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Conserved domains on  [gi|4507483|ref|NP_000352|]
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thrombomodulin precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 30-171 4.73e-51

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


:

Pssm-ID: 153070  Cd Length: 141  Bit Score: 171.85  E-value: 4.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483   30 CVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGD---GGVGRRRLWIGLQLPPG-CGDPKRlgPL 105
Cdd:cd03600   1 CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGpgrHGRGSLRLWIGLQREPRqCSDPSL--PL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507483  106 RGFQWVTGDNNTSYSRWARLdlnGAPLCG-PLCVAVSAAEATvPSEPIWEEQQCEVKADGFLCEFHF 171
Cdd:cd03600  79 RGFSWVTGDQDTDFSNWLQE---PAGTCTsPRCVALSAAGST-PDNLKWKDGPCSARADGYLCKFSF 141
Tme5_EGF_like pfam09064
Thrombomodulin like fifth domain, EGF-like; Members of this family adopt a fold similar to ...
 406-439 1.86e-10

Thrombomodulin like fifth domain, EGF-like; Members of this family adopt a fold similar to other EGF domains, with a flat major and a twisted minor beta sheet. Disulphide pairing, however, is not of the usual 1-3, 2-4, 5-6 type; rather 1-2, 3-4, 5-6 pairing is found. Its extended major sheet (strands beta-2 and beta-3 and the connecting loop) projects into thrombin's active site groove. This domain is required for interaction of thrombomodulin with thrombin, and subsequent activation of protein-C.


:

Pssm-ID: 312559  Cd Length: 34  Bit Score: 56.05  E-value: 1.86e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4507483    406 MFCNQTACPADCDPNTQASCECPEGYILDDGFIC 439
Cdd:pfam09064   1 LHCAEKKCPAVCDPNSGGSCYCPEGFILDDNFVC 34
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 245-280 1.61e-06

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: 44.93  E-value: 1.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 4507483    245 CSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSC 280
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 289-323 1.71e-04

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: 39.15  E-value: 1.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 4507483    289 NDLCEHFCVPnpdQPGSYSCMCETGYRLAADQHRC 323
Cdd:pfam14670   5 NGGCSHLCLN---TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
441-468 2.53e-04

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 2.53e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 4507483     441 DIDECENGGFCS--GVCHNLPGTFECICGP 468
Cdd:smart00179   1 DIDECASGNPCQngGTCVNTVGSYRCECPP 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
325-355 1.46e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 4507483     325 DVDDCiLEPSPCPQ--RCVNTQGGFECHCYPNY 355
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGY 32
 
Name Accession Description Interval E-value
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 30-171 4.73e-51

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 171.85  E-value: 4.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483   30 CVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGD---GGVGRRRLWIGLQLPPG-CGDPKRlgPL 105
Cdd:cd03600   1 CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGpgrHGRGSLRLWIGLQREPRqCSDPSL--PL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507483  106 RGFQWVTGDNNTSYSRWARLdlnGAPLCG-PLCVAVSAAEATvPSEPIWEEQQCEVKADGFLCEFHF 171
Cdd:cd03600  79 RGFSWVTGDQDTDFSNWLQE---PAGTCTsPRCVALSAAGST-PDNLKWKDGPCSARADGYLCKFSF 141
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 25-168 1.62e-10

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 58.77  E-value: 1.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483      25 PGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNgdGGVGRRRLWIGLQlppgcgdpkRLGP 104
Cdd:smart00034   2 PSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLK--NSGSSDYYWIGLS---------DPDS 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507483     105 LRGFQWVTGDNNTSYSRWARLDLNGAplcGPLCVAVSAAEATvpsepiWEEQQCEVKAdGFLCE 168
Cdd:smart00034  71 NGSWQWSDGSGPVSYSNWAPGEPNNS---SGDCVVLSTSGGK------WNDVSCTSKL-PFVCE 124
Tme5_EGF_like pfam09064
Thrombomodulin like fifth domain, EGF-like; Members of this family adopt a fold similar to ...
 406-439 1.86e-10

Thrombomodulin like fifth domain, EGF-like; Members of this family adopt a fold similar to other EGF domains, with a flat major and a twisted minor beta sheet. Disulphide pairing, however, is not of the usual 1-3, 2-4, 5-6 type; rather 1-2, 3-4, 5-6 pairing is found. Its extended major sheet (strands beta-2 and beta-3 and the connecting loop) projects into thrombin's active site groove. This domain is required for interaction of thrombomodulin with thrombin, and subsequent activation of protein-C.


Pssm-ID: 312559  Cd Length: 34  Bit Score: 56.05  E-value: 1.86e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4507483    406 MFCNQTACPADCDPNTQASCECPEGYILDDGFIC 439
Cdd:pfam09064   1 LHCAEKKCPAVCDPNSGGSCYCPEGFILDDNFVC 34
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 245-280 1.61e-06

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: 44.93  E-value: 1.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 4507483    245 CSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSC 280
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 42-169 7.74e-06

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 44.78  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483     42 PATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGgvgrRRLWIGLqlppgcGDPKRLGplrGFQWVTGDNNTsYSR 121
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN----KYFWIGL------TDRKNEG---TWKWVDGSPVN-YTN 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4507483    122 WARLDLNGAPlcGPLCVAVSAAEATvpsepiWEEQQCEVKAdGFLCEF 169
Cdd:pfam00059  67 WAPEPNNNGE--NEDCVELSSSSGK------WNDENCNSKN-PFVCEK 105
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 289-323 1.71e-04

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: 39.15  E-value: 1.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 4507483    289 NDLCEHFCVPnpdQPGSYSCMCETGYRLAADQHRC 323
Cdd:pfam14670   5 NGGCSHLCLN---TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
441-468 2.53e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 2.53e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 4507483     441 DIDECENGGFCS--GVCHNLPGTFECICGP 468
Cdd:smart00179   1 DIDECASGNPCQngGTCVNTVGSYRCECPP 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 441-468 1.20e-03

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: 36.85  E-value: 1.20e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 4507483  441 DIDECENGGFCS--GVCHNLPGTFECICGP 468
Cdd:cd00054   1 DIDECASGNPCQngGTCVNTVGSYRCSCPP 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
325-355 1.46e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 4507483     325 DVDDCiLEPSPCPQ--RCVNTQGGFECHCYPNY 355
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
325-351 4.27e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.91  E-value: 4.27e-03
                          10        20
                  ....*....|....*....|....*....
gi 4507483    325 DVDDCILEPSPCPQR--CVNTQGGFECHC 351
Cdd:pfam07645   1 DVDECATGTHNCPANtvCVNTIGSFECRC 29
EGF_CA pfam07645
Calcium-binding EGF domain;
441-466 9.49e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.14  E-value: 9.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 4507483    441 DIDECENGGF-C--SGVCHNLPGTFECIC 466
Cdd:pfam07645   1 DVDECATGTHnCpaNTVCVNTIGSFECRC 29
 
Name Accession Description Interval E-value
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 30-171 4.73e-51

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 171.85  E-value: 4.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483   30 CVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGD---GGVGRRRLWIGLQLPPG-CGDPKRlgPL 105
Cdd:cd03600   1 CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGpgrHGRGSLRLWIGLQREPRqCSDPSL--PL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507483  106 RGFQWVTGDNNTSYSRWARLdlnGAPLCG-PLCVAVSAAEATvPSEPIWEEQQCEVKADGFLCEFHF 171
Cdd:cd03600  79 RGFSWVTGDQDTDFSNWLQE---PAGTCTsPRCVALSAAGST-PDNLKWKDGPCSARADGYLCKFSF 141
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 35-169 8.35e-12

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 62.25  E-value: 8.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483   35 CFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGGvgrRRLWIGLQlppgcgdpkRLGPLRGFQWVTGD 114
Cdd:cd00037   2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSS---SDVWIGLN---------DLSSEGTWKWSDGS 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4507483  115 NNTSYSRWARLDLNGAPlcGPLCVAVSAAEATVpsepiWEEQQCEVKAdGFLCEF 169
Cdd:cd00037  70 PLVDYTNWAPGEPNPGG--SEDCVVLSSSSDGK-----WNDVSCSSKL-PFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 25-168 1.62e-10

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 58.77  E-value: 1.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483      25 PGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNgdGGVGRRRLWIGLQlppgcgdpkRLGP 104
Cdd:smart00034   2 PSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLK--NSGSSDYYWIGLS---------DPDS 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507483     105 LRGFQWVTGDNNTSYSRWARLDLNGAplcGPLCVAVSAAEATvpsepiWEEQQCEVKAdGFLCE 168
Cdd:smart00034  71 NGSWQWSDGSGPVSYSNWAPGEPNNS---SGDCVVLSTSGGK------WNDVSCTSKL-PFVCE 124
Tme5_EGF_like pfam09064
Thrombomodulin like fifth domain, EGF-like; Members of this family adopt a fold similar to ...
 406-439 1.86e-10

Thrombomodulin like fifth domain, EGF-like; Members of this family adopt a fold similar to other EGF domains, with a flat major and a twisted minor beta sheet. Disulphide pairing, however, is not of the usual 1-3, 2-4, 5-6 type; rather 1-2, 3-4, 5-6 pairing is found. Its extended major sheet (strands beta-2 and beta-3 and the connecting loop) projects into thrombin's active site groove. This domain is required for interaction of thrombomodulin with thrombin, and subsequent activation of protein-C.


Pssm-ID: 312559  Cd Length: 34  Bit Score: 56.05  E-value: 1.86e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4507483    406 MFCNQTACPADCDPNTQASCECPEGYILDDGFIC 439
Cdd:pfam09064   1 LHCAEKKCPAVCDPNSGGSCYCPEGFILDDNFVC 34
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 245-280 1.61e-06

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: 44.93  E-value: 1.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 4507483    245 CSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSC 280
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 42-169 7.74e-06

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 44.78  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507483     42 PATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGgvgrRRLWIGLqlppgcGDPKRLGplrGFQWVTGDNNTsYSR 121
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN----KYFWIGL------TDRKNEG---TWKWVDGSPVN-YTN 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4507483    122 WARLDLNGAPlcGPLCVAVSAAEATvpsepiWEEQQCEVKAdGFLCEF 169
Cdd:pfam00059  67 WAPEPNNNGE--NEDCVELSSSSGK------WNDENCNSKN-PFVCEK 105
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 289-323 1.71e-04

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: 39.15  E-value: 1.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 4507483    289 NDLCEHFCVPnpdQPGSYSCMCETGYRLAADQHRC 323
Cdd:pfam14670   5 NGGCSHLCLN---TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
441-468 2.53e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 2.53e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 4507483     441 DIDECENGGFCS--GVCHNLPGTFECICGP 468
Cdd:smart00179   1 DIDECASGNPCQngGTCVNTVGSYRCECPP 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 441-468 1.20e-03

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: 36.85  E-value: 1.20e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 4507483  441 DIDECENGGFCS--GVCHNLPGTFECICGP 468
Cdd:cd00054   1 DIDECASGNPCQngGTCVNTVGSYRCSCPP 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
325-355 1.46e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 4507483     325 DVDDCiLEPSPCPQ--RCVNTQGGFECHCYPNY 355
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
325-351 4.27e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.91  E-value: 4.27e-03
                          10        20
                  ....*....|....*....|....*....
gi 4507483    325 DVDDCILEPSPCPQR--CVNTQGGFECHC 351
Cdd:pfam07645   1 DVDECATGTHNCPANtvCVNTIGSFECRC 29
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 424-444 8.57e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. 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 cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 33.92  E-value: 8.57e-03
                          10        20
                  ....*....|....*....|..
gi 4507483    424 SCECPEGYILD-DGFICTDIDE 444
Cdd:pfam12662   1 TCSCPPGYQLDpDGRTCVDIDE 22
EGF_CA pfam07645
Calcium-binding EGF domain;
441-466 9.49e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.14  E-value: 9.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 4507483    441 DIDECENGGF-C--SGVCHNLPGTFECIC 466
Cdd:pfam07645   1 DVDECATGTHnCpaNTVCVNTIGSFECRC 29
 
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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