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Conserved domains on  [gi|1770966605|ref|NP_001362535|]
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vitamin K-dependent protein C isoform 3 precursor [Homo sapiens]

Protein Classification

GLA and Tryp_SPc domain-containing protein( domain architecture ID 10637923)

protein containing domains GLA, FXa_inhibition, and Tryp_SPc

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 ...
269-504 1.35e-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: 281.86  E-value: 1.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 269 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 346
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 347 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 426
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 427 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 504
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
45-108 7.74e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


:

Pssm-ID: 214503  Cd Length: 65  Bit Score: 100.08  E-value: 7.74e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770966605   45 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
196-231 1.91e-12

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 61.49  E-value: 1.91e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770966605 196 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 231
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
269-504 1.35e-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: 281.86  E-value: 1.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 269 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 346
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 347 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 426
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 427 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 504
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
267-501 8.24e-87

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: 266.85  E-value: 8.24e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605  267 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 344
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605  345 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 424
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770966605  425 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 501
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
269-501 9.30e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 253.52  E-value: 9.30e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 269 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 348
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 349 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 428
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770966605 429 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 501
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
260-506 5.39e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 203.73  E-value: 5.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 260 QEDQVDPRLIDGKMTRRGDSPWQVVLL--DSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 335
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQssNGPSGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 336 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 415
Cdd:COG5640   103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 416 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 495
Cdd:COG5640   170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|.
gi 1770966605 496 RYLDWIHGHIR 506
Cdd:COG5640   249 AYRDWIKSTAG 259
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
45-108 7.74e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 100.08  E-value: 7.74e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770966605   45 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
68-108 6.53e-19

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 79.88  E-value: 6.53e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1770966605  68 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
196-231 1.91e-12

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 61.49  E-value: 1.91e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770966605 196 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 231
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
269-504 1.35e-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: 281.86  E-value: 1.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 269 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 346
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 347 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 426
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 427 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 504
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
267-501 8.24e-87

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: 266.85  E-value: 8.24e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605  267 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 344
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605  345 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 424
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770966605  425 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 501
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
269-501 9.30e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 253.52  E-value: 9.30e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 269 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 348
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 349 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 428
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770966605 429 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 501
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
260-506 5.39e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 203.73  E-value: 5.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 260 QEDQVDPRLIDGKMTRRGDSPWQVVLL--DSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 335
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQssNGPSGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 336 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 415
Cdd:COG5640   103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 416 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 495
Cdd:COG5640   170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|.
gi 1770966605 496 RYLDWIHGHIR 506
Cdd:COG5640   249 AYRDWIKSTAG 259
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
45-108 7.74e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 100.08  E-value: 7.74e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770966605   45 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
68-108 6.53e-19

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 79.88  E-value: 6.53e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1770966605  68 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
294-491 8.55e-15

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 72.79  E-value: 8.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 294 CGAVLIHPSWVLTAAHCMDESK------KLLVRLGeYDLRRWEKWEldldIKEVFVHPNYSKSTTDN-DIALLHLAQPAT 366
Cdd:COG3591    14 CTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPG-YNGGPYGTAT----ATRFRVPPGWVASGDAGyDYALLRLDEPLG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966605 367 LSQTIVPICLPDSGLAERELNQAgqetlvtgwGYHSSREKEAKRNRTfvlnfikipvvphNECSEVMSNMVSenMLCagi 446
Cdd:COG3591    89 DTTGWLGLAFNDAPLAGEPVTII---------GYPGDRPKDLSLDCS-------------GRVTGVQGNRLS--YDC--- 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1770966605 447 lgdrqDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGllHNYGVY 491
Cdd:COG3591   142 -----DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR--ANTGVR 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
196-231 1.91e-12

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 61.49  E-value: 1.91e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770966605 196 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 231
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
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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