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Conserved domains on  [gi|440923791|pdb|1SBH|A]
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Chain A, SUBTILISIN 8397+1

Protein Classification

S8 family peptidase( domain architecture ID 10165578)

S8 family peptidase is a subtilisin-like serine protease containing an Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to Bacillus subtilis major intracellular serine protease

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
25-253 2.67e-115

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: 330.65  E-value: 2.67e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDLK--VAGGASFVPSETNPFQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGADGSG 102
Cdd:cd07477   1 GVKVAVIDTGIDSSHPDLKlnIVGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVGVVGVAPEADLYAVKVLNDDGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      103 QYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTvgYPAKYPSVIAVGAVDS 182
Cdd:cd07477  81 TYSDIIAGIEWAIENGMDIINMSLGGPSDSPALREAIKKAYAAGILVVAAAGNSGNGDSSYD--YPAKYPSVIAVGAVDS 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1SBH_A      183 SNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT 253
Cdd:cd07477 159 NNNRASFSSTGPEVELAAPGVDILSTYPNNDYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
 
Name Accession Description Interval E-value
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
25-253 2.67e-115

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: 330.65  E-value: 2.67e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDLK--VAGGASFVPSETNPFQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGADGSG 102
Cdd:cd07477   1 GVKVAVIDTGIDSSHPDLKlnIVGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVGVVGVAPEADLYAVKVLNDDGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      103 QYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTvgYPAKYPSVIAVGAVDS 182
Cdd:cd07477  81 TYSDIIAGIEWAIENGMDIINMSLGGPSDSPALREAIKKAYAAGILVVAAAGNSGNGDSSYD--YPAKYPSVIAVGAVDS 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1SBH_A      183 SNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT 253
Cdd:cd07477 159 NNNRASFSSTGPEVELAAPGVDILSTYPNNDYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
13-273 7.05e-84

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 258.49  E-value: 7.05e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       13 APALHSQGYTGSNVKVAVIDSGIDSSHPDL--KVAGGASFVPSETNPfQDNNSHGTHVAGTVAA-LDNSIGVLGVAPSAS 89
Cdd:COG1404  98 AAGSSAAGLTGAGVTVAVIDTGVDADHPDLagRVVGGYDFVDGDGDP-SDDNGHGTHVAGIIAAnGNNGGGVAGVAPGAK 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       90 LYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPS--GSAALKAAVDKAVASGVVVVAAAGNEGTSgsSSTVGY 167
Cdd:COG1404 177 LLPVRVLDDNGSGTTSDIAAAIDWAADNGADVINLSLGGPAdgYSDALAAAVDYAVDKGVLVVAAAGNSGSD--DATVSY 254
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      168 PAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVR 247
Cdd:COG1404 255 PAAYPNVIAVGAVDANGQLASFSNYGPKVDVAAPGVDILSTYPGGGYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVR 334
                       250       260
                ....*....|....*....|....*..
1SBH_A      248 SSLENTTTYLGDS-FYYGKGLINVQAA 273
Cdd:COG1404 335 AILLNTATPLGAPgPYYGYGLLADGAA 361
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
23-266 4.74e-62

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: 197.30  E-value: 4.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         23 GSNVKVAVIDSGIDSSHPDLKVAGGASFVPSE-------------TNPFQDNNSHGTHVAGTVAALDN-SIGVLGVAPSA 88
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPeasvdfnnewddpRDDIDDKNGHGTHVAGIIAAGGNnSIGVSGVAPGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         89 SLYAVKVLGaDGSGQYSWIINGIEWAIANNMDVINMSLGGPS---GSAALKAAVDKAVASGVVVV---AAAGNEGTSG-S 161
Cdd:pfam00082  81 KILGVRVFG-DGGGTDAITAQAISWAIPQGADVINMSWGSDKtdgGPGSWSAAVDQLGGAEAAGSlfvWAAGNGSPGGnN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        162 SSTVGYPAKYPSVIAVGAVD--SSNQRASFSSVGPEL------DVMAPGVSI*------------STLPGNKYGAYSGTS 221
Cdd:pfam00082 160 GSSVGYPAQYKNVIAVGAVDeaSEGNLASFSSYGPTLdgrlkpDIVAPGGNITggnisstlltttSDPPNQGYDSMSGTS 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
1SBH_A        222 MASPHVAGAAALILSKHPNWTNTQVRSSLENTTTYLGD---SFYYGKG 266
Cdd:pfam00082 240 MATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDaglDRLFGYG 287
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
22-273 6.22e-50

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


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 167.89  E-value: 6.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         22 TGSNVKVAVIDSGIDSsHPDLK--VAGGASFVPSeTNPFQDNNSHGTHVAGTVAAL-DNSIGVLGVAPSASLYAVKVLGA 98
Cdd:TIGR03921  11 TGAGVTVAVIDTGVDD-HPRLPglVLPGGDFVGS-GDGTDDCDGHGTLVAGIIAGRpGEGDGFSGVAPDARILPIRQTSA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         99 DGS--------GQYSWIINGIEWAIANNMDVINMSL------GGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSST 164
Cdd:TIGR03921  89 AFEpdegtsgvGDLGTLAKAIRRAADLGADVINISLvaclpaGSGADDPELGAAVRYALDKGVVVVAAAGNTGGDGQKTT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        165 VGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGA-YSGTSMASPHVAGAAALILSKHPNWTN 243
Cdd:TIGR03921 169 VVYPAWYPGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGENIVSLSPGGDGLAtTSGTSFAAPFVSGTAALVRSRFPDLTA 248
                         250       260       270
                  ....*....|....*....|....*....|...
1SBH_A        244 TQVRSSLENTTTY---LGDSFYYGKGLINVQAA 273
Cdd:TIGR03921 249 AQVRRRIEATADHparGGRDDYVGYGVVDPVAA 281
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
24-257 1.26e-28

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 114.68  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        24 SNVKVAVIDSGIDSSHPDLK---------VAG----------------GASFVPSETNPFqDNNSHGTHVAGTVAAL-DN 77
Cdd:PTZ00262 316 NDTNICVIDSGIDYNHPDLHdnidvnvkeLHGrkgidddnngnvddeyGANFVNNDGGPM-DDNYHGTHVSGIISAIgNN 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        78 SIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNeG 157
Cdd:PTZ00262 395 NIGIVGVDKRSKLIICKALDSHKLGRLGDMFKCFDYCISREAHMINGSFSFDEYSGIFNESVKYLEEKGILFVVSASN-C 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       158 TSGSSSTVGYP-------AKYP--------SVIAVGAV--DSSNQRA----SFSSvGPELDVMAPGVSI*STLPGNKYGA 216
Cdd:PTZ00262 474 SHTKESKPDIPkcdldvnKVYPpilskklrNVITVSNLikDKNNQYSlspnSFYS-AKYCQLAAPGTNIYSTFPKNSYRK 552
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
1SBH_A       217 YSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTYL 257
Cdd:PTZ00262 553 LNGTSMAAPHVAAIASLILSINPSLSYEEVIRILKESIVQL 593
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
164-271 4.10e-14

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: 72.12  E-value: 4.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        164 TVGYPAKYPSVIAVGAVDSSNQRA-SFSSVGPEL------DVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILS 236
Cdd:NF040809  967 TINYPAVQDDIITVGAYDTINNSIwPTSSRGPTIrniqkpDIVAPGVNIIAPYPGNTYATITGTSAAAAHVSGVAALYLQ 1046
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1SBH_A        237 ------KHPNWTNTQ-VRSSLENTTTYLGDSFY----YGKGLINVQ 271
Cdd:NF040809 1047 ytlverRYPNQAFTQkIKTFMQAGATRSTNIEYpnttSGYGLLNIR 1092
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
164-235 1.52e-10

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: 61.33  E-value: 1.52e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1SBH_A        164 TVGYPAKYPSVIAVGAVDS-SNQRASFSSVGP------ELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALIL 235
Cdd:NF040809  395 TVTVPGTASRVITVGSFNSrTDVVSVFSGEGDiengiyKPDLLAPGENIVSYLPGGTTGALTGTSMATPHVTGVCSLLM 473
 
Name Accession Description Interval E-value
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
25-253 2.67e-115

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: 330.65  E-value: 2.67e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDLK--VAGGASFVPSETNPFQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGADGSG 102
Cdd:cd07477   1 GVKVAVIDTGIDSSHPDLKlnIVGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVGVVGVAPEADLYAVKVLNDDGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      103 QYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTvgYPAKYPSVIAVGAVDS 182
Cdd:cd07477  81 TYSDIIAGIEWAIENGMDIINMSLGGPSDSPALREAIKKAYAAGILVVAAAGNSGNGDSSYD--YPAKYPSVIAVGAVDS 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1SBH_A      183 SNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT 253
Cdd:cd07477 159 NNNRASFSSTGPEVELAAPGVDILSTYPNNDYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
13-273 7.05e-84

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 258.49  E-value: 7.05e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       13 APALHSQGYTGSNVKVAVIDSGIDSSHPDL--KVAGGASFVPSETNPfQDNNSHGTHVAGTVAA-LDNSIGVLGVAPSAS 89
Cdd:COG1404  98 AAGSSAAGLTGAGVTVAVIDTGVDADHPDLagRVVGGYDFVDGDGDP-SDDNGHGTHVAGIIAAnGNNGGGVAGVAPGAK 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       90 LYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPS--GSAALKAAVDKAVASGVVVVAAAGNEGTSgsSSTVGY 167
Cdd:COG1404 177 LLPVRVLDDNGSGTTSDIAAAIDWAADNGADVINLSLGGPAdgYSDALAAAVDYAVDKGVLVVAAAGNSGSD--DATVSY 254
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      168 PAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVR 247
Cdd:COG1404 255 PAAYPNVIAVGAVDANGQLASFSNYGPKVDVAAPGVDILSTYPGGGYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVR 334
                       250       260
                ....*....|....*....|....*..
1SBH_A      248 SSLENTTTYLGDS-FYYGKGLINVQAA 273
Cdd:COG1404 335 AILLNTATPLGAPgPYYGYGLLADGAA 361
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
22-258 2.95e-78

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: 237.54  E-value: 2.95e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       22 TGSNVKVAVIDSGIDSSHPDL---KVAGGASFVPSETNPfQDNNSHGTHVAGTVAA-LDNSIGVLGVAPSASLYAVKVLG 97
Cdd:cd07484  26 GGSGVTVAVVDTGVDPTHPDLlkvKFVLGYDFVDNDSDA-MDDNGHGTHVAGIIAAaTNNGTGVAGVAPKAKIMPVKVLD 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       98 ADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSgsssTVGYPAKYPSVIAV 177
Cdd:cd07484 105 ANGSGSLADIANGIRYAADKGAKVINLSLGGGLGSTALQEAINYAWNKGVVVVAAAGNEGVS----SVSYPAAYPGAIAV 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      178 GAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPnWTNTQVRSSLENTTTYL 257
Cdd:cd07484 181 AATDQDDKRASFSNYGKWVDVSAPGGGILSTTPDGDYAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTADDI 259

                .
1SBH_A      258 G 258
Cdd:cd07484 260 G 260
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
24-255 2.51e-68

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: 212.44  E-value: 2.51e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       24 SNVKVAVIDSGIDSSHPDLK---------VAG---------------GASFVpSETNPFQDNNSHGTHVAGTVAAL-DNS 78
Cdd:cd07473   2 GDVVVAVIDTGVDYNHPDLKdnmwvnpgeIPGngidddgngyvddiyGWNFV-NNDNDPMDDNGHGTHVAGIIGAVgNNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       79 IGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGT 158
Cdd:cd07473  81 IGIAGVAWNVKIMPLKFLGADGSGTTSDAIKAIDYAVDMGAKIINNSWGGGGPSQALRDAIARAIDAGILFVAAAGNDGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      159 SGSSSTVgYPAKY--PSVIAVGAVDSSNQRASFSSVGPE-LDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALIL 235
Cdd:cd07473 161 NNDKTPT-YPASYdlDNIISVAATDSNDALASFSNYGKKtVDLAAPGVDILSTSPGGGYGYMSGTSMATPHVAGAAALLL 239
                       250       260
                ....*....|....*....|
1SBH_A      236 SKHPNWTNTQVRSSLENTTT 255
Cdd:cd07473 240 SLNPNLTAAQIKDAILSSAD 259
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
23-266 4.74e-62

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: 197.30  E-value: 4.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         23 GSNVKVAVIDSGIDSSHPDLKVAGGASFVPSE-------------TNPFQDNNSHGTHVAGTVAALDN-SIGVLGVAPSA 88
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPeasvdfnnewddpRDDIDDKNGHGTHVAGIIAAGGNnSIGVSGVAPGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         89 SLYAVKVLGaDGSGQYSWIINGIEWAIANNMDVINMSLGGPS---GSAALKAAVDKAVASGVVVV---AAAGNEGTSG-S 161
Cdd:pfam00082  81 KILGVRVFG-DGGGTDAITAQAISWAIPQGADVINMSWGSDKtdgGPGSWSAAVDQLGGAEAAGSlfvWAAGNGSPGGnN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        162 SSTVGYPAKYPSVIAVGAVD--SSNQRASFSSVGPEL------DVMAPGVSI*------------STLPGNKYGAYSGTS 221
Cdd:pfam00082 160 GSSVGYPAQYKNVIAVGAVDeaSEGNLASFSSYGPTLdgrlkpDIVAPGGNITggnisstlltttSDPPNQGYDSMSGTS 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
1SBH_A        222 MASPHVAGAAALILSKHPNWTNTQVRSSLENTTTYLGD---SFYYGKG 266
Cdd:pfam00082 240 MATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDaglDRLFGYG 287
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
21-255 6.15e-62

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: 195.81  E-value: 6.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       21 YTGSNVKVAVIDSGIDSSHPDL--KVAGGASFVPSETNpfQDNNSHGTHVAGTVAALDNsigvlGVAPSASLYAVKVLGA 98
Cdd:cd04077  22 STGSGVDVYVLDTGIRTTHVEFggRAIWGADFVGGDPD--SDCNGHGTHVAGTVGGKTY-----GVAKKANLVAVKVLDC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       99 DGSGQYSWIINGIEWAIAN-----NMDVINMSLGGPsGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTvgyPAKYPS 173
Cdd:cd04077  95 NGSGTLSGIIAGLEWVANDatkrgKPAVANMSLGGG-ASTALDAAVAAAVNAGVVVVVAAGNSNQDACNYS---PASAPE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      174 VIAVGAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGA--YSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLE 251
Cdd:cd04077 171 AITVGATDSDDARASFSNYGSCVDIFAPGVDILSAWIGSDTATatLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLL 250

                ....
1SBH_A      252 NTTT 255
Cdd:cd04077 251 NLAT 254
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
23-255 1.32e-61

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: 195.11  E-value: 1.32e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       23 GSNVKVAVIDSGIDSSHPDLKVAGGA-----SFVPSETNPFqDNNSHGTHVAGTVAALDNSIG--VLGVAPSASLYAVKV 95
Cdd:cd07487   1 GKGITVAVLDTGIDAPHPDFDGRIIRfadfvNTVNGRTTPY-DDNGHGTHVAGIIAGSGRASNgkYKGVAPGANLVGVKV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       96 LGADGSGQYSWIINGIEWAIAN----NMDVINMSLGGPSGSA----ALKAAVDKAVASGVVVVAAAGNEGtsGSSSTVGY 167
Cdd:cd07487  80 LDDSGSGSESDIIAGIDWVVENnekyNIRVVNLSLGAPPDPSygedPLCQAVERLWDAGIVVVVAAGNSG--PGPGTITS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      168 PAKYPSVIAVGAVDSSNQR----ASFSSVGPEL------DVMAPGVSI*S---------TLPGNKYGAYSGTSMASPHVA 228
Cdd:cd07487 158 PGNSPKVITVGAVDDNGPHddgiSYFSSRGPTGdgrikpDVVAPGENIVScrspggnpgAGVGSGYFEMSGTSMATPHVS 237
                       250       260
                ....*....|....*....|....*..
1SBH_A      229 GAAALILSKHPNWTNTQVRSSLENTTT 255
Cdd:cd07487 238 GAIALLLQANPILTPDEVKCILRDTAT 264
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
23-273 1.89e-58

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: 188.31  E-value: 1.89e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       23 GSNVKVAVIDSGIDSSHPDL--------KVAGGASFVPSETNPF--------------QDNNSHGTHVAGTVAALDNSIG 80
Cdd:cd07474   1 GKGVKVAVIDTGIDYTHPDLggpgfpndKVKGGYDFVDDDYDPMdtrpypsplgdasaGDATGHGTHVAGIIAGNGVNVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       81 VL-GVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSA--ALKAAVDKAVASGVVVVAAAGNEG 157
Cdd:cd07474  81 TIkGVAPKADLYAYKVLGPGGSGTTDVIIAAIEQAVDDGMDVINLSLGSSVNGPddPDAIAINNAVKAGVVVVAAAGNSG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      158 TSGSssTVGYPAKYPSVIAVGAVDS-----SNQRASFSSVGPEL-------DVMAPGVSI*STLP--GNKYGAYSGTSMA 223
Cdd:cd07474 161 PAPY--TIGSPATAPSAITVGASTVadvaeADTVGPSSSRGPPTsdsaikpDIVAPGVDIMSTAPgsGTGYARMSGTSMA 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
1SBH_A      224 SPHVAGAAALILSKHPNWTNTQVRSSLENTTTYLGDSFY-------YGKGLINVQAA 273
Cdd:cd07474 239 APHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSDGvvypvsrQGAGRVDALRA 295
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
16-274 1.24e-56

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: 183.96  E-value: 1.24e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       16 LHSQGYTGSNVKVAVIDSGIDSSHPDL--------KVAGGASFVPSETNPF---------QDNNSHGTHVAGTVAALDNS 78
Cdd:cd07489   5 LHAEGITGKGVKVAVVDTGIDYTHPALggcfgpgcKVAGGYDFVGDDYDGTnppvpdddpMDCQGHGTHVAGIIAANPNA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       79 IGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSG--SAALKAAVDKAVASGVVVVAAAGNE 156
Cdd:cd07489  85 YGFTGVAPEATLGAYRVFGCSGSTTEDTIIAAFLRAYEDGADVITASLGGPSGwsEDPWAVVASRIVDAGVVVTIAAGND 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      157 GTSGSSSTvGYPAKYPSVIAVGAVDSsnqraSFSSVGP--EL----DVMAPGVSI*STLPGNK--YGAYSGTSMASPHVA 228
Cdd:cd07489 165 GERGPFYA-SSPASGRGVIAVASVDS-----YFSSWGPtnELylkpDVAAPGGNILSTYPLAGggYAVLSGTSMATPYVA 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
1SBH_A      229 GAAALILS-KHPNWTNTQVRSSLENTTTYL----GDSFYY--------GKGLINVQAAA 274
Cdd:cd07489 239 GAAALLIQaRHGKLSPAELRDLLASTAKPLpwsdGTSALPdlapvaqqGAGLVNAYKAL 297
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
26-253 2.62e-52

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: 170.84  E-value: 2.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       26 VKVAVIDSGIDSSHPDLKVAGG-------ASFVPSETNPFQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGA 98
Cdd:cd00306   1 VTVAVIDTGVDPDHPDLDGLFGggdggndDDDNENGPTDPDDGNGHGTHVAGIIAASANNGGGVGVAPGAKLIPVKVLDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       99 DGSGQYSWIINGIEWAIA-NNMDVINMSLGGPS--GSAALKAAVDKAVASGVVVV-AAAGNEGTSGsSSTVGYPAKYPSV 174
Cdd:cd00306  81 DGSGSSSDIAAAIDYAAAdQGADVINLSLGGPGspPSSALSEAIDYALAKLGVLVvAAAGNDGPDG-GTNIGYPAASPNV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      175 IAVGAVDSSNQRAS-FSSVGPELDVMAPGVSI*S--TLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLE 251
Cdd:cd00306 160 IAVGAVDRDGTPASpSSNGGAGVDIAAPGGDILSspTTGGGGYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAALL 239

                ..
1SBH_A      252 NT 253
Cdd:cd00306 240 ST 241
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
26-253 8.35e-52

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: 169.45  E-value: 8.35e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       26 VKVAVIDSGIDSSHPDL----KVAGGASFVPSETNPFQDNNsHGTHVAGTVAAL-DNSIGVLGVAPSASLYAVKVLGADG 100
Cdd:cd07498   1 VVVAIIDTGVDLNHPDLsgkpKLVPGWNFVSNNDPTSDIDG-HGTACAGVAAAVgNNGLGVAGVAPGAKLMPVRIADSLG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      101 SGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVV-----AAAGNEGTSgsssTVGYPAKYPSVI 175
Cdd:cd07498  80 YAYWSDIAQAITWAADNGADVISNSWGGSDSTESISSAIDNAATYGRNGKggvvlFAAGNSGRS----VSSGYAANPSVI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      176 AVGAVDSSNQRASFSSVGPELDVMAPGVSI*STL---------PGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQV 246
Cdd:cd07498 156 AVAATDSNDARASYSNYGNYVDLVAPGVGIWTTGtgrgsagdyPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAEV 235

                ....*..
1SBH_A      247 RSSLENT 253
Cdd:cd07498 236 EDILTST 242
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
22-273 6.22e-50

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


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 167.89  E-value: 6.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         22 TGSNVKVAVIDSGIDSsHPDLK--VAGGASFVPSeTNPFQDNNSHGTHVAGTVAAL-DNSIGVLGVAPSASLYAVKVLGA 98
Cdd:TIGR03921  11 TGAGVTVAVIDTGVDD-HPRLPglVLPGGDFVGS-GDGTDDCDGHGTLVAGIIAGRpGEGDGFSGVAPDARILPIRQTSA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A         99 DGS--------GQYSWIINGIEWAIANNMDVINMSL------GGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSST 164
Cdd:TIGR03921  89 AFEpdegtsgvGDLGTLAKAIRRAADLGADVINISLvaclpaGSGADDPELGAAVRYALDKGVVVVAAAGNTGGDGQKTT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        165 VGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGA-YSGTSMASPHVAGAAALILSKHPNWTN 243
Cdd:TIGR03921 169 VVYPAWYPGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGENIVSLSPGGDGLAtTSGTSFAAPFVSGTAALVRSRFPDLTA 248
                         250       260       270
                  ....*....|....*....|....*....|...
1SBH_A        244 TQVRSSLENTTTY---LGDSFYYGKGLINVQAA 273
Cdd:TIGR03921 249 AQVRRRIEATADHparGGRDDYVGYGVVDPVAA 281
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
21-240 1.37e-48

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: 162.93  E-value: 1.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       21 YTGSNVKVAVIDSGIDSSHPDLKVAGG--ASFVPSETNpfQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGA 98
Cdd:cd07480   5 FTGAGVRVAVLDTGIDLTHPAFAGRDIttKSFVGGEDV--QDGHGHGTHCAGTIFGRDVPGPRYGVARGAEIALIGKVLG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       99 DGSGQYSWIINGIEWAIANNMDVINMSLG-------------GPSGSAALKA----AVDKAVASGVVVVAAAGNEGT--- 158
Cdd:cd07480  83 DGGGGDGGILAGIQWAVANGADVISMSLGadfpglvdqgwppGLAFSRALEAyrqrARLFDALMTLVAAQAALARGTliv 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      159 --SGSSST-------VGYPAKYPSVIAVGAVDSSNQRASFSSVGP----ELDVMAPGVSI*STLPGNKYGAYSGTSMASP 225
Cdd:cd07480 163 aaAGNESQrpagippVGNPAACPSAMGVAAVGALGRTGNFSAVANfsngEVDIAAPGVDIVSAAPGGGYRSMSGTSMATP 242
                       250
                ....*....|....*
1SBH_A      226 HVAGAAALILSKHPN 240
Cdd:cd07480 243 HVAGVAALWAEALPK 257
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
25-253 2.53e-46

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: 156.68  E-value: 2.53e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDL--KVAGGASFV-------------------------------PSETNPFQDNNSHGTHVAGT 71
Cdd:cd07496   1 GVVVAVLDTGVLFHHPDLagVLLPGYDFIsdpaiandgdgrdsdptdpgdwvtgddvppgGFCGSGVSPSSWHGTHVAGT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       72 VAAL-DNSIGVLGVAPSASLYAVKVLGADGsGQYSWIINGIEWAI----------ANNMDVINMSLGGP-SGSAALKAAV 139
Cdd:cd07496  81 IAAVtNNGVGVAGVAWGARILPVRVLGKCG-GTLSDIVDGMRWAAglpvpgvpvnPNPAKVINLSLGGDgACSATMQNAI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      140 DKAVASGVVVVAAAGNEGtsgSSSTVGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSI*STLPGNK------ 213
Cdd:cd07496 160 NDVRARGVLVVVAAGNEG---SSASVDAPANCRGVIAVGATDLRGQRASYSNYGPAVDVSAPGGDCASDVNGDGypdsnt 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
1SBH_A      214 ---------YGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT 253
Cdd:cd07496 237 gttspggstYGFLQGTSMAAPHVAGVAALMKSVNPSLTPAQIESLLQST 285
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
14-275 2.65e-45

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: 155.50  E-value: 2.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       14 PALHSQGYTGSNVKVAVIDSGIDSSHPDLKVA--------------------GGASFVpSETNPF----QDNN------- 62
Cdd:cd07475   1 PLWDKGGYKGEGMVVAVIDSGVDPTHDAFRLDddskakyseefeakkkkagiGYGKYY-NEKVPFaynyADNNddilded 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       63 ---SHGTHVAGTVAA----LDNSIGVLGVAPSASLYAVKVLG-ADGSGQYSWII-NGIEWAIANNMDVINMSLGGPSGS- 132
Cdd:cd07475  80 dgsSHGMHVAGIVAGngdeEDNGEGIKGVAPEAQLLAMKVFSnPEGGSTYDDAYaKAIEDAVKLGADVINMSLGSTAGFv 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      133 ---AALKAAVDKAVASGVVVVAAAGNEGTSGS------------SSTVGYPAKYPSVIAVGAVDSS------NQRASFSS 191
Cdd:cd07475 160 dldDPEQQAIKRAREAGVVVVVAAGNDGNSGSgtskplatnnpdTGTVGSPATADDVLTVASANKKvpnpngGQMSGFSS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      192 VG--PEL----DVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILS----KHPNWTNTQ----VRSSLENTTTYL 257
Cdd:cd07475 240 WGptPDLdlkpDITAPGGNIYSTVNDNTYGYMSGTSMASPHVAGASALVKQrlkeKYPKLSGEElvdlVKNLLMNTATPP 319
                       330       340
                ....*....|....*....|....*..
1SBH_A      258 GDSFYY---------GKGLINVQAAAQ 275
Cdd:cd07475 320 LDSEDTktyysprrqGAGLIDVAKAIA 346
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
26-254 9.92e-45

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: 151.55  E-value: 9.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       26 VKVAVIDSGIDSSHPDL--KVAGGASFVPSET---NPFQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLgADG 100
Cdd:cd07490   2 VTVAVLDTGVDADHPDLagRVAQWADFDENRRisaTEVFDAGGHGTHVSGTIGGGGAKGVYIGVAPEADLLHGKVL-DDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      101 SGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKA----AVDKAVASGVVVVAAAGNEGTSGSsstvgyPAKYPSVIA 176
Cdd:cd07490  81 GGSLSQIIAGMEWAVEKDADVVSMSLGGTYYSEDPLEeaveALSNQTGALFVVSAGNEGHGTSGS------PGSAYAALS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      177 VGAVDSSNQRASFSSVGPEL-----------------DVMAPGVSI*STL----PGNKYGAYSGTSMASPHVAGAAALIL 235
Cdd:cd07490 155 VGAVDRDDEDAWFSSFGSSGaslvsapdsppdeytkpDVAAPGVDVYSARqganGDGQYTRLSGTSMAAPHVAGVAALLA 234
                       250
                ....*....|....*....
1SBH_A      236 SKHPNWTNTQVRSSLENTT 254
Cdd:cd07490 235 AAHPDLSPEQIKDALTETA 253
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
23-255 4.69e-43

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: 147.52  E-value: 4.69e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       23 GSNVKVAVIDSGIDSSHPDLKVAGG---ASFVPSETNPFQ---------DNNSHGTHVAGTVAALDNSIGVLGVAPSASL 90
Cdd:cd07481   1 GTGIVVANIDTGVDWTHPALKNKYRgwgGGSADHDYNWFDpvgntplpyDDNGHGTHTMGTMVGNDGDGQQIGVAPGARW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       91 YAVKVLGADGsGQYSWIINGIEWAIA------------NNMDVINMSLGGPSG-SAALKAAVDKAVASGVVVVAAAGNEG 157
Cdd:cd07481  81 IACRALDRNG-GNDADYLRCAQWMLAptdsagnpadpdLAPDVINNSWGGPSGdNEWLQPAVAAWRAAGIFPVFAAGNDG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      158 TSGSSSTvGYPAKYPSVIAVGAVDSSNQRASFSSVGPEL------DVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAA 231
Cdd:cd07481 160 PRCSTLN-APPANYPESFAVGATDRNDVLADFSSRGPSTygrikpDISAPGVNIRSAVPGGGYGSSSGTSMAAPHVAGVA 238
                       250       260
                ....*....|....*....|....
1SBH_A      232 ALILSKHPNWTNTQVRSSLENTTT 255
Cdd:cd07481 239 ALLWSANPSLIGDVDATEAILTET 262
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
22-255 4.64e-40

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: 139.77  E-value: 4.64e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       22 TGSNVKVAVIDSGIDSSHPDL---KVAGGASFVPSETNPF--QDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVL 96
Cdd:cd04848   1 TGAGVKVGVIDSGIDLSHPEFagrVSEASYYVAVNDAGYAsnGDGDSHGTHVAGVIAAARDGGGMHGVAPDATLYSARAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       97 GADGSGQ-YSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAG---------------NEGTSG 160
Cdd:cd04848  81 ASAGSTFsDADIAAAYDFLAASGVRIINNSWGGNPAIDTVSTTYKGSAATQGNTLLAALaraanagglfvfaagNDGQAN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      161 SSST-VGYPAKYP----SVIAVGAVDSSNQRASFSSVGPELD-----VMAPGVSI*STLP--GNKYGAYSGTSMASPHVA 228
Cdd:cd04848 161 PSLAaAALPYLEPelegGWIAVVAVDPNGTIASYSYSNRCGVaanwcLAAPGENIYSTDPdgGNGYGRVSGTSFAAPHVS 240
                       250       260
                ....*....|....*....|....*..
1SBH_A      229 GAAALILSKHPNWTNTQVRSSLENTTT 255
Cdd:cd04848 241 GAAALLAQKFPWLTADQVRQTLLTTAT 267
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
25-253 2.82e-39

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


Pssm-ID: 173808 [Multi-domain]  Cd Length: 294  Bit Score: 138.65  E-value: 2.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDLK---VAGGASFVP------------SETNPFQDNNSHGTHVAGTVAALDNsigVLGVAPSAS 89
Cdd:cd07482   1 KVTVAVIDSGIDPDHPDLKnsiSSYSKNLVPkggydgkeagetGDINDIVDKLGHGTAVAGQIAANGN---IKGVAPGIG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       90 LYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGG-----------PSGSAALKAAVDKAVASGVVVVAAAGNEGT 158
Cdd:cd07482  78 IVSYRVFGSCGSAESSWIIKAIIDAADDGVDVINLSLGGyliiggeyeddDVEYNAYKKAINYAKSKGSIVVAAAGNDGL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      159 SGSSS------------------TVGYPAKYPSVIAVGAVDSSNQRASFSSVG-PELDVMAPG----------------- 202
Cdd:cd07482 158 DVSNKqelldflssgddfsvngeVYDVPASLPNVITVSATDNNGNLSSFSNYGnSRIDLAAPGgdfllldqygkekwvnn 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
1SBH_A      203 -----VSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNT-QVRSSLENT 253
Cdd:cd07482 238 glmtkEQILTTAPEGGYAYMYGTSLAAPKVSGALALIIDKNPLKKPPdEAIRILYNT 294
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
20-253 6.08e-39

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: 137.23  E-value: 6.08e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       20 GYTGSNVKVAVIDSGIDSSHPDLK----------VAGGASFVPSETNPFQDN---NSHGTHVAGTVAALDNSIGVLG--- 83
Cdd:cd07485   6 GTGGPGIIVAVVDTGVDGTHPDLQgngdgdgydpAVNGYNFVPNVGDIDNDVsvgGGHGTHVAGTIAAVNNNGGGVGgia 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       84 ----VAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSG---SAALKAAVDkavASGVVVVAAAGNE 156
Cdd:cd07485  86 gaggVAPGVKIMSIQIFAGRYYVGDDAVAAAIVYAADNGAVILQNSWGGTGGgiySPLLKDAFD---YFIENAGGSPLDG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      157 GT----SGSSSTVG--YPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGV-SI*STLP------GNKYGAYSGTSMA 223
Cdd:cd07485 163 GIvvfsAGNSYTDEhrFPAAYPGVIAVAALDTNDNKASFSNYGRWVDIAAPGVgTILSTVPkldgdgGGNYEYLSGTSMA 242
                       250       260       270
                ....*....|....*....|....*....|.
1SBH_A      224 SPHVAGAAALILSKHPNWTNT-QVRSSLENT 253
Cdd:cd07485 243 APHVSGVAALVLSKFPDVFTPeQIRKLLEES 273
Peptidases_S8_4 cd05561
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ...
26-260 1.66e-35

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: 127.02  E-value: 1.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       26 VKVAVIDSGIDSSHPDLK---VAGGASFVPSETNPfqdnNSHGTHVAGTVAAldNSIGVLGVAPSASLYAVKVLGADGSG 102
Cdd:cd05561   1 VRVGMIDTGIDTAHPALSavvIARLFFAGPGAPAP----SAHGTAVASLLAG--AGAQRPGLLPGADLYGADVFGRAGGG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      103 QYSW---IINGIEWAIANNMDVINMSLGGPsGSAALKAAVDKAVASGVVVVAAAGNEGtsgSSSTVGYPAKYPSVIAVGA 179
Cdd:cd05561  75 EGASalaLARALDWLAEQGVRVVNISLAGP-PNALLAAAVAAAAARGMVLVAAAGNDG---PAAPPLYPAAYPGVIAVTA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      180 VDSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTnTQVRSSLENTTTYLGD 259
Cdd:cd05561 151 VDARGRLYREANRGAHVDFAAPGVDVWVAAPGGGYRYVSGTSFAAPFVTAALALLLQASPLAP-DDARARLAATAKDLGP 229

                .
1SBH_A      260 S 260
Cdd:cd05561 230 P 230
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
26-255 1.14e-33

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: 122.06  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       26 VKVAVIDSGIDSSHPDLKV--AGGASFVPSE----TNPFQDNNSHGTHVAGTVAALdnsigvlgvAPSASLYAVKVLGAD 99
Cdd:cd07492   2 VRVAVIDSGVDTDHPDLGNlaLDGEVTIDLEiivvSAEGGDKDGHGTACAGIIKKY---------APEAEIGSIKILGED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      100 GSGQYSWIINGIEWAIANNMDVINMSLGGPS--GSAALKAAVDKAVASGVVVVAAAGNEGTSGssstvGYPAKYPSVIAV 177
Cdd:cd07492  73 GRCNSFVLEKALRACVENDIRIVNLSLGGPGdrDFPLLKELLEYAYKAGGIIVAAAPNNNDIG-----TPPASFPNVIGV 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1SBH_A      178 GavdSSNQRASFSSVGPELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTT 255
Cdd:cd07492 148 K---SDTADDPKSFWYIYVEFSADGVDIIAPAPHGRYLTVSGNSFAAPHVTGMVALLLSEKPDIDANDLKRLLQRLAV 222
Peptidases_S8_3 cd04852
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ...
7-250 1.68e-33

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: 123.86  E-value: 1.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        7 GVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDL-----------------------------KVAGGASFV------ 51
Cdd:cd04852  13 GLPGAWGGSLLGAANAGEGIIIGVLDTGIWPEHPSFadvgggpyphtwpgdcvtgedfnpfscnnKLIGARYFSdgyday 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       52 -----PSETNPFQDNNSHGTHVAGTVA--ALDNSIG-------VLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIAN 117
Cdd:cd04852  93 ggfnsDGEYRSPRDYDGHGTHTASTAAgnVVVNASVggfafgtASGVAPRARIAVYKVCWPDGGCFGSDILAAIDQAIAD 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      118 NMDVINMSLGGPSGS--------AALkAAVDKAVASGVVVvaaagneGTSG-SSSTVGYPAkyPSVIAVGAvdssnqras 188
Cdd:cd04852 173 GVDVISYSIGGGSPDpyedpiaiAFL-HAVEAGIFVAASA-------GNSGpGASTVPNVA--PWVTTVAA--------- 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1SBH_A      189 fSSVGPelDVMAPGVSI----------*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSL 250
Cdd:cd04852 234 -STLKP--DIAAPGVDIlaawtpegadPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSAL 302
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
26-253 3.83e-33

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: 121.64  E-value: 3.83e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       26 VKVAVIDSGIDSSHP---------DLKVAGGASFVPSETNPFQDNNSHGTHVAGTVAAldNSIGVL-GVAPSASLYAVKV 95
Cdd:cd07493   2 ITIAVIDAGFPKVHEafafkhlfkNLRILGEYDFVDNSNNTNYTDDDHGTAVLSTMAG--YTPGVMvGTAPNASYYLART 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       96 lgADGSGQY-----SWIInGIEWAIANNMDVINMSLG-----GPSGS----------AALKAAVDKAVASGVVVVAAAGN 155
Cdd:cd07493  80 --EDVASETpveedNWVA-AAEWADSLGVDIISSSLGyttfdNPTYSytyadmdgktSFISRAANIAASKGMLVVNSAGN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      156 EGtSGSSSTVGYPAKYPSVIAVGAVDSSNQRASFSSVGPELD------VMAPGVSI*STLPGNKYGAYSGTSMASPHVAG 229
Cdd:cd07493 157 EG-STQWKGIGAPADAENVLSVGAVDANGNKASFSSIGPTADgrlkpdVMALGTGIYVINGDGNITYANGTSFSCPLIAG 235
                       250       260
                ....*....|....*....|....
1SBH_A      230 AAALILSKHPNWTNTQVRSSLENT 253
Cdd:cd07493 236 LIACLWQAHPNWTNLQIKEAILKS 259
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
19-240 1.00e-30

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: 115.24  E-value: 1.00e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       19 QGYTGSNVKVAVIDSGIDSSHPDLK-VAGGASFVPSETNpfQDNNSHGTHVAGTVAALDNSigVLGVAPSASLYAVKVLG 97
Cdd:cd07479   3 LGYTGAGVKVAVFDTGLAKDHPHFRnVKERTNWTNEKTL--DDGLGHGTFVAGVIASSREQ--CLGFAPDAEIYIFRVFT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       98 ADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAalKAAVDKAVASGVVVVAAAGNEGTSGS-SSTVGYPAKYPSVIA 176
Cdd:cd07479  79 NNQVSYTSWFLDAFNYAILTKIDVLNLSIGGPDFMD--KPFVDKVWELTANNIIMVSAIGNDGPlYGTLNNPADQMDVIG 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1SBH_A      177 VGAVDSSNQRASFSSVGP---EL---------DVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPN 240
Cdd:cd07479 157 VGGIDFDDNIARFSSRGMttwELpggygrvkpDIVTYGSGVYGSKLKGGCRALSGTSVASPVVAGAVALLLSTVPE 232
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
25-247 6.16e-30

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: 114.00  E-value: 6.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDLK---------VAG---------------GASFVPSE-------------TNPFQDNN----- 62
Cdd:cd07483   2 TVIVAVLDSGVDIDHEDLKgklwinkkeIPGngidddnngyiddvnGWNFLGQYdprrivgddpydlTEKGYGNNdvngp 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       63 ----SHGTHVAGTVAAL-DNSIGVLGVAPSASLYAVKVLGaDGSGQYSWIINGIEWAIANNMDVINMSLGG--PSGSAAL 135
Cdd:cd07483  82 isdaDHGTHVAGIIAAVrDNGIGIDGVADNVKIMPLRIVP-NGDERDKDIANAIRYAVDNGAKVINMSFGKsfSPNKEWV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      136 KAAVDKAVASGVVVVAAAGNEGTSgSSSTVGYPAKYP--------SVIAVGAV---DSSNQRASFSSVGPE-LDVMAPGV 203
Cdd:cd07483 161 DDAIKYAESKGVLIVHAAGNDGLD-LDITPNFPNDYDknggepanNFITVGASskkYENNLVANFSNYGKKnVDVFAPGE 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
1SBH_A      204 SI*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVR 247
Cdd:cd07483 240 RIYSTTPDNEYETDSGTSMAAPVVSGVAALIWSYYPNLTAKEVK 283
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
24-257 1.26e-28

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 114.68  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        24 SNVKVAVIDSGIDSSHPDLK---------VAG----------------GASFVPSETNPFqDNNSHGTHVAGTVAAL-DN 77
Cdd:PTZ00262 316 NDTNICVIDSGIDYNHPDLHdnidvnvkeLHGrkgidddnngnvddeyGANFVNNDGGPM-DDNYHGTHVSGIISAIgNN 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        78 SIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNeG 157
Cdd:PTZ00262 395 NIGIVGVDKRSKLIICKALDSHKLGRLGDMFKCFDYCISREAHMINGSFSFDEYSGIFNESVKYLEEKGILFVVSASN-C 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       158 TSGSSSTVGYP-------AKYP--------SVIAVGAV--DSSNQRA----SFSSvGPELDVMAPGVSI*STLPGNKYGA 216
Cdd:PTZ00262 474 SHTKESKPDIPkcdldvnKVYPpilskklrNVITVSNLikDKNNQYSlspnSFYS-AKYCQLAAPGTNIYSTFPKNSYRK 552
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
1SBH_A       217 YSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTYL 257
Cdd:PTZ00262 553 LNGTSMAAPHVAAIASLILSINPSLSYEEVIRILKESIVQL 593
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
16-242 1.73e-27

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: 107.65  E-value: 1.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       16 LHSQGYTGSNVKVAVIDSGIDSSHPDLK----VAGGASFVPSETNP---FQDNNSHGTHVAGTVAAL-DNSIGVLGVAPS 87
Cdd:cd04059  31 AWEQGITGKGVTVAVVDDGLEITHPDLKdnydPEASYDFNDNDPDPtprYDDDNSHGTRCAGEIAAVgNNGICGVGVAPG 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       88 ASLYAVKVLGADGSGqyswIINGIEWAIANNM-DVINMSLG--------GPSGSAALKAAVDKAVASGVVVVA----AAG 154
Cdd:cd04059 111 AKLGGIRMLDGDVTD----VVEAESLGLNPDYiDIYSNSWGpdddgktvDGPGPLAQRALENGVTNGRNGKGSifvwAAG 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      155 NEGTSGSSSTV-GYpAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPG----------VSI*STLPGNKYGAYSGTSMA 223
Cdd:cd04059 187 NGGNLGDNCNCdGY-NNSIYTISVSAVTANGVRASYSEVGSSVLASAPSggsgnpeasiVTTDLGGNCNCTSSHNGTSAA 265
                       250
                ....*....|....*....
1SBH_A      224 SPHVAGAAALILSKHPNWT 242
Cdd:cd04059 266 APLAAGVIALMLEANPNLT 284
Peptidases_S8_thiazoline_oxidase_subtilisin-like_p cd07476
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ...
16-236 1.65e-23

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: 96.24  E-value: 1.65e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       16 LHSQGYTGSNVKVAVIDSGIDSSHPDLKvagGASFVPSET-----NPFQDNNSHGTHVAGTVAALDNSiGVLGVAPSASL 90
Cdd:cd07476   2 LFAFGGGDPRITIAILDGPVDRTHPCFR---GANLTPLFTyaaaaCQDGGASAHGTHVASLIFGQPCS-SVEGIAPLCRG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       91 YAVKVlGADGSGQYSW--IINGIEWAIANNMDVINMSLGGPS----GSAALKAAVDKAVASGVVVVAAAGNEGtsgsSST 164
Cdd:cd07476  78 LNIPI-FAEDRRGCSQldLARAINLALEQGAHIINISGGRLTqtgeADPILANAVAMCQQNNVLIVAAAGNEG----CAC 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1SBH_A      165 VGYPAKYPSVIAVGAVDSSNQRASFSSVGPELD---VMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILS 236
Cdd:cd07476 153 LHVPAALPSVLAVGAMDDDGLPLKFSNWGADYRkkgILAPGENILGAALGGEVVRRSGTSFAAAIVAGIAALLLS 227
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
20-234 2.77e-22

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: 93.55  E-value: 2.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       20 GYTGSNVKVAVIDSGIDSSHPDLKVAGGASFVP---------SETNPFQDNNSHGTHVAGTVA--ALDNSIGVL--GVAP 86
Cdd:cd04842   3 GLTGKGQIVGVADTGLDTNHCFFYDPNFNKTNLfhrkivrydSLSDTKDDVDGHGTHVAGIIAgkGNDSSSISLykGVAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       87 SASLYAVKVlgADGSGQYSWIING---IEWAIANNMDVINMSLGGPSGSA--ALKAAVDKAVASGVVVVA--AAGNEGTS 159
Cdd:cd04842  83 KAKLYFQDI--GDTSGNLSSPPDLnklFSPMYDAGARISSNSWGSPVNNGytLLARAYDQFAYNNPDILFvfSAGNDGND 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      160 GSSsTVGYPAKYPSVIAVGAV---------------DSSNQRASFSSVGPEL------DVMAPGVSI*STLPG------- 211
Cdd:cd04842 161 GSN-TIGSPATAKNVLTVGASnnpsvsngegglgqsDNSDTVASFSSRGPTYdgrikpDLVAPGTGILSARSGgggigdt 239
                       250       260
                ....*....|....*....|....*
1SBH_A      212 --NKYGAYSGTSMASPHVAGAAALI 234
Cdd:cd04842 240 sdSAYTSKSGTSMATPLVAGAAALL 264
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
21-235 2.23e-19

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: 86.90  E-value: 2.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       21 YTGSNVKVAVIDSGIDSSHPDLKVAGG------------------------------------ASFVPSETNPFQDNNSH 64
Cdd:cd07478   1 LTGKGVLVGIIDTGIDYLHPEFRNEDGttrilyiwdqtipggpppggyygggeyteeiinaalASDNPYDIVPSRDENGH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       65 GTHVAGTVAAL-DNSIGVLGVAPSASLYAVKVLGADGSG----------QYSWIINGIEWAI--ANNMD---VINMSLG- 127
Cdd:cd07478  81 GTHVAGIAAGNgDNNPDFKGVAPEAELIVVKLKQAKKYLrefyedvpfyQETDIMLAIKYLYdkALELNkplVINISLGt 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      128 --GP-SGSAALKAAVDKAVASGVVVVAAAG-NEGT--------------------------------------------- 158
Cdd:cd07478 161 nfGShDGTSLLERYIDAISRLRGIAVVVGAgNEGNtqhhhsggivpngetktvelnvgegekgfnleiwgdfpdrfsvsi 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      159 ---SGSSS------------------------------------------------------------------------ 163
Cdd:cd07478 241 ispSGESSgrinpgiggsesykfvfegttvyvyyylpepytgdqlifirfknikpgiwkirltgvsitdgrfdawlpsrg 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      164 ---------------TVGYPAKYPSVIAVGAVDSSNQR-ASFSSVGPEL------DVMAPGVSI*STLPGNKYGAYSGTS 221
Cdd:cd07478 321 llsentrflepdpytTLTIPGTARSVITVGAYNQNNNSiAIFSGRGPTRdgrikpDIAAPGVNILTASPGGGYTTRSGTS 400
                       410
                ....*....|....
1SBH_A      222 MASPHVAGAAALIL 235
Cdd:cd07478 401 VAAAIVAGACALLL 414
Peptidases_S8_Tripeptidyl_Aminopeptidase_II cd04857
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ...
60-257 3.38e-18

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: 83.49  E-value: 3.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       60 DNNSHGTHVAGTVAALDNSIGVL-GVAPSASLYAVKV----LGADGSGQYswIINGIEWAIANNMDVINMSLGGPSGSA- 133
Cdd:cd04857 183 DSGAHGTHVAGIAAAHFPEEPERnGVAPGAQIVSIKIgdtrLGSMETGTA--LVRAMIAAIETKCDLINMSYGEATHWPn 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      134 ------ALKAAVDKAVASGVVVVaaagneGTSGSS-STVGYPA-KYPSVIAVGA-VDSSNQRASFS-------------S 191
Cdd:cd04857 261 sgriieLMNEAVNKHGVIFVSSA------GNNGPAlSTVGAPGgTTSSVIGVGAyVSPEMMAAEYSlreklpgnqytwsS 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      192 VGPELD------VMAPGVSI*S----TLPGNKYgaYSGTSMASPHVAGAAALILS--KHPN--WTNTQVRSSLENTTTYL 257
Cdd:cd04857 335 RGPTADgalgvsISAPGGAIASvpnwTLQGSQL--MNGTSMSSPNACGGIALLLSglKAEGipYTPYSVRRALENTAKKL 412
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
11-253 2.95e-17

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


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 79.83  E-value: 2.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       11 IKAPALHSQGYTGSNVKVAVIDSGIdSSHPDLKVAGGASFV---PSETNPFQDNNSHGThvaGTVAALdnsigvLGVAPS 87
Cdd:cd07494   8 LNATRVHQRGITGRGVRVAMVDTGF-YAHPFFESRGYQVRVvlaPGATDPACDENGHGT---GESANL------FAIAPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       88 ASLYAVKVLGADGSGqyswIINGIEWAIANNMDVINMSLG------GPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGS 161
Cdd:cd07494  78 AQFIGVKLGGPDLVN----SVGAFKKAISLSPDIISNSWGydlrspGTSWSRSLPNALKALAATLQDAVARGIVVVFSAG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      162 SSTVGYPAKYPSVIAVGAV--------DSSNQRASFSS--------------VGpeLDVMA--------PGVSI------ 205
Cdd:cd07494 154 NGGWSFPAQHPEVIAAGGVfvdedgarRASSYASGFRSkiypgrqvpdvcglVG--MLPHAaylmlpvpPGSQLdrscaa 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
1SBH_A      206 --*STLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT 253
Cdd:cd07494 232 fpDGTPPNDGWGVFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKT 281
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
20-275 1.86e-16

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: 76.95  E-value: 1.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       20 GYTGSNVKVAVIDSGIDS-SHPDLKVAGGAsfVPSETNPFQDNNS------HGTHVAGTVAaldnsigvlGVAPSASLYA 92
Cdd:cd05562   1 GVDGTGIKIGVISDGFDGlGDAADDQASGD--LPGNVNVLGDLDGgsgggdEGRAMLEIIH---------DIAPGAELAF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       93 VKVLGADGSgqyswIINGIEWAIANNMDVINMSLG---------GPSgSAALKAAVDKAVASGVVVVaaagneGTSGSSS 163
Cdd:cd05562  70 HTAGGGELD-----FAAAIRALAAAGADIIVDDIGylnepffqdGPI-AQAVDEVVASPGVLYFSSA------GNDGQSG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      164 TVGYPAKYPSVIAVGAVDSSNQRA------------SFSSVG-----PEL----DVMAP-GVSI*STLPGNKYGAYSGTS 221
Cdd:cd05562 138 SIFGHAAAPGAIAVGAVDYGNTPAfgsdpapggtpsSFDPVGirlptPEVrqkpDVTAPdGVNGTVDGDGDGPPNFFGTS 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
1SBH_A      222 MASPHVAGAAALILSKHPNWTNTQVRSSLENTTTYL---GDSFYYGKGLINVQAAAQ 275
Cdd:cd05562 218 AAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMgepGYDNASGSGLVDADRAVA 274
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
25-236 2.53e-16

Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173816  Cd Length: 247  Bit Score: 76.22  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       25 NVKVAVIDSGIDSSHPDL--KVAGGASFVPSETNPFQDN------NSHGTHVAgtvaaldNSIgvLGVAPSASLYAVKV- 95
Cdd:cd07491   4 RIKVALIDDGVDILDSDLqgKIIGGKSFSPYEGDGNKVSpyyvsaDGHGTAMA-------RMI--CRICPSAKLYVIKLe 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       96 -LGADGSGQYS----WIINGIEWAIANNMDVINMS------LGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSST 164
Cdd:cd07491  75 dRPSPDSNKRSitpqSAAKAIEAAVEKKVDIISMSwtikkpEDNDNDINELENAIKEALDRGILLFCSASDQGAFTGDTY 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1SBH_A      165 vGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSI---*STLPGNKYGAYSGTSMASPHVAGAAALILS 236
Cdd:cd07491 155 -PPPAARDRIFRIGAADEDGGADAPVGDEDRVDYILPGENVearDRPPLSNSFVTHTGSSVATALAAGLAALILY 228
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
19-255 3.08e-15

Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173792  Cd Length: 277  Bit Score: 73.50  E-value: 3.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       19 QGYTGSNVKVAVIDSGIDSSHPDLKvagGASFVPSETNPFQDNNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGA 98
Cdd:cd04843  11 PGGSGQGVTFVDIEQGWNLNHEDLV---GNGITLISGLTDQADSDHGTAVLGIIVAKDNGIGVTGIAHGAQAAVVSSTRV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       99 DGSGQYswIINGIEWAIANNMDVINMSLGGPSGSA-------------ALKAAVDKAVASGVVVVAAAGN----EGTSGS 161
Cdd:cd04843  88 SNTADA--ILDAADYLSPGDVILLEMQTGGPNNGYpplpveyeqanfdAIRTATDLGIIVVEAAGNGGQDldapVYNRGP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      162 SSTVGYPAKYPS-VIAVGAVDSSNQ--RASFSSVGPELDVMAPGVSI*ST-------LPGNK---YGAYSGTSMASPHVA 228
Cdd:cd04843 166 ILNRFSPDFRDSgAIMVGAGSSTTGhtRLAFSNYGSRVDVYGWGENVTTTgygdlqdLGGENqdyTDSFSGTSSASPIVA 245
                       250       260       270
                ....*....|....*....|....*....|..
1SBH_A      229 GAAALILS-----KHPNWTNTQVRSSLENTTT 255
Cdd:cd04843 246 GAAASIQGiakqkGGTPLTPIEMRELLTATGT 277
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
164-271 4.10e-14

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: 72.12  E-value: 4.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A        164 TVGYPAKYPSVIAVGAVDSSNQRA-SFSSVGPEL------DVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALILS 236
Cdd:NF040809  967 TINYPAVQDDIITVGAYDTINNSIwPTSSRGPTIrniqkpDIVAPGVNIIAPYPGNTYATITGTSAAAAHVSGVAALYLQ 1046
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1SBH_A        237 ------KHPNWTNTQ-VRSSLENTTTYLGDSFY----YGKGLINVQ 271
Cdd:NF040809 1047 ytlverRYPNQAFTQkIKTFMQAGATRSTNIEYpnttSGYGLLNIR 1092
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
27-240 1.74e-11

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


Pssm-ID: 173793 [Multi-domain]  Cd Length: 291  Bit Score: 63.09  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       27 KVAVIDSGIDSSHPDLKVAGGASFVPSETN-PFQDNNSHGTHVAGtvAALDNSIGVLG---VAPSASLYAVKVLGADG-S 101
Cdd:cd04847   2 IVCVLDSGINRGHPLLAPALAEDDLDSDEPgWTADDLGHGTAVAG--LALYGDLTLPGnglPRPGCRLESVRVLPPNGeN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      102 GQYSW---IINGIEWAIANN---MDVINMSLGGPS-----GSAALKAAVDKAVASGV---------VVVAAAGNEGTSGS 161
Cdd:cd04847  80 DPELYgdiTLRAIRRAVIQNpdiVRVFNLSLGSPLpiddgRPSSWAAALDQLAAEYDvlfvvsagnLGDDDAADGPPRIQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      162 SSTVGYPAkyPSV--IAVGAVDSSN--------------QRASFSSVGPEL------DVMAPG----------------- 202
Cdd:cd04847 160 DDEIEDPA--DSVnaLTVGAITSDDditdrarysavgpaPAGATTSSGPGSpgpikpDVVAFGgnlaydpsgnaadgdls 237
                       250       260       270
                ....*....|....*....|....*....|....*....
1SBH_A      203 VSI*STLPGNKYGAY-SGTSMASPHVAGAAALILSKHPN 240
Cdd:cd04847 238 LLTTLSSPSGGGFVTvGGTSFAAPLAARLAAGLFAELPE 276
germ_prot_CspBA NF040809
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ...
164-235 1.52e-10

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: 61.33  E-value: 1.52e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1SBH_A        164 TVGYPAKYPSVIAVGAVDS-SNQRASFSSVGP------ELDVMAPGVSI*STLPGNKYGAYSGTSMASPHVAGAAALIL 235
Cdd:NF040809  395 TVTVPGTASRVITVGSFNSrTDVVSVFSGEGDiengiyKPDLLAPGENIVSYLPGGTTGALTGTSMATPHVTGVCSLLM 473
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
23-236 7.01e-09

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: 55.55  E-value: 7.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       23 GSNVKVAVIDSGIDSSHPDLKVAGGASFVPSETNP----------------FQDNNSHGTHVAGTVA-------ALDNSI 79
Cdd:cd07497   1 GEGVVIAIVDTGVDYSHPDLDIYGNFSWKLKFDYKayllpgmdkwggfyviMYDFFSHGTSCASVAAgrgkmeyNLYGYT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       80 G---VLGVAPSASLYAVKVLG----------ADGSGQYSWIINGIeWAIANNMDVINMSLG--------GPSGSAALKAA 138
Cdd:cd07497  81 GkflIRGIAPDAKIAAVKALWfgdviyawlwTAGFDPVDRKLSWI-YTGGPRVDVISNSWGisnfaytgYAPGLDISSLV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      139 VDKAVASGVVVVAAAGNEGTSGsSSTVGYPAKYPSVIAVGAVDSSNQR---------------ASFSSVGPEL------D 197
Cdd:cd07497 160 IDALVTYTGVPIVSAAGNGGPG-YGTITAPGAASLAISVGAATNFDYRpfylfgylpggsgdvVSWSSRGPSIagdpkpD 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
1SBH_A      198 VMAPG-VSI*STLPGNKYGAYS---------GTSMASPHVAGAAALILS 236
Cdd:cd07497 239 LAAIGaFAWAPGRVLDSGGALDgneafdlfgGTSMATPMTAGSAALVIS 287
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
56-240 1.42e-06

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: 48.23  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       56 NPFQDNnsHGTHVAGTVAALDnsigvlGVAPSASLYAVKVlgadGSGQYSWIINGIEWA--IANNMDVINMSLGGPSGSA 133
Cdd:cd07488  33 NNTFDD--HATLVASIMGGRD------GGLPAVNLYSSAF----GIKSNNGQWQECLEAqqNGNNVKIINHSYGEGLKRD 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      134 AlKAAVDKAVASGVVVVAAAGNEG-----TSGSSSTVGYPAKYPSV-------IAVGAVDSSNQRASFSSV--------- 192
Cdd:cd07488 101 P-RAVLYGYALLSLYLDWLSRNYEvinvfSAGNQGKEKEKFGGISIptlaynsIVVGSTDRNGDRFFASDVsnagseins 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1SBH_A      193 --GPELDVMAPGVSI*sTLPGNKYGAYSGTSMASPHVAGAAALILSKHPN 240
Cdd:cd07488 180 ygRRKVLIVAPGSNY--NLPDGKDDFVSGTSFSAPLVTGIIALLLEFYDR 227
COG4934 COG4934
Serine protease, subtilase family [Posttranslational modification, protein turnover, ...
18-238 4.83e-03

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


Pssm-ID: 443961 [Multi-domain]  Cd Length: 519  Bit Score: 38.02  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       18 SQGYTGSNVKVAVIDSGIDSSHP-DLKV----AGGASFVPSETNPFQDNNSHGTHVAGTV-AALDNSIgVLGVAPSASLY 91
Cdd:COG4934 181 SAGTTGTGQTIAIVDAGGDPYIPsDLATydsqFGLPPPTLTVVNVDGGYDPSGDPSGWAGeTALDVEM-AHAIAPGAKIV 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A       92 AVKVLGADGSgqyswIINGIEWAIANNM-DVINMSLGGP--SGSAALKAAVDKAVASGVVVVA--------AAGNEGTSG 160
Cdd:COG4934 260 VYEAPNTDAG-----LLDAYAYAVNDNLaDVISNSWGGPesSASPSSLAAYDQLFAQAAAQGItvfaasgdSGAYDGTGT 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SBH_A      161 SSSTVGYPAKYPSVIAVG----AVDSSNQRASFSSVGPELDVMAP-----GVSI*STLP--------------------- 210
Cdd:COG4934 335 GGLSVDFPASSPYVTAVGgttlSVDSNGRYSSETAWNDGSSYGGYggsggGVSTVFPKPswqtgtgvpagggrgvpdvsa 414
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
1SBH_A      211 -------------GNKYGAYSGTSMASPHVAGAAALILSKH 238
Cdd:COG4934 415 dadpntgylvyvtGSGWGVVGGTSAAAPLWAGLLALINQAL 455
 
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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