NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1770966936|ref|NP_001362537|]
View 

vitamin K-dependent protein C isoform 9 precursor [Homo sapiens]

Protein Classification

GLA and Tryp_SPc domain-containing protein( domain architecture ID 10637833)

protein containing domains GLA, EGF_CA, and Tryp_SPc

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
194-429 3.97e-93

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: 280.70  E-value: 3.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 194 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 271
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 272 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 351
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 352 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 429
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
24-87 3.95e-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: 3.95e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770966936   24 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
101-132 1.97e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 49.94  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1770966936 101 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 132
Cdd:cd00054     5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
194-429 3.97e-93

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: 280.70  E-value: 3.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 194 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 271
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 272 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 351
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 352 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 429
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
192-426 1.74e-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 [Multi-domain]  Cd Length: 229  Bit Score: 266.08  E-value: 1.74e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936  192 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 269
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936  270 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 349
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770966936  350 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 426
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
194-426 1.20e-82

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 253.52  E-value: 1.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 194 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 273
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 274 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 353
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770966936 354 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 426
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
186-438 3.44e-31

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 123.83  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 186 EDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA----CGAVLIHPSWVLTAAHCMDESK--KLLVRLGEYDLRRWEKWEl 259
Cdd:COG5640    26 ADEVSSRIIGGSNANAGEYPSLVALVDRISDYVsgtfCGGSKLGGRYVLTAAHCADASSpiSSDVNRVVVDLNDSSQAE- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 260 DLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivpICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRN--R 337
Cdd:COG5640   105 RGHVRTIYVHEFYSPGNLGNDIAVLELARAASLPR----VKITSFDASDTFLNSVTTVSPMTNGTFGVTTPSDVPRSspK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 338 TFVLNFIKIPVVPHNECSEVMSNMVSENM------LCAGILgdRQDACEGDSGGPMVASFHGTWFLVGLVSWGEG-CGLL 410
Cdd:COG5640   181 GTILHEVAVLFVPLSTCAQYKGCANASDGatgltgFCAGRP--PKDACQGDSGGPIFHKGEEGRVQRGVVSWGDGgCGGT 258
                         250       260
                  ....*....|....*....|....*...
gi 1770966936 411 HNYGVYTKVSRYLDWIHGHIRDKEAPQK 438
Cdd:COG5640   259 LIPGVYTNVSNYQDWIAAMTNGLSYLQF 286
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
24-87 3.95e-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: 3.95e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770966936   24 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
47-87 5.46e-18

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: 425770  Cd Length: 41  Bit Score: 76.79  E-value: 5.46e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1770966936  47 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
101-132 1.97e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 49.94  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1770966936 101 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 132
Cdd:cd00054     5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
101-132 3.43e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 3.43e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1770966936  101 CAS--LCCGHGTCIDGIGSFSCDCRSGWE-GRFCQ 132
Cdd:smart00179   5 CASgnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
101-130 1.62e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.82  E-value: 1.62e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1770966936 101 CASL-CCGHGTCIDGIGSFSCDCRSGWEGRF 130
Cdd:pfam00008   1 CAPNpCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
194-429 3.97e-93

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: 280.70  E-value: 3.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 194 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 271
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 272 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 351
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 352 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 429
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
192-426 1.74e-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 [Multi-domain]  Cd Length: 229  Bit Score: 266.08  E-value: 1.74e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936  192 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 269
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936  270 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 349
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770966936  350 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 426
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
194-426 1.20e-82

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 253.52  E-value: 1.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 194 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 273
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 274 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 353
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770966936 354 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 426
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
186-438 3.44e-31

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 123.83  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 186 EDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA----CGAVLIHPSWVLTAAHCMDESK--KLLVRLGEYDLRRWEKWEl 259
Cdd:COG5640    26 ADEVSSRIIGGSNANAGEYPSLVALVDRISDYVsgtfCGGSKLGGRYVLTAAHCADASSpiSSDVNRVVVDLNDSSQAE- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 260 DLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivpICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRN--R 337
Cdd:COG5640   105 RGHVRTIYVHEFYSPGNLGNDIAVLELARAASLPR----VKITSFDASDTFLNSVTTVSPMTNGTFGVTTPSDVPRSspK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770966936 338 TFVLNFIKIPVVPHNECSEVMSNMVSENM------LCAGILgdRQDACEGDSGGPMVASFHGTWFLVGLVSWGEG-CGLL 410
Cdd:COG5640   181 GTILHEVAVLFVPLSTCAQYKGCANASDGatgltgFCAGRP--PKDACQGDSGGPIFHKGEEGRVQRGVVSWGDGgCGGT 258
                         250       260
                  ....*....|....*....|....*...
gi 1770966936 411 HNYGVYTKVSRYLDWIHGHIRDKEAPQK 438
Cdd:COG5640   259 LIPGVYTNVSNYQDWIAAMTNGLSYLQF 286
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
24-87 3.95e-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: 3.95e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770966936   24 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
47-87 5.46e-18

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: 425770  Cd Length: 41  Bit Score: 76.79  E-value: 5.46e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1770966936  47 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
101-132 1.97e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 49.94  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1770966936 101 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 132
Cdd:cd00054     5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
101-132 3.43e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 3.43e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1770966936  101 CAS--LCCGHGTCIDGIGSFSCDCRSGWE-GRFCQ 132
Cdd:smart00179   5 CASgnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
100-132 7.75e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 39.77  E-value: 7.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770966936 100 PCA--SLCCGHGTCIDGIGSFSCDCRSGWEG-RFCQ 132
Cdd:cd00053     1 ECAasNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
100-132 1.17e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.04  E-value: 1.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1770966936  100 PCASLC-CGHGTCIDGIGSFSCDCRSGWEG-RFCQ 132
Cdd:smart00181   1 ECASGGpCSNGTCINTPGSYTCSCPPGYTGdKRCE 35
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
101-130 1.62e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.82  E-value: 1.62e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1770966936 101 CASL-CCGHGTCIDGIGSFSCDCRSGWEGRF 130
Cdd:pfam00008   1 CAPNpCSNGGTCVDTPGGYTCICPEGYTGKR 31
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
105-126 2.07e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteristic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 432703  Cd Length: 22  Bit Score: 35.39  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|..
gi 1770966936 105 CCGHGTCIDGIGSFSCDCRSGW 126
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
104-131 7.70e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 33.86  E-value: 7.70e-03
                          10        20
                  ....*....|....*....|....*...
gi 1770966936 104 LCCGHGTCIDGIGSfsCDCRSGWEGRFC 131
Cdd:pfam07974   1 ICSGRGTCVNQCGK--CVCDSGYQGATC 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH