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Conserved domains on  [gi|1622467294|ref|NP_001356777|]
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serine protease 56 isoform 1 precursor [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
105-335 2.31e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 283.78  E-value: 2.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 105 IVGGSAAPPGAWPWLVRLQLG-GQPLCGGVLVAASWVLTAAHCFVGAPNELlWTVTLAE---GSRGEQAEEVPVNRILPH 180
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGShdlSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPEAEAVREARVPLLSTDTCRRAL 260
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622467294 261 GPGLR-PSTMLCAGYLAGGVDSCQGDSGGPLTCSEPGprpREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDWLQEQ 335
Cdd:cd00190   160 SYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
178-602 1.20e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.17  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  178 LPHPKFDPRTFHNdlALVQL--------WTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPEAEAVREARVP 249
Cdd:COG3321    823 LRRGEDELAQLLT--ALAQLwvagvpvdWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAAL 900
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  250 LLSTDTCRRALGPGLRPSTMLCAGYLAGGVDSC---QGDSGGPLTCSEPGPRPREVLFGVTSWGDGCGEPGKPGVYTRVA 326
Cdd:COG3321    901 AAALAAALLALAAAAAAALALAAAALAALLALValaAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAA 980
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  327 VFKDWLQEQMSAASSSREPSCRELLAWDPPQELQADAARLCAFYARLCPGSQGACARLAHQQCLQRRRRCELRSLAHTLL 406
Cdd:COG3321    981 AAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAA 1060
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  407 GLLRNAQELLGPRPGLRRLAPALALPAPALRESPLHPARELRLHSGSRAAGTRFPKRRPEPRGEANGCPGLEPLRQKLAA 486
Cdd:COG3321   1061 LALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAAL 1140
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  487 LQGAHAWILQVPSEHLAMNFHEVLADLGSKTLTGLFRAWVRAGLGGRHVAFSGLVGLEPATLARSLPRLLVQALQAFRVA 566
Cdd:COG3321   1141 AAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAA 1220
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1622467294  567 ALAEGEPEGPWMDVGQGPGLERKGHHPLNPQVPPAR 602
Cdd:COG3321   1221 AALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
105-335 2.31e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 283.78  E-value: 2.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 105 IVGGSAAPPGAWPWLVRLQLG-GQPLCGGVLVAASWVLTAAHCFVGAPNELlWTVTLAE---GSRGEQAEEVPVNRILPH 180
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGShdlSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPEAEAVREARVPLLSTDTCRRAL 260
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622467294 261 GPGLR-PSTMLCAGYLAGGVDSCQGDSGGPLTCSEPGprpREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDWLQEQ 335
Cdd:cd00190   160 SYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
104-331 2.09e-91

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 281.49  E-value: 2.09e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  104 RIVGGSAAPPGAWPWLVRLQL-GGQPLCGGVLVAASWVLTAAHCFVGAPNELlWTVTLAE--GSRGEQAEEVPVNRILPH 180
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGShdLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFED-GPEAEAVREARVPLLSTDTCRRA 259
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622467294  260 LGPGLR-PSTMLCAGYLAGGVDSCQGDSGGPLTCSepgpRPREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDW 331
Cdd:smart00020 160 YSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCN----DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
105-332 2.10e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 236.96  E-value: 2.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 105 IVGGSAAPPGAWPWLVRLQL-GGQPLCGGVLVAASWVLTAAHCFVGAPNellWTVTLAEGSRGEQ---AEEVPVNRILPH 180
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLReggEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPeAEAVREARVPLLSTDTCRRAL 260
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622467294 261 GPGLRPsTMLCAGYlaGGVDSCQGDSGGPLTCSepgprpREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDWL 332
Cdd:pfam00089 157 GGTVTD-TMICAGA--GGKDACQGDSGGPLVCS------DGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
94-340 1.72e-70

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.38  E-value: 1.72e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  94 STANVTRAHGRIVGGSAAPPGAWPWLVRLQLGG---QPLCGGVLVAASWVLTAAHCFVGAPNEllwTVTLAEGS---RGE 167
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS---DLRVVIGStdlSTS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 168 QAEEVPVNRILPHPKFDPRTFHNDLALVQLWTPVSpggSARPVCLPQEPQEPPAGTACAIAGWGALFED-GPEAEAVREA 246
Cdd:COG5640    97 GGTVVKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 247 RVPLLSTDTCrrALGPGLRPSTMLCAGYLAGGVDSCQGDSGGPLTCSEPGprpREVLFGVTSWGDGCGEPGKPGVYTRVA 326
Cdd:COG5640   174 DVPVVSDATC--AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGG---GWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|....
gi 1622467294 327 VFKDWLQEQMSAAS 340
Cdd:COG5640   249 AYRDWIKSTAGGLG 262
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
178-602 1.20e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.17  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  178 LPHPKFDPRTFHNdlALVQL--------WTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPEAEAVREARVP 249
Cdd:COG3321    823 LRRGEDELAQLLT--ALAQLwvagvpvdWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAAL 900
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  250 LLSTDTCRRALGPGLRPSTMLCAGYLAGGVDSC---QGDSGGPLTCSEPGPRPREVLFGVTSWGDGCGEPGKPGVYTRVA 326
Cdd:COG3321    901 AAALAAALLALAAAAAAALALAAAALAALLALValaAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAA 980
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  327 VFKDWLQEQMSAASSSREPSCRELLAWDPPQELQADAARLCAFYARLCPGSQGACARLAHQQCLQRRRRCELRSLAHTLL 406
Cdd:COG3321    981 AAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAA 1060
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  407 GLLRNAQELLGPRPGLRRLAPALALPAPALRESPLHPARELRLHSGSRAAGTRFPKRRPEPRGEANGCPGLEPLRQKLAA 486
Cdd:COG3321   1061 LALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAAL 1140
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  487 LQGAHAWILQVPSEHLAMNFHEVLADLGSKTLTGLFRAWVRAGLGGRHVAFSGLVGLEPATLARSLPRLLVQALQAFRVA 566
Cdd:COG3321   1141 AAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAA 1220
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1622467294  567 ALAEGEPEGPWMDVGQGPGLERKGHHPLNPQVPPAR 602
Cdd:COG3321   1221 AALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
105-335 2.31e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 283.78  E-value: 2.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 105 IVGGSAAPPGAWPWLVRLQLG-GQPLCGGVLVAASWVLTAAHCFVGAPNELlWTVTLAE---GSRGEQAEEVPVNRILPH 180
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGShdlSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPEAEAVREARVPLLSTDTCRRAL 260
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622467294 261 GPGLR-PSTMLCAGYLAGGVDSCQGDSGGPLTCSEPGprpREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDWLQEQ 335
Cdd:cd00190   160 SYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
104-331 2.09e-91

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 281.49  E-value: 2.09e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  104 RIVGGSAAPPGAWPWLVRLQL-GGQPLCGGVLVAASWVLTAAHCFVGAPNELlWTVTLAE--GSRGEQAEEVPVNRILPH 180
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGShdLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFED-GPEAEAVREARVPLLSTDTCRRA 259
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622467294  260 LGPGLR-PSTMLCAGYLAGGVDSCQGDSGGPLTCSepgpRPREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDW 331
Cdd:smart00020 160 YSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCN----DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
105-332 2.10e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 236.96  E-value: 2.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 105 IVGGSAAPPGAWPWLVRLQL-GGQPLCGGVLVAASWVLTAAHCFVGAPNellWTVTLAEGSRGEQ---AEEVPVNRILPH 180
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLReggEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 181 PKFDPRTFHNDLALVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPeAEAVREARVPLLSTDTCRRAL 260
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622467294 261 GPGLRPsTMLCAGYlaGGVDSCQGDSGGPLTCSepgprpREVLFGVTSWGDGCGEPGKPGVYTRVAVFKDWL 332
Cdd:pfam00089 157 GGTVTD-TMICAGA--GGKDACQGDSGGPLVCS------DGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
94-340 1.72e-70

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.38  E-value: 1.72e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  94 STANVTRAHGRIVGGSAAPPGAWPWLVRLQLGG---QPLCGGVLVAASWVLTAAHCFVGAPNEllwTVTLAEGS---RGE 167
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS---DLRVVIGStdlSTS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 168 QAEEVPVNRILPHPKFDPRTFHNDLALVQLWTPVSpggSARPVCLPQEPQEPPAGTACAIAGWGALFED-GPEAEAVREA 246
Cdd:COG5640    97 GGTVVKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 247 RVPLLSTDTCrrALGPGLRPSTMLCAGYLAGGVDSCQGDSGGPLTCSEPGprpREVLFGVTSWGDGCGEPGKPGVYTRVA 326
Cdd:COG5640   174 DVPVVSDATC--AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGG---GWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|....
gi 1622467294 327 VFKDWLQEQMSAAS 340
Cdd:COG5640   249 AYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
120-312 1.29e-08

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.07  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 120 VRLQL-GGQPLCGGVLVAASWVLTAAHCFVGAPNELLWT-VTLAEGSRGEQAEEVPVNRILPHPKFDPRT-FHNDLALVQ 196
Cdd:COG3591     3 GRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnIVFVPGYNGGPYGTATATRFRVPPGWVASGdAGYDYALLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 197 LWTPVspgGSARPVCLPQEPQEPPAGTACAIAGWGAlfeDGPEAEAVREARvPLLSTDTcrralgpglrpstmlcaGYLA 276
Cdd:COG3591    83 LDEPL---GDTTGWLGLAFNDAPLAGEPVTIIGYPG---DRPKDLSLDCSG-RVTGVQG-----------------NRLS 138
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622467294 277 GGVDSCQGDSGGPLTCSEPGPRpreVLFGVTSWGDG 312
Cdd:COG3591   139 YDCDTTGGSSGSPVLDDSDGGG---RVVGVHSAGGA 171
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
116-229 2.36e-04

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 40.99  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 116 WPWLVRLQLGGQPLCGGVLVAASWVLTAAHCFVGAPNELLWTVTLAEGSRGEQAEEVPVNRILphpKFDPR--TFHNDLA 193
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGAKTLKSIEGPYEQIV---RVDCRhdIPESEIS 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622467294 194 LVQLWTPVSPGGSARPVCLPQEPQEPPAGTACAIAG 229
Cdd:pfam09342  78 LLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
178-602 1.20e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.17  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  178 LPHPKFDPRTFHNdlALVQL--------WTPVSPGGSARPVCLPQEPQEPPAGTACAIAGWGALFEDGPEAEAVREARVP 249
Cdd:COG3321    823 LRRGEDELAQLLT--ALAQLwvagvpvdWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAAL 900
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  250 LLSTDTCRRALGPGLRPSTMLCAGYLAGGVDSC---QGDSGGPLTCSEPGPRPREVLFGVTSWGDGCGEPGKPGVYTRVA 326
Cdd:COG3321    901 AAALAAALLALAAAAAAALALAAAALAALLALValaAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAA 980
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  327 VFKDWLQEQMSAASSSREPSCRELLAWDPPQELQADAARLCAFYARLCPGSQGACARLAHQQCLQRRRRCELRSLAHTLL 406
Cdd:COG3321    981 AAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAA 1060
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  407 GLLRNAQELLGPRPGLRRLAPALALPAPALRESPLHPARELRLHSGSRAAGTRFPKRRPEPRGEANGCPGLEPLRQKLAA 486
Cdd:COG3321   1061 LALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAAL 1140
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294  487 LQGAHAWILQVPSEHLAMNFHEVLADLGSKTLTGLFRAWVRAGLGGRHVAFSGLVGLEPATLARSLPRLLVQALQAFRVA 566
Cdd:COG3321   1141 AAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAA 1220
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1622467294  567 ALAEGEPEGPWMDVGQGPGLERKGHHPLNPQVPPAR 602
Cdd:COG3321   1221 AALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
132-290 5.38e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.79  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 132 GVLVAAS-WVLTAAHCFVGAPNELLWTVTLAEGSRgeqaEEVPVNRIlphpKFDPRTfhnDLALVQLWTPVSPGGSARpv 210
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADG----REYPATVV----ARDPDL---DLALLRVSGDGRGLPPLP-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622467294 211 clPQEPQEPPAGTACAIAGwgalFEDGPEAEAVREARVpllstDTCRRALGPGLRPSTMLCAGYLAGgvdscqGDSGGPL 290
Cdd:pfam13365  70 --LGDSEPLVGGERVYAVG----YPLGGEKLSLSEGIV-----SGVDEGRDGGDDGRVIQTDAALSP------GSSGGPV 132
 
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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