGQLASF-------------SNYGPK 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  416 adgalgVSISAPGGAIAS-VPNwtlRGTQLMNGTSMSSPNACGGIALVLSglkaNNVDYTVHSVRRALENTAIKADNIEV 494
Cdd:COG1404   283 ------VDVAAPGVDILStYPG---GGYATLSGTSMAAPHVAGAAALLLS----ANPDLTPAQVRAILLNTATPLGAPGP 349

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 887218382  495 FaQGHGIIQVDKAYDYLIQNTSFANRLGFTVTVGNNRG 532
Cdd:COG1404   350 Y-YGYGLLADGAAGATSAGAGLAAAAGAAGAAAAATAA 386
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 233-507 3.37e-35

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: 136.31  E-value: 3.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  233 YSSFGTAEMlNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTmeTGTGLIR 312
Cdd:cd07474    34 YDFVDDDYD-PMDTRPYPSPLGDASAGDATGHGTHVAGIIAGNGVNVGTIKGVAPKADLYAYKVLGPGGSG--TTDVIIA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  313 AMIEVINHKCDLVNYSYGEathwpNSGRICEVINEAV---WKHNTIYVSSAGNNGPCLSTVGCPgGTTSSVIGVGAYVSP 389
Cdd:cd07474   111 AIEQAVDDGMDVINLSLGS-----SVNGPDDPDAIAInnaVKAGVVVVAAAGNSGPAPYTIGSP-ATAPSAITVGASTVA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  390 DMMVAEYSlreklpaNQYTwSSRGPSADGALGVSISAPGGAIAS-VPNWTLRGTQlMNGTSMSSPNACGGIALvlsgLKA 468
Cdd:cd07474   185 DVAEADTV-------GPSS-SRGPPTSDSAIKPDIVAPGVDIMStAPGSGTGYAR-MSGTSMAAPHVAGAAAL----LKQ 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 887218382  469 NNVDYTVHSVRRALENTAiKADNIE------VFAQGHGIIQVDKA 507
Cdd:cd07474   252 AHPDWSPAQIKAALMNTA-KPLYDSdgvvypVSRQGAGRVDALRA 295
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 243-485 3.87e-35

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: 134.63  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  243 NYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHfPEEPERNGVAPGAQILSIKIGDTRLSTmeTGTGLIRAMIEVI-NHK 321
Cdd:cd00306    25 DGGNDDDDNENGPTDPDDGNGHGTHVAGIIAAS-ANNGGGVGVAPGAKLIPVKVLDGDGSG--SSSDIAAAIDYAAaDQG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  322 CDLVNYSYGEATHWPnSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYvspdmmvaeyslrek 401
Cdd:cd00306   102 ADVINLSLGGPGSPP-SSALSEAIDYALAKLGVLVVAAAGNDGPDGGTNIGYPAASPNVIAVGAV--------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  402 lpANQYTWSSrgPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSglkaNNVDYTVHSVRRA 481
Cdd:cd00306   166 --DRDGTPAS--PSSNGGAGVDIAAPGGDILSSPTTGGGGYATLSGTSMAAPIVAGVAALLLS----ANPDLTPAQVKAA 237


                  ....
gi 887218382  482 LENT 485
Cdd:cd00306   238 LLST 241
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 244-507 2.67e-33

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: 132.39  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  244 YSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERN---GVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINH 320
Cdd:cd07475    64 FAYNYADNNDDILDEDDGSSHGMHVAGIVAGNGDEEDNGEgikGVAPEAQLLAMKVFSNPEGGSTYDDAYAKAIEDAVKL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  321 KCDLVNYSYG---------EATHwpnsgricEVINEAVwKHNTIYVSSAGNNG--------------PCLSTVGCPGgTT 377
Cdd:cd07475   144 GADVINMSLGstagfvdldDPEQ--------QAIKRAR-EAGVVVVVAAGNDGnsgsgtskplatnnPDTGTVGSPA-TA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  378 SSVIGVGAYVSpdmMVAEYslreklPANQYT-WSSRGPSADGALGVSISAPGGAIASvpnwTLRGTQL--MNGTSMSSPN 454
Cdd:cd07475   214 DDVLTVASANK---KVPNP------NGGQMSgFSSWGPTPDLDLKPDITAPGGNIYS----TVNDNTYgyMSGTSMASPH 280

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887218382  455 ACGGIALVLSGLKANNVDYT----VHSVRRALENTAIKADNIEVFA-------QGHGIIQVDKA 507
Cdd:cd07475   281 VAGASALVKQRLKEKYPKLSgeelVDLVKNLLMNTATPPLDSEDTKtyysprrQGAGLIDVAKA 344
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 237-485 3.72e-26

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: 108.00  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  237 GTAEMLNYSVNIYDDGNllsivtsggAHGTHVASIAAGHfPEEPERNGVAPGAQILSIKI----GDTRLSTmetgtgLIR 312
Cdd:cd07477    24 GGANFTGDDNNDYQDGN---------GHGTHVAGIIAAL-DNGVGVVGVAPEADLYAVKVlnddGSGTYSD------IIA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  313 AMIEVINHKCDLVNYSYGeaTHWPNSgRICEVINEAVwKHNTIYVSSAGNNGPCLSTVGCPGGTtSSVIGVGAyVSPDMM 392
Cdd:cd07477    88 GIEWAIENGMDIINMSLG--GPSDSP-ALREAIKKAY-AAGILVVAAAGNSGNGDSSYDYPAKY-PSVIAVGA-VDSNNN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  393 VAEYSlreklpanqytwsSRGPsadgalGVSISAPGGAIAS-VPNWTLRgtqLMNGTSMSSPNACGGIALVLSglkaNNV 471
Cdd:cd07477   162 RASFS-------------STGP------EVELAAPGVDILStYPNNDYA---YLSGTSMATPHVAGVAALVWS----KRP 215

                         250
                  ....*....|....
gi 887218382  472 DYTVHSVRRALENT 485
Cdd:cd07477   216 ELTNAQVRQALNKT 229
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 247-486 6.27e-26

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: 108.44  E-value: 6.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  247 NIYDDgnllsivtSGgaHGTHVASIAAGHFP-EEPERNGVAPGAQILSIKIGDtrlstmETGTGLIRAMIEVINHKCDL- 324
Cdd:cd07487    39 TPYDD--------NG--HGTHVAGIIAGSGRaSNGKYKGVAPGANLVGVKVLD------DSGSGSESDIIAGIDWVVENn 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  325 -------VNYSYGeATHWPNSGR--ICEVINEAvWKHNTIYVSSAGNNGPCLSTVGCPgGTTSSVIGVGAyvSPDMMVAE 395
Cdd:cd07487   103 ekynirvVNLSLG-APPDPSYGEdpLCQAVERL-WDAGIVVVVAAGNSGPGPGTITSP-GNSPKVITVGA--VDDNGPHD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  396 YSLREklpanqytWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQL-------MNGTSMSSPNACGGIALVLSglka 468
Cdd:cd07487   178 DGISY--------FSSRGPTGDGRIKPDVVAPGENIVSCRSPGGNPGAGvgsgyfeMSGTSMATPHVSGAIALLLQ---- 245

                         250
                  ....*....|....*...
gi 887218382  469 NNVDYTVHSVRRALENTA 486
Cdd:cd07487   246 ANPILTPDEVKCILRDTA 263
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 246-462 7.25e-25

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: 106.26  E-value: 7.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  246 VNIYDDGNLLSIVTSGgaHGTHVASIAAGHFPEEPER---NGVAPGAQILSIKIGDT--RLSTMETGTGLIRAMIEVinh 320
Cdd:cd04842    40 IVRYDSLSDTKDDVDG--HGTHVAGIIAGKGNDSSSIslyKGVAPKAKLYFQDIGDTsgNLSSPPDLNKLFSPMYDA--- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  321 KCDLVNYSYGEATHwPNSGRICEVINEAVWKH-NTIYVSSAGNNGP-CLSTVGCPGgTTSSVIGVGA--YVSPDMMVaEY 396
Cdd:cd04842   115 GARISSNSWGSPVN-NGYTLLARAYDQFAYNNpDILFVFSAGNDGNdGSNTIGSPA-TAKNVLTVGAsnNPSVSNGE-GG 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 887218382  397 SLREKLPANQYTWSSRGPSADGALGVSISAPGGAIAS-VPNWTLRGT------QLMNGTSMSSPNACGGIALV 462
Cdd:cd04842   192 LGQSDNSDTVASFSSRGPTYDGRIKPDLVAPGTGILSaRSGGGGIGDtsdsayTSKSGTSMATPLVAGAAALL 264
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 262-513 3.65e-23

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


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 101.53  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  262 GAHGTHVASIAAGHfPEEPERNGVAPGAQILSIKI-GDTRLSTMETgtgLIRAMIEVINHKCDLVNYSYGEATHWPNS-- 338
Cdd:cd07489    68 QGHGTHVAGIIAAN-PNAYGFTGVAPEATLGAYRVfGCSGSTTEDT---IIAAFLRAYEDGADVITASLGGPSGWSEDpw 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  339 ----GRICEvineavwkHNTIYVSSAGNNG---PCLSTVGcpgGTTSSVIGVGAYVSpdmmvaeyslreklpanqyTWSS 411
Cdd:cd07489   144 avvaSRIVD--------AGVVVTIAAGNDGergPFYASSP---ASGRGVIAVASVDS-------------------YFSS 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  412 RGPSADGALGVSISAPGGAIAS-VPNwTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTvhsVRRALENTAI--- 487
Cdd:cd07489   194 WGPTNELYLKPDVAAPGGNILStYPL-AGGGYAVLSGTSMATPYVAGAAALLIQARHGKLSPAE---LRDLLASTAKplp 269

                         250       260       270
                  ....*....|....*....|....*....|...
gi 887218382  488 -----KADNIE--VFAQGHGIIQVDKAYDYLIQ 513
Cdd:cd07489   270 wsdgtSALPDLapVAQQGAGLVNAYKALYATTT 302
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 262-486 8.04e-22

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: 96.68  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  262 GAHGTHVASIAAGHFPEEPeRNGVAPGAQILSIKIGDTRLSTMETgtgLIRAM--------IEVINHKCDL----VNYSY 329
Cdd:cd07481    52 NGHGTHTMGTMVGNDGDGQ-QIGVAPGARWIACRALDRNGGNDAD---YLRCAqwmlaptdSAGNPADPDLapdvINNSW 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  330 GEATHWPNSGRicEVINeaVWKHNTIY-VSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMvaeyslreklpanqYT 408
Cdd:cd07481   128 GGPSGDNEWLQ--PAVA--AWRAAGIFpVFAAGNDGPRCSTLNAPPANYPESFAVGATDRNDVL--------------AD 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  409 WSSRGPSADGALGVSISAPGGAI-ASVPNwtlRGTQLMNGTSMSSPNACGGIALVLSglkAN-----NVDYTvhsvRRAL 482
Cdd:cd07481   190 FSSRGPSTYGRIKPDISAPGVNIrSAVPG---GGYGSSSGTSMAAPHVAGVAALLWS---ANpsligDVDAT----EAIL 259


                  ....
gi 887218382  483 ENTA 486
Cdd:cd07481   260 TETA 263
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 251-486 1.51e-20

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: 94.07  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  251 DGNLLSIVTSGGAHGTHVASIAAGHfpEEPERN-----------GVAPGAQILSIK---IGDTRLSTMETG--------- 307
Cdd:cd07497    45 WGGFYVIMYDFFSHGTSCASVAAGR--GKMEYNlygytgkflirGIAPDAKIAAVKalwFGDVIYAWLWTAgfdpvdrkl 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  308 ----TGliramieviNHKCDLVNYSYGeATHWPNSG------RICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPgGTT 377
Cdd:cd07497   123 swiyTG---------GPRVDVISNSWG-ISNFAYTGyapgldISSLVIDALVTYTGVPIVSAAGNGGPGYGTITAP-GAA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  378 SSVIGVGAYVSPDmmvaeYSLREKLPANQY------TWSSRGPSADGALGVSISAPGG-AIASVPNWTLRGT-------Q 443
Cdd:cd07497   192 SLAISVGAATNFD-----YRPFYLFGYLPGgsgdvvSWSSRGPSIAGDPKPDLAAIGAfAWAPGRVLDSGGAldgneafD 266

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 887218382  444 LMNGTSMSSPNACGGIALVLSGLK--ANNVDYTVHSVRRALENTA 486
Cdd:cd07497   267 LFGGTSMATPMTAGSAALVISALKekEGVGEYDPFLVRTILMSTA 311
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 240-486 1.16e-18

Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173815 [Multi-domain]  Cd Length: 254  Bit Score: 87.22  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  240 EMLNYSVNIYDDGNllsivtsggAHGTHVASIAAGHfPEEPERNGVAPGAQILSIKIGDTRLSTMetgTGLIRAMIEVIN 319
Cdd:cd07490    30 ENRRISATEVFDAG---------GHGTHVSGTIGGG-GAKGVYIGVAPEADLLHGKVLDDGGGSL---SQIIAGMEWAVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  320 HKCDLVNYSYGEAThwPNSGRICEVINEAVWKHNTIYVSSAGNNGPclSTVGCPGgTTSSVIGVGAyVSPDMMVAEYSLR 399
Cdd:cd07490    97 KDADVVSMSLGGTY--YSEDPLEEAVEALSNQTGALFVVSAGNEGH--GTSGSPG-SAYAALSVGA-VDRDDEDAWFSSF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  400 EKLPANQytwSSRGPSADGALGV-SISAPGGAIASVPNWTLRGTQL--MNGTSMSSPNACGGIALvlsgLKANNVDYTVH 476
Cdd:cd07490   171 GSSGASL---VSAPDSPPDEYTKpDVAAPGVDVYSARQGANGDGQYtrLSGTSMAAPHVAGVAAL----LAAAHPDLSPE 243

                         250
                  ....*....|
gi 887218382  477 SVRRALENTA 486
Cdd:cd07490   244 QIKDALTETA 253
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 263-486 1.92e-18

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: 86.55  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  263 AHGTHVASIAAGhfpeepERN------GVAPGAQILSIKIGDtrlstmETGTGLIRAMIEVI----NHKCDLVNYSYGEA 332
Cdd:cd07484    69 GHGTHVAGIIAA------ATNngtgvaGVAPKAKIMPVKVLD------ANGSGSLADIANGIryaaDKGAKVINLSLGGG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  333 THwpnSGRICEVINEAvWKHNTIYVSSAGNNGpcLSTVGCPgGTTSSVIGVGAyVSPDMMVAEYSlreklpanqytwssr 412
Cdd:cd07484   137 LG---STALQEAINYA-WNKGVVVVAAAGNEG--VSSVSYP-AAYPGAIAVAA-TDQDDKRASFS--------------- 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887218382  413 gpsaDGALGVSISAPGGAIASvpNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDytvhsVRRALENTA 486
Cdd:cd07484   194 ----NYGKWVDVSAPGGGILS--TTPDGDYAYMSGTSMATPHVAGVAALLYSQGPLSASE-----VRDALKKTA 256
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 264-488 5.01e-18

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: 85.26  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  264 HGTHVASIAAGhfpeepERNGVAPGAQILSIKIGDTRLSTmeTGTGLIRAMIEVINHKCDL-----VNYSYGEATHwpns 338
Cdd:cd04077    65 HGTHVAGTVGG------KTYGVAKKANLVAVKVLDCNGSG--TLSGIIAGLEWVANDATKRgkpavANMSLGGGAS---- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  339 gricEVINEAV---WKHNTIYVSSAGNNG--PCLSTvgcPGGtTSSVIGVGAYVSPDmmvaeyslreklpaNQYTWSSRG 413
Cdd:cd04077   133 ----TALDAAVaaaVNAGVVVVVAAGNSNqdACNYS---PAS-APEAITVGATDSDD--------------ARASFSNYG 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 887218382  414 PsadgalGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSglkaNNVDYTVHSVRRALENTAIK 488
Cdd:cd04077   191 S------CVDIFAPGVDILSAWIGSDTATATLSGTSMAAPHVAGLAAYLLS----LGPDLSPAEVKARLLNLATK 255
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 242-464 1.43e-17

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: 84.30  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  242 LNYSVNIYDDGNLLSIVTSGgaHGTHVASIAAGHFPEEPERnGVAPGAQILSIKIGDTRLSTMETgTGLIRAMIEVINHK 321
Cdd:cd04848    28 ASYYVAVNDAGYASNGDGDS--HGTHVAGVIAAARDGGGMH-GVAPDATLYSARASASAGSTFSD-ADIAAAYDFLAASG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  322 CDLVNYSYGEAThWPNSGRICEVINEAVWKH------------NTIYVSSAGNNGpclstvgcpgGTTSSVIGVGA-YVS 388
Cdd:cd04848   104 VRIINNSWGGNP-AIDTVSTTYKGSAATQGNtllaalaraanaGGLFVFAAGNDG----------QANPSLAAAALpYLE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  389 PD-----MMVAeySLREKLPANQYTWSSRGpsadgalGV----SISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGI 459
Cdd:cd04848   173 PEleggwIAVV--AVDPNGTIASYSYSNRC-------GVaanwCLAAPGENIYSTDPDGGNGYGRVSGTSFAAPHVSGAA 243


                  ....*
gi 887218382  460 ALVLS 464
Cdd:cd04848   244 ALLAQ 248
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 246-486 3.15e-16

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: 79.93  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  246 VNIYDDGNLLSIVTSGGAHGTHVASIAAGhfpeepERN------GVAPGAQILSIKIGDtrlstmETGTGL----IRAMI 315
Cdd:cd07473    47 IYGWNFVNNDNDPMDDNGHGTHVAGIIGA------VGNngigiaGVAWNVKIMPLKFLG------ADGSGTtsdaIKAID 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  316 EVINHKCDLVNYSYGEATHwpnSGRICEVINEAVwKHNTIYVSSAGNNGPCLSTVGC-PGG-TTSSVIGVGAYVSPDMMv 393
Cdd:cd07473   115 YAVDMGAKIINNSWGGGGP---SQALRDAIARAI-DAGILFVAAAGNDGTNNDKTPTyPASyDLDNIISVAATDSNDAL- 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  394 aeyslreklpanqYTWSSRGPSAdgalgVSISAPGGAIASvpNWTLRGTQLMNGTSMSSPNACGGIALVLSglkaNNVDY 473
Cdd:cd07473   190 -------------ASFSNYGKKT-----VDLAAPGVDILS--TSPGGGYGYMSGTSMATPHVAGAAALLLS----LNPNL 245

                         250
                  ....*....|...
gi 887218382  474 TVHSVRRALENTA 486
Cdd:cd07473   246 TAAQIKDAILSSA 258
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 243-485 5.07e-15

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: 76.76  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  243 NYSVNIYDDGNLLSIvtsGGAHGTHVAS-IAA-----GHFPEEPERNGVAPGAQILSIKIGDTRLSTmeTGTGLIRAMIE 316
Cdd:cd07485    45 NFVPNVGDIDNDVSV---GGGHGTHVAGtIAAvnnngGGVGGIAGAGGVAPGVKIMSIQIFAGRYYV--GDDAVAAAIVY 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  317 VINHKCDLVNYSYGEATHWPNSGRICEVINEAV------WKHNTIYVSSAGNNgpclST------VGCPGgttssVIGVG 384
Cdd:cd07485   120 AADNGAVILQNSWGGTGGGIYSPLLKDAFDYFIenaggsPLDGGIVVFSAGNS----YTdehrfpAAYPG-----VIAVA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  385 AYVSPDmmvaeyslreklpaNQYTWSSRGpsadgaLGVSISAPGGA--IASVPNWTLRGT---QLMNGTSMSSPNACGGI 459
Cdd:cd07485   191 ALDTND--------------NKASFSNYG------RWVDIAAPGVGtiLSTVPKLDGDGGgnyEYLSGTSMAAPHVSGVA 250

                         250       260
                  ....*....|....*....|....*.
gi 887218382  460 ALVLSGLKannVDYTVHSVRRALENT 485
Cdd:cd07485   251 ALVLSKFP---DVFTPEQIRKLLEES 273
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 259-510 6.88e-15

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: 76.56  E-value: 6.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  259 TSGGAHGTHVASIAagHfpeepernGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVInhkCDLVNYSygeATHWPNS 338
Cdd:cd05562    45 SGGGDEGRAMLEII--H--------DIAPGAELAFHTAGGGELDFAAAIRALAAAGADII---VDDIGYL---NEPFFQD 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  339 GRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGttSSVIGVGAY-VSPDMMVAEYSLREKLPANQYTWSSRGPSAD 417
Cdd:cd05562   109 GPIAQAVDEVVASPGVLYFSSAGNDGQSGSIFGHAAA--PGAIAVGAVdYGNTPAFGSDPAPGGTPSSFDPVGIRLPTPE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  418 GALGVSISAPGGAIASVpnwTLRGTQLMN--GTSMSSPNACGGIALVLSglkaNNVDYTVHSVRRALENTAIkaDNIEV- 494
Cdd:cd05562   187 VRQKPDVTAPDGVNGTV---DGDGDGPPNffGTSAAAPHAAGVAALVLS----ANPGLTPADIRDALRSTAL--DMGEPg 257

                         250
                  ....*....|....*...
gi 887218382  495 --FAQGHGIIQVDKAYDY 510
Cdd:cd05562   258 ydNASGSGLVDADRAVAA 275
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 264-485 6.19e-13

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: 70.78  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  264 HGTHVAS-IAAGHfpeeperN------GVAPGAQILSIKI---GDTRLSTMETG----TGLIRAMIEVINHKCDLVNYSY 329
Cdd:cd07496    73 HGTHVAGtIAAVT-------NngvgvaGVAWGARILPVRVlgkCGGTLSDIVDGmrwaAGLPVPGVPVNPNPAKVINLSL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  330 GEAThwPNSGRICEVINEAVWKhNTIYVSSAGNNGPCLSTV---GCPGgttssVIGVGAyVSPDMMVAEYSlreklpanq 406
Cdd:cd07496   146 GGDG--ACSATMQNAINDVRAR-GVLVVVAAGNEGSSASVDapaNCRG-----VIAVGA-TDLRGQRASYS--------- 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  407 ytwsSRGPsadgalGVSISAPGGAIAS------VPNWTLRGT-------QLMNGTSMSSPNACGGIALvlsgLKANNVDY 473
Cdd:cd07496   208 ----NYGP------AVDVSAPGGDCASdvngdgYPDSNTGTTspggstyGFLQGTSMAAPHVAGVAAL----MKSVNPSL 273

                         250
                  ....*....|..
gi 887218382  474 TVHSVRRALENT 485
Cdd:cd07496   274 TPAQIESLLQST 285
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 263-485 1.18e-12

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: 69.29  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  263 AHGTHVASIAAGhfpeepERN------GVAPGAQILSIKIGD----TRLSTMETGtgLIRAMieviNHKCDLVNYSYGEA 332
Cdd:cd07498    41 GHGTACAGVAAA------VGNnglgvaGVAPGAKLMPVRIADslgyAYWSDIAQA--ITWAA----DNGADVISNSWGGS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  333 ThwpNSGRICEVINEAVWK----HNTIYVSSAGNNGPclSTVGCPGGTTSsVIGVGAYVSPDMMVAeyslreklpanqyt 408
Cdd:cd07498   109 D---STESISSAIDNAATYgrngKGGVVLFAAGNSGR--SVSSGYAANPS-VIAVAATDSNDARAS-------------- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  409 WSSRGPSadgalgVSISAPGGAIASVPNWTLR-------GTQLMNGTSMSSPNACGGIALVLSGlkanNVDYTVHSVRRA 481
Cdd:cd07498   169 YSNYGNY------VDLVAPGVGIWTTGTGRGSagdypggGYGSFSGTSFASPVAAGVAALILSA----NPNLTPAEVEDI 238


                  ....
gi 887218382  482 LENT 485
Cdd:cd07498   239 LTST 242
Peptidases_S8_thiazoline_oxidase_subtilisin-like_p cd07476
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ...
 263-490 5.62e-12

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: 67.74  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  263 AHGTHVASIAAGHfpEEPERNGVAPGAQILSIKI--GDTRLSTMetgTGLIRAMIEVINHKCDLVNYSYGEAThwpNSGR 340
Cdd:cd07476    51 AHGTHVASLIFGQ--PCSSVEGIAPLCRGLNIPIfaEDRRGCSQ---LDLARAINLALEQGAHIINISGGRLT---QTGE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  341 ICEVINEAVWK---HNTIYVSSAGNNG-PCLSTvgcPGGtTSSVIGVGAyvspdMMVAEYSLREKLPANQYTwsSRGPSA 416
Cdd:cd07476   123 ADPILANAVAMcqqNNVLIVAAAGNEGcACLHV---PAA-LPSVLAVGA-----MDDDGLPLKFSNWGADYR--KKGILA 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887218382  417 DGAlGVSISAPGGaiasvpnwtlrGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKAD 490
Cdd:cd07476   192 PGE-NILGAALGG-----------EVVRRSGTSFAAAIVAGIAALLLSLQLRRGAPPDPLAVRRALLETATPCD 253
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 259-486 2.69e-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: 65.40  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  259 TSGGAHGTHVASIAAGHFPEEPErnGVAPGAQ--ILSIKIGDTRLSTMETGtgLIRAMIEVINHKCDLVNYSYGEAT-HW 335
Cdd:cd07493    44 YTDDDHGTAVLSTMAGYTPGVMV--GTAPNASyyLARTEDVASETPVEEDN--WVAAAEWADSLGVDIISSSLGYTTfDN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  336 PNSG-----------RICEVINEAVWKhNTIYVSSAGNNGP-CLSTVGCPGgTTSSVIGVGAyVSPDMMVAEYSlreklp 403
Cdd:cd07493   120 PTYSytyadmdgktsFISRAANIAASK-GMLVVNSAGNEGStQWKGIGAPA-DAENVLSVGA-VDANGNKASFS------ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  404 anqytwsSRGPSADGALGVSISAPG-GAIASVPNWTLRgtqLMNGTSMSSPNACGGIALvlsgLKANNVDYTVHSVRRAL 482
Cdd:cd07493   191 -------SIGPTADGRLKPDVMALGtGIYVINGDGNIT---YANGTSFSCPLIAGLIAC----LWQAHPNWTNLQIKEAI 256


                  ....
gi 887218382  483 ENTA 486
Cdd:cd07493   257 LKSA 260
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
 243-487 3.11e-11

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: 66.08  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  243 NYSVNIYDDGNLLSIVTSGGaHGTHVASIAAGHF--PEEPERN------GVAPGAQILSIKIGDTRLSTmeTGTGLIRAM 314
Cdd:cd04852    90 DAYGGFNSDGEYRSPRDYDG-HGTHTASTAAGNVvvNASVGGFafgtasGVAPRARIAVYKVCWPDGGC--FGSDILAAI 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  315 IEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKhnTIYVS-SAGNNGPCLSTVgcpggTTSS--VIGVGAY-VSPD 390
Cdd:cd04852   167 DQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEA--GIFVAaSAGNSGPGASTV-----PNVApwVTTVAAStLKPD 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  391 MMvaeyslreklpanqytwssrgpsadgALGVSISAPGGAIASVPNWTLRGT-QLMNGTSMSSPNACGGIALvlsgLKAN 469
Cdd:cd04852   240 IA--------------------------APGVDILAAWTPEGADPGDARGEDfAFISGTSMASPHVAGVAAL----LKSA 289

                         250
                  ....*....|....*...
gi 887218382  470 NVDYTVHSVRRALENTAI 487
Cdd:cd04852   290 HPDWSPAAIKSALMTTAY 307
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 263-469 2.75e-10

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: 62.96  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  263 AHGTHVASIAAGhfpeepERN------GVAPGAQILSIKIGDTRLSTMETGTGLIRAMievinHKCDLVNYSYGEAT--- 333
Cdd:cd04059    85 SHGTRCAGEIAA------VGNngicgvGVAPGAKLGGIRMLDGDVTDVVEAESLGLNP-----DYIDIYSNSWGPDDdgk 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  334 --------------HWPNSGRicevineavWKHNTIYVSSAGNNGPCLSTVGCPGGTTSS-VIGVGAyVSPDMMVAEYSl 398
Cdd:cd04059   154 tvdgpgplaqraleNGVTNGR---------NGKGSIFVWAAGNGGNLGDNCNCDGYNNSIyTISVSA-VTANGVRASYS- 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887218382  399 reklpanqytwsSRGPSadgalgVSISAPGG-------AIASV-PNWTLRGTQLMNGTSMSSPNACGGIALVLSglkAN 469
Cdd:cd04059   223 ------------EVGSS------VLASAPSGgsgnpeaSIVTTdLGGNCNCTSSHNGTSAAAPLAAGVIALMLE---AN 280
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 264-486 5.01e-10

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: 60.82  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  264 HGTHVASIAAGHFPEeperngvapgAQILSIKIGDTRLSTmeTGTGLIRAMIEVINHKCDLVNYSYGeATHWPNSGRICE 343
Cdd:cd07492    46 HGTACAGIIKKYAPE----------AEIGSIKILGEDGRC--NSFVLEKALRACVENDIRIVNLSLG-GPGDRDFPLLKE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  344 VINEAVwKHNTIYVSSAGNNGPCLstvGCPGGTTsSVIGVGAYVSPDMMVAEYslreklPANQYtwssrgpSADgalGVS 423
Cdd:cd07492   113 LLEYAY-KAGGIIVAAAPNNNDIG---TPPASFP-NVIGVKSDTADDPKSFWY------IYVEF-------SAD---GVD 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 887218382  424 ISAPGGAIASVPNwtlrgtqlmNGTSMSSPNACGGIALVLSglkaNNVDYTVHSVRRALENTA 486
Cdd:cd07492   172 IIAPAPHGRYLTV---------SGNSFAAPHVTGMVALLLS----EKPDIDANDLKRLLQRLA 221
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 264-461 5.83e-10

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: 62.01  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  264 HGTHVASIAAGHFpEEPERNGVAPGAQILSIK--IGDTRlstmETGTGLIRAMIEVINHKCDLVNYSYGEATH------W 335
Cdd:cd07480    48 HGTHCAGTIFGRD-VPGPRYGVARGAEIALIGkvLGDGG----GGDGGILAGIQWAVANGADVISMSLGADFPglvdqgW 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  336 PN------------------SGRICEVINEAVWKHNTIYVSSAGNNG------PCLSTVGCPggttSSVIGVGAyVSPDM 391
Cdd:cd07480   123 PPglafsraleayrqrarlfDALMTLVAAQAALARGTLIVAAAGNESqrpagiPPVGNPAAC----PSAMGVAA-VGALG 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 887218382  392 MVAEYSlreklpanqytwssrgPSADGALG-VSISAPGGAIASVpnWTLRGTQLMNGTSMSSPNACGGIAL 461
Cdd:cd07480   198 RTGNFS----------------AVANFSNGeVDIAAPGVDIVSA--APGGGYRSMSGTSMATPHVAGVAAL 250
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 260-464 5.91e-10

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: 62.00  E-value: 5.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  260 SGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKI---GDtrlstmETGTGLIRAMIEVINHKCDLVNYSYGEaTHWP 336
Cdd:cd07483    83 SDADHGTHVAGIIAAVRDNGIGIDGVADNVKIMPLRIvpnGD------ERDKDIANAIRYAVDNGAKVINMSFGK-SFSP 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  337 NSGRICEVINEAVwKHNTIYVSSAGNNG------PCL--STVGCPGGTTSSVIGVGA--YVSPDMMVAEYSlreklpanQ 406
Cdd:cd07483   156 NKEWVDDAIKYAE-SKGVLIVHAAGNDGldlditPNFpnDYDKNGGEPANNFITVGAssKKYENNLVANFS--------N 226

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 887218382  407 YtwssrgpsadGALGVSISAPGGAIASVPNWTLRGTQlmNGTSMSSPNACGGIALVLS 464
Cdd:cd07483   227 Y----------GKKNVDVFAPGERIYSTTPDNEYETD--SGTSMAAPVVSGVAALIWS 272
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 258-488 1.43e-09

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: 60.16  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  258 VTSGGAHGTHVASIAAGHFPEEPernGVAPGAQILSIKI-GDTRLSTMetgTGLIRAMIEVINHKCDLVNYSYG--EATH 334
Cdd:cd07479    41 LDDGLGHGTFVAGVIASSREQCL---GFAPDAEIYIFRVfTNNQVSYT---SWFLDAFNYAILTKIDVLNLSIGgpDFMD 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  335 WPnsgricevINEAVWK---HNTIYVSSAGNNGPCLSTVGCPGgTTSSVIGVGAyVSPDMMVAEYSLReklpaNQYTWSS 411
Cdd:cd07479   115 KP--------FVDKVWEltaNNIIMVSAIGNDGPLYGTLNNPA-DQMDVIGVGG-IDFDDNIARFSSR-----GMTTWEL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 887218382  412 rgPSADGALGVSISAPGGAIASVPNWTlrGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIK 488
Cdd:cd07479   180 --PGGYGRVKPDIVTYGSGVYGSKLKG--GCRALSGTSVASPVVAGAVALLLSTVPEKRDLINPASMKQALIESATR 252
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 369-463 9.08e-08

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: 56.09  E-value: 9.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  369 TVGCPGgTTSSVIGVGAYVSpdmmvaeyslrekLPANQYTWSSRGPSADGALGVSISAPG-GAIASVPNwtlRGTQLMNG 447
Cdd:cd07478   336 TLTIPG-TARSVITVGAYNQ-------------NNNSIAIFSGRGPTRDGRIKPDIAAPGvNILTASPG---GGYTTRSG 398

                          90
                  ....*....|....*.
gi 887218382  448 TSMSSPNACGGIALVL 463
Cdd:cd07478   399 TSVAAAIVAGACALLL 414
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 225-436 6.69e-07

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: 53.39  E-value: 6.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  225 RNYKEAQEYSSFGTAEMLNYsvnIYDDGNLLSIVTS--GGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLS 302
Cdd:cd07478    42 GPPPGGYYGGGEYTEEIINA---ALASDNPYDIVPSrdENGHGTHVAGIAAGNGDNNPDFKGVAPEAELIVVKLKQAKKY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  303 TMETG--------TGLIRAmIEVINHKCDL------VNYSYGeATHWPNSGR--ICEVINEAVWKHNTIYVSSAGNNGpc 366
Cdd:cd07478   119 LREFYedvpfyqeTDIMLA-IKYLYDKALElnkplvINISLG-TNFGSHDGTslLERYIDAISRLRGIAVVVGAGNEG-- 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  367 lstvGCPGGTTSSVIGVGAYVSPDMMVAEyslREKLPANQYtWssrGPSADGaLGVSISAPGGAIASVPN 436
Cdd:cd07478   195 ----NTQHHHSGGIVPNGETKTVELNVGE---GEKGFNLEI-W---GDFPDR-FSVSIISPSGESSGRIN 252
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
 260-463 1.14e-06

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: 51.14  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  260 SGGAHGTHVASIAAGHfpeEPERNGVAPGAQILSIK-IGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSY-GEathwPN 337
Cdd:cd05561    34 APSAHGTAVASLLAGA---GAQRPGLLPGADLYGADvFGRAGGGEGASALALARALDWLAEQGVRVVNISLaGP----PN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  338 sgRICEVINEAVWKHNTIYVSSAGNNGPclSTVGCPGGTTSSVIGVGAYVSpdmmvaeyslREKLpanqYTWSSRGPsad 417
Cdd:cd05561   107 --ALLAAAVAAAAARGMVLVAAAGNDGP--AAPPLYPAAYPGVIAVTAVDA----------RGRL----YREANRGA--- 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 887218382  418 galGVSISAPGGAIASVPNwtLRGTQLMNGTSMSSPNACGGIALVL 463
Cdd:cd05561   166 ---HVDFAAPGVDVWVAAP--GGGYRYVSGTSFAAPFVTAALALLL 206
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 243-364 1.71e-05

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


Pssm-ID: 468750 [Multi-domain]  Cd Length: 1099  Bit Score: 49.39  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  243 NYSVNIYDDGNLLSIVTSGGAHGTHVASIAAghfpeepernGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKC 322
Cdd:NF040809  137 NEDINEAINGNKYIPISTTSMHGTHVAGIAA----------SIANEASIIVVRVGRRQTDTFSKSTEFMRAIKFILDKAL 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 887218382  323 DL-----VNYSYG--EATHWPNSgRICEVINE--AVWKHNTiyVSSAGNNG 364
Cdd:NF040809  207 ELkmpvaINISYGsnEGSHRGLS-LFEQYIDDmcLFWKNNI--VVAAGNNA 254
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 262-454 5.39e-04

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: 43.45  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  262 GAHGTHVASIAA-GHFpEEPERNGVAPGAQILSIKI------GDTRLSTMETGTgLIRAMIEVINHKCDLVNYSYGEATH 334
Cdd:cd04847    38 LGHGTAVAGLALyGDL-TLPGNGLPRPGCRLESVRVlppngeNDPELYGDITLR-AIRRAVIQNPDIVRVFNLSLGSPLP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  335 wPNSGRICE---VINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSV---------IGVGAYVSPDMMVAEYSLREKL 402
Cdd:cd04847   116 -IDDGRPSSwaaALDQLAAEYDVLFVVSAGNLGDDDAADGPPRIQDDEIedpadsvnaLTVGAITSDDDITDRARYSAVG 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 887218382  403 PANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPN 454
Cdd:cd04847   195 PAPAGATTSSGPGSPGPIKPDVVAFGGNLAYDPSGNAADGDLSLLTTLSSPS 246
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 262-464 6.23e-04

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: 42.84  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  262 GAHGTHVASIAAGhfpeepeRNGVAPGAQILSIKIGDTRLST--METGTGLIRAM-IEVINH--------KCDLVNYSYG 330
Cdd:cd07488    37 DDHATLVASIMGG-------RDGGLPAVNLYSSAFGIKSNNGqwQECLEAQQNGNnVKIINHsygeglkrDPRAVLYGYA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  331 EATHWpnsgricevINEAVWKHNTIYVSSAGNNGPCLSTVG-CPGGTTSS-VIGVGAYV-SPDMMVAEYSLREKLPANQY 407
Cdd:cd07488   110 LLSLY---------LDWLSRNYEVINVFSAGNQGKEKEKFGgISIPTLAYnSIVVGSTDrNGDRFFASDVSNAGSEINSY 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 887218382  408 twssrgpsadGALGVSISAPGgaiasvPNWTLRGTQL--MNGTSMSSPNACGGIALVLS 464
Cdd:cd07488   181 ----------GRRKVLIVAPG------SNYNLPDGKDdfVSGTSFSAPLVTGIIALLLE 223
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 31-77 7.04e-04

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: 43.13  E-value: 7.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 887218382   31 PEYDGRGVLIAVLDTGVDPGAP---GMQVTTdgkpkiidiIDTTGSGDVN 77
Cdd:cd07480     3 SPFTGAGVRVAVLDTGIDLTHPafaGRDITT---------KSFVGGEDVQ 43
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
 380-511 3.62e-03

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: 41.69  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218382  380 VIGVGAYvspDMMvaeyslreklpaNQYTW--SSRGPSADGALGVSISAPG-GAIASVPNWTLrGTqlMNGTSMSSPNAC 456
Cdd:NF040809  977 IITVGAY---DTI------------NNSIWptSSRGPTIRNIQKPDIVAPGvNIIAPYPGNTY-AT--ITGTSAAAAHVS 1038

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 887218382  457 GGIALVLSGLKANNvDYT----VHSVRRALENTAIKADNIEV--FAQGHGIIQVDKAYDYL 511
Cdd:NF040809 1039 GVAALYLQYTLVER-RYPnqafTQKIKTFMQAGATRSTNIEYpnTTSGYGLLNIRGMFDQL 1098
 
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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