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Conserved domains on  [gi|9966885|ref|NP_065137|]
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endosialin precursor [Homo sapiens]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 10856337)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

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, ...
 29-160 1.71e-57

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: 192.26  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   29 CGPSSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGP-----ASRLLWIGLQRQARQCQL-QRPLRG 102
Cdd:cd03600   1 CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPgrhgrGSLRLWIGLQREPRQCSDpSLPLRG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9966885  103 FTWTTGDQDTAFTNWAQPaSGGPCPAQRCVALEASG----EHRWLEGSCTLAVDGYLCQFGF 160
Cdd:cd03600  81 FSWVTGDQDTDFSNWLQE-PAGTCTSPRCVALSAAGstpdNLKWKDGPCSARADGYLCKFSF 141
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 235-271 6.26e-10

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: 54.56  E-value: 6.26e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 9966885    235 CSPDNGGCEHECVEEVDGHVsCRCTEGFRLAADGRSC 271
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYELQDDGRTC 36
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 400-674 1.33e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    400 PTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPAlsRD 479
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP--RR 2782

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    480 HQIPVIAANYPDLPSAYQPgilsvSHSAQPPAHQPPMISTKYPELFPAHQSPmfPDTRVAGTQttthlPGIPPNHAPLVT 559
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSP-----WDPADPPAAVLAPAAALPPAASPAGPLP--PPTSAQPTA-----PPPPPGPPPPSL 2850

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    560 TLGAQLPPQAPdaLVLRTQATQLPIIPTAQPsltttsRSPVSPAHQISVPAATQPAALPTLLPSQSPTnqtsPISPTHPH 639
Cdd:PHA03247 2851 PLGGSVAPGGD--VRRRPPSRSPAAKPAAPA------RPPVRRLARPAVSRSTESFALPPDQPERPPQ----PQAPPPPQ 2918

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 9966885    640 SKA--PQIPREDGPSPKLALWLPSPAPTAAPTALGEA 674
Cdd:PHA03247 2919 PQPqpPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
EGF_CA smart00179
Calcium-binding EGF-like domain;
312-350 2.93e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 2.93e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 9966885     312 DTDECQIAGVCQQ--MCVNYVGGFECYCSEGHEleaDGISC 350
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
 
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, ...
 29-160 1.71e-57

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: 192.26  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   29 CGPSSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGP-----ASRLLWIGLQRQARQCQL-QRPLRG 102
Cdd:cd03600   1 CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPgrhgrGSLRLWIGLQREPRQCSDpSLPLRG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9966885  103 FTWTTGDQDTAFTNWAQPaSGGPCPAQRCVALEASG----EHRWLEGSCTLAVDGYLCQFGF 160
Cdd:cd03600  81 FSWVTGDQDTDFSNWLQE-PAGTCTSPRCVALSAAGstpdNLKWKDGPCSARADGYLCKFSF 141
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 33-157 1.70e-19

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: 84.96  E-value: 1.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885      33 SCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQlqrplrgFTWTTGDQDT 112
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGS-------WQWSDGSGPV 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 9966885     113 AFTNWA--QPASGGpcpaQRCVALEASGeHRWLEGSCTLAVdGYLCQ 157
Cdd:smart00034  84 SYSNWApgEPNNSS----GDCVVLSTSG-GKWNDVSCTSKL-PFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 41-158 4.62e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 60.18  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885     41 RRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASrlLWIGLQRQARQcqlqrplRGFTWTTGDQDTaFTNWAQP 120
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY--FWIGLTDRKNE-------GTWKWVDGSPVN-YTNWAPE 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 9966885    121 ASGGPcPAQRCVALEASGeHRWLEGSCTLaVDGYLCQF 158
Cdd:pfam00059  71 PNNNG-ENEDCVELSSSS-GKWNDENCNS-KNPFVCEK 105
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 235-271 6.26e-10

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: 54.56  E-value: 6.26e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 9966885    235 CSPDNGGCEHECVEEVDGHVsCRCTEGFRLAADGRSC 271
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYELQDDGRTC 36
PHA03247 PHA03247
large tegument protein UL36; Provisional
 400-674 1.33e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    400 PTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPAlsRD 479
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP--RR 2782

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    480 HQIPVIAANYPDLPSAYQPgilsvSHSAQPPAHQPPMISTKYPELFPAHQSPmfPDTRVAGTQttthlPGIPPNHAPLVT 559
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSP-----WDPADPPAAVLAPAAALPPAASPAGPLP--PPTSAQPTA-----PPPPPGPPPPSL 2850

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    560 TLGAQLPPQAPdaLVLRTQATQLPIIPTAQPsltttsRSPVSPAHQISVPAATQPAALPTLLPSQSPTnqtsPISPTHPH 639
Cdd:PHA03247 2851 PLGGSVAPGGD--VRRRPPSRSPAAKPAAPA------RPPVRRLARPAVSRSTESFALPPDQPERPPQ----PQAPPPPQ 2918

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 9966885    640 SKA--PQIPREDGPSPKLALWLPSPAPTAAPTALGEA 674
Cdd:PHA03247 2919 PQPqpPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
EGF_CA smart00179
Calcium-binding EGF-like domain;
312-350 2.93e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 2.93e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 9966885     312 DTDECQIAGVCQQ--MCVNYVGGFECYCSEGHEleaDGISC 350
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 322-350 2.77e-05

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: 41.46  E-value: 2.77e-05
                          10        20
                  ....*....|....*....|....*....
gi 9966885    322 CQQMCVNYVGGFECYCSEGHELEADGISC 350
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 312-343 3.56e-05

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: 41.47  E-value: 3.56e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 9966885  312 DTDECQIAGVCQ--QMCVNYVGGFECYCSEGHEL 343
Cdd:cd00054   1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTG 34
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 398-666 1.16e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    398 MEPTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPV--------------VVSATHPTLPSA 463
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNqtqstaaphtliqqTPTLHPQRLPSP 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    464 HqPPVIPATHPA-----LSRDHQIPVIAANYPDLPSAYQPG----------------------------ILSVSHSAQPP 510
Cdd:pfam03154 246 H-PPLQPMTQPPppsqvSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvppqpfpltpqssqsqvppgpSPAAPGQSQQR 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    511 AHQPPMISTKYPELFPAHQ--------------SPMFPDTRVAGTQTTTHLPGI--------------PPNHAPLvTTLG 562
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPREQplppaplsmphikpPPTTPIPQLPNPQSHKHPPHLsgpspfqmnsnlppPPALKPL-SSLS 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    563 AQLPPQA-PDALVLRTQATQLPiIPTAQPSLTTTSRSPVSPAHQISVPAATQPAalptllPSQSPTNQTSPISPTHPHSK 641
Cdd:pfam03154 404 THHPPSAhPPPLQLMPQSQQLP-PPPAQPPVLTQSQSLPPPAASHPPTSGLHQV------PSQSPFPQHPFVPGGPPPIT 476

                         330       340
                  ....*....|....*....|....*
gi 9966885    642 APQIPREDGPSPKLALWLPSPAPTA 666
Cdd:pfam03154 477 PPSGPPTSTSSAMPGIQPPSSASVS 501
 
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, ...
 29-160 1.71e-57

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: 192.26  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   29 CGPSSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGP-----ASRLLWIGLQRQARQCQL-QRPLRG 102
Cdd:cd03600   1 CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPgrhgrGSLRLWIGLQREPRQCSDpSLPLRG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9966885  103 FTWTTGDQDTAFTNWAQPaSGGPCPAQRCVALEASG----EHRWLEGSCTLAVDGYLCQFGF 160
Cdd:cd03600  81 FSWVTGDQDTDFSNWLQE-PAGTCTSPRCVALSAAGstpdNLKWKDGPCSARADGYLCKFSF 141
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 33-158 4.17e-23

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: 94.99  E-value: 4.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   33 SCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASRlLWIGLQRQARQCQlqrplrgFTWTTGDQDT 112
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD-VWIGLNDLSSEGT-------WKWSDGSPLV 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 9966885  113 AFTNWAqPASGGPCPAQRCVALEASGEHRWLEGSCTlAVDGYLCQF 158
Cdd:cd00037  73 DYTNWA-PGEPNPGGSEDCVVLSSSSDGKWNDVSCS-SKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 33-157 1.70e-19

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: 84.96  E-value: 1.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885      33 SCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQlqrplrgFTWTTGDQDT 112
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGS-------WQWSDGSGPV 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 9966885     113 AFTNWA--QPASGGpcpaQRCVALEASGeHRWLEGSCTLAVdGYLCQ 157
Cdd:smart00034  84 SYSNWApgEPNNSS----GDCVVLSTSG-GKWNDVSCTSKL-PFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 41-158 4.62e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 60.18  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885     41 RRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASrlLWIGLQRQARQcqlqrplRGFTWTTGDQDTaFTNWAQP 120
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY--FWIGLTDRKNE-------GTWKWVDGSPVN-YTNWAPE 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 9966885    121 ASGGPcPAQRCVALEASGeHRWLEGSCTLaVDGYLCQF 158
Cdd:pfam00059  71 PNNNG-ENEDCVELSSSS-GKWNDENCNS-KNPFVCEK 105
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 235-271 6.26e-10

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: 54.56  E-value: 6.26e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 9966885    235 CSPDNGGCEHECVEEVDGHVsCRCTEGFRLAADGRSC 271
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYELQDDGRTC 36
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 35-148 1.21e-09

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. 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. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 56.23  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   35 YALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGpaSRLLWIGLQRQArqcqlqrplRGFTWTTGDqDTAF 114
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVS--NSAAWIGLYRDV---------DSWRWSDGS-ESSF 70

                        90       100       110
                ....*....|....*....|....*....|....
gi 9966885  115 TNWAQPASGGpcpAQRCVALEASGehRWLEGSCT 148
Cdd:cd03602  71 RNWNTFQPFG---QGDCATMYSSG--RWYAALCS 99
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 33-158 1.31e-09

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 56.31  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   33 SCYALFPRRRTFLEAWRACREL-GGDLATPRTPEEAQRVDSLVGAGPASRlLWIGLQRQAR-QCqlqrplRGFTWTTGDQ 110
Cdd:cd03598   2 RCYRFVKSPRTFRDAQVICRRCyRGNLASIHSFAFNYRVQRLVSTLNQAQ-VWIGGIITGKgRC------RRFSWVDGSV 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 9966885  111 dTAFTNWAQpasGGPCPAQR-CVALEASGEHrWLEGSCTLAVdGYLCQF 158
Cdd:cd03598  75 -WNYAYWAP---GQPGNRRGhCVELCTRGGH-WRRAHCKLRR-PFICSY 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
 400-674 1.33e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    400 PTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPAlsRD 479
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP--RR 2782

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    480 HQIPVIAANYPDLPSAYQPgilsvSHSAQPPAHQPPMISTKYPELFPAHQSPmfPDTRVAGTQttthlPGIPPNHAPLVT 559
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSP-----WDPADPPAAVLAPAAALPPAASPAGPLP--PPTSAQPTA-----PPPPPGPPPPSL 2850

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    560 TLGAQLPPQAPdaLVLRTQATQLPIIPTAQPsltttsRSPVSPAHQISVPAATQPAALPTLLPSQSPTnqtsPISPTHPH 639
Cdd:PHA03247 2851 PLGGSVAPGGD--VRRRPPSRSPAAKPAAPA------RPPVRRLARPAVSRSTESFALPPDQPERPPQ----PQAPPPPQ 2918

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 9966885    640 SKA--PQIPREDGPSPKLALWLPSPAPTAAPTALGEA 674
Cdd:PHA03247 2919 PQPqpPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 31-158 2.61e-09

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 55.84  E-value: 2.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   31 PSSCYALFPRRRTFLEAWRACREL--GGDLATPRTPEEAQRVDSLVGA-GPASRLLWIGLQRQARQcqlqrplRGFTWTT 107
Cdd:cd03594   9 KGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSyQKAYQPVWIGLHDPQQS-------RGWEWSD 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 9966885  108 GDQdTAFTNW--AQPASGGpcpaQRCVALEA-SGEHRWLEGSCTlAVDGYLCQF 158
Cdd:cd03594  82 GSK-LDYRSWdrNPPYARG----GYCAELSRsTGFLKWNDANCE-ERNPFICKY 129
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 35-158 4.06e-09

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 54.99  E-value: 4.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   35 YALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGpaSRLLWIGLQRQARQCQlqrplrgFTWTTGDQDTaF 114
Cdd:cd03591   4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKG--NTYAFIGITDLETEGQ-------FVYLDGGPLT-Y 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 9966885  115 TNW--AQPASGGpcPAQRCVALEASGEhrWLEGSCT---LAVdgylCQF 158
Cdd:cd03591  74 TNWkpGEPNNAG--GGEDCVEMYTSGK--WNDVACNltrLFV----CEF 114
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 34-158 4.07e-09

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 55.47  E-value: 4.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   34 CYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRV-DSLVGAGPASRLLWIGLQRQARQCQlqrplrgFTWTTGdQDT 112
Cdd:cd03596  11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALrDYVKASVPGNWEVWLGINDMVAEGK-------WVDVNG-SPI 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 9966885  113 AFTNW-----AQPASGgpcPAQRCVALEASGEHRWLEGSCTLAVDgYLCQF 158
Cdd:cd03596  83 SYFNWereitAQPDGG---KRENCVALSSSAQGKWFDEDCRREKP-YVCEF 129
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 35-125 1.16e-07

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 50.89  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   35 YALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASrllWIGLQRQARQcqlqrplRGFTWTTGDQDTaF 114
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS---WIGASDAATE-------GTWKWSDGEEST-Y 71

                        90
                ....*....|...
gi 9966885  115 TNWA--QPASGGP 125
Cdd:cd03603  72 TNWGsgEPHNNGG 84
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 33-134 1.77e-07

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 51.04  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   33 SCYAL-----FPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLV-GAGPASRLLWIGLQR-QARQCQLQRPLRGFTW 105
Cdd:cd03595  11 PCYKIayfqdSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIqTLRASDGDFWIGLRRsSQYNVTSSACSSLYYW 90

                        90       100       110
                ....*....|....*....|....*....|.
gi 9966885  106 TTGDQDTaFTNW--AQPAsggpCPAQRCVAL 134
Cdd:cd03595  91 LDGSIST-FRNWyvDEPS----CGSEVCVVM 116
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 32-122 4.01e-07

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 49.50  E-value: 4.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   32 SSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLvgagpASRLLWIGLQrqarqcqlQRPLRG-FTWTTGdQ 110
Cdd:cd03588  10 GHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN-----AQDYQWIGLN--------DRTIEGdFRWSDG-H 75

                        90
                ....*....|....
gi 9966885  111 DTAFTNWA--QPAS 122
Cdd:cd03588  76 PLQFENWRpnQPDN 89
EGF_CA smart00179
Calcium-binding EGF-like domain;
312-350 2.93e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 2.93e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 9966885     312 DTDECQIAGVCQQ--MCVNYVGGFECYCSEGHEleaDGISC 350
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
PHA03247 PHA03247
large tegument protein UL36; Provisional
 400-668 4.09e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    400 PTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSAThPTLPSAHQPPViPATHPAlsrd 479
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLS-ESRESLPSPWD-PADPPA---- 2809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    480 hqiPVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAGTQTTTHLPGIPPNhaPLVT 559
Cdd:PHA03247 2810 ---AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR--PPVR 2884

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    560 TLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRSPV--SPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTH 637
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPppQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964

                         250       260       270
                  ....*....|....*....|....*....|...
gi 9966885    638 PHSKAPQ--IPREDGPSPKLAlwLPSPAPTAAP 668
Cdd:PHA03247 2965 GALVPGRvaVPRFRVPQPAPS--REAPASSTPP 2995
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 32-156 1.14e-05

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 45.81  E-value: 1.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   32 SSCYALFPRRRTFLEAWRACRELG-----GDLATPRTPEEAQRV----DSLVGAGPASRlLWIGLQRQARQCQlqrplrg 102
Cdd:cd03589  10 GYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVydlfESSRGPDTPYG-LWIGLHDRTSEGP------- 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966885  103 FTWTTGdQDTAFTNWA--QPASGGpcPAQRCVAL--EASGEHRWLEGSCTLAVDgYLC 156
Cdd:cd03589  82 FEWTDG-SPVDFTKWAggQPDNYG--GNEDCVQMwrRGDAGQSWNDMPCDAVFP-YIC 135
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 322-350 2.77e-05

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: 41.46  E-value: 2.77e-05
                          10        20
                  ....*....|....*....|....*....
gi 9966885    322 CQQMCVNYVGGFECYCSEGHELEADGISC 350
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 312-343 3.56e-05

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: 41.47  E-value: 3.56e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 9966885  312 DTDECQIAGVCQ--QMCVNYVGGFECYCSEGHEL 343
Cdd:cd00054   1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTG 34
PHA03247 PHA03247
large tegument protein UL36; Provisional
 400-672 4.41e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    400 PTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIP-ATHPALSR 478
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrVSRPRRAR 2668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    479 DHQIPVIAANYPDLPS--AYQPGILSVSHSAQPPAHQPPmistkyPELFPAHQSPMFPDTRVAGTQTTThLPGIPPNHAP 556
Cdd:PHA03247 2669 RLGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPT------PEPAPHALVSATPLPPGPAAARQA-SPALPAAPAP 2741

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    557 LVTTLGAQLPpqAPDALVLRTQATQLPIIPT--AQPSLTTTSRSPVSPAhqisVPAATQPAALPTLLPSQSPTNQTSPIS 634
Cdd:PHA03247 2742 PAVPAGPATP--GGPARPARPPTTAGPPAPAppAAPAAGPPRRLTRPAV----ASLSESRESLPSPWDPADPPAAVLAPA 2815

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 9966885    635 PTHPHSKAPQIPREDGPSPKLALWLPSPAPTAAPTALG 672
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
EGF_CA pfam07645
Calcium-binding EGF domain;
312-340 8.78e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.91  E-value: 8.78e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 9966885    312 DTDECQIAG-VCQQM--CVNYVGGFECYCSEG 340
Cdd:pfam07645   1 DVDECATGThNCPANtvCVNTIGSFECRCPDG 32
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 398-666 1.16e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    398 MEPTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPV--------------VVSATHPTLPSA 463
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNqtqstaaphtliqqTPTLHPQRLPSP 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    464 HqPPVIPATHPA-----LSRDHQIPVIAANYPDLPSAYQPG----------------------------ILSVSHSAQPP 510
Cdd:pfam03154 246 H-PPLQPMTQPPppsqvSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvppqpfpltpqssqsqvppgpSPAAPGQSQQR 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    511 AHQPPMISTKYPELFPAHQ--------------SPMFPDTRVAGTQTTTHLPGI--------------PPNHAPLvTTLG 562
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPREQplppaplsmphikpPPTTPIPQLPNPQSHKHPPHLsgpspfqmnsnlppPPALKPL-SSLS 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    563 AQLPPQA-PDALVLRTQATQLPiIPTAQPSLTTTSRSPVSPAHQISVPAATQPAalptllPSQSPTNQTSPISPTHPHSK 641
Cdd:pfam03154 404 THHPPSAhPPPLQLMPQSQQLP-PPPAQPPVLTQSQSLPPPAASHPPTSGLHQV------PSQSPFPQHPFVPGGPPPIT 476

                         330       340
                  ....*....|....*....|....*
gi 9966885    642 APQIPREDGPSPKLALWLPSPAPTA 666
Cdd:pfam03154 477 PPSGPPTSTSSAMPGIQPPSSASVS 501
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 390-669 1.61e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    390 TEMPGILWMEPTQPPDFALAYRPSFPEDRE--------PQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLP 461
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQSQLQSQQPPREQPlppaplsmPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPP 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    462 SAHQPPVIPATHPalsrdhqipviaanypdlPSAYQP--GILSVSHSAQPPAHQPPMIstkypelfpahqspmfpdtrva 539
Cdd:pfam03154 395 ALKPLSSLSTHHP------------------PSAHPPplQLMPQSQQLPPPPAQPPVL---------------------- 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    540 gTQTTTHlPGIPPNHAPlvTTLGAQLPPQAPDAlvlrtqatQLPIIPTAQPSLTTTSRSPVSPAHqiSVPAATQPAALPT 619
Cdd:pfam03154 435 -TQSQSL-PPPAASHPP--TSGLHQVPSQSPFP--------QHPFVPGGPPPITPPSGPPTSTSS--AMPGIQPPSSASV 500

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 9966885    620 LLPSQSPTNQTSPISPTHPHSKAPQIPrEDGPSPKLALWLPSPAPTAAPT 669
Cdd:pfam03154 501 SSSGPVPAAVSCPLPPVQIKEEALDEA-EEPESPPPPPRSPSPEPTVVNT 549
PHA03247 PHA03247
large tegument protein UL36; Provisional
 435-669 2.52e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    435 APRVPYHSSVLSVTRPVV-------------------VSATHPTLPSAHQP-PVIPATHPALSRDHQIPVIAANYPDLP- 493
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAppqsarprapvddrgdprgPAPPSPLPPDTHAPdPPPPSPSPAANEPDPHPPPTVPPPERPr 2653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    494 SAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAgtqtTTHLPGIPPNHAPLVTTLGAQLPPQAPDAL 573
Cdd:PHA03247 2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLA----DPPPPPPTPEPAPHALVSATPLPPGPAAAR 2729

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    574 VLRTQATQLPIIPT--AQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPRE-DG 650
Cdd:PHA03247 2730 QASPALPAAPAPPAvpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADpPA 2809

                         250       260
                  ....*....|....*....|..
gi 9966885    651 PSPKLALWLP---SPAPTAAPT 669
Cdd:PHA03247 2810 AVLAPAAALPpaaSPAGPLPPP 2831
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 516-665 5.64e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    516 MISTKYPElfPAHQSPMFPDTRVAGTQTTTHLPGipPNHAPLVTTLGAQLPPQAPDALVLR-----TQATQLPIIPTAQP 590
Cdd:pfam05109 419 VIFSKAPE--STTTSPTLNTTGFAAPNTTTGLPS--STHVPTNLTAPASTGPTVSTADVTSptpagTTSGASPVTPSPSP 494

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9966885    591 SLT-TTSRSP--VSPAHQISVPaaTQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLALWLPSPAPT 665
Cdd:pfam05109 495 RDNgTESKAPdmTSPTSAVTTP--TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNAT 570
PHA03247 PHA03247
large tegument protein UL36; Provisional
 400-678 8.76e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    400 PTQPPDFALAYRPSFPedrePQipypeptwpppLSAPRVPYHSSvlsvTRPVVVSATHPTLPSAHQP-PVIPATHPALSR 478
Cdd:PHA03247 2577 PSEPAVTSRARRPDAP----PQ-----------SARPRAPVDDR----GDPRGPAPPSPLPPDTHAPdPPPPSPSPAANE 2637

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    479 DHQIPVIAANYPDLP-SAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAgtqtTTHLPGIPPNHAPL 557
Cdd:PHA03247 2638 PDPHPPPTVPPPERPrDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLA----DPPPPPPTPEPAPH 2713

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    558 VTTLGAQLPPQAPDALVLRTQATQLPIIPT--AQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISP 635
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAAPAPPAvpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 9966885    636 THPHSKAPqipredgpspklalwlpsPAPTAAPTALGEAGLAE 678
Cdd:PHA03247 2794 SRESLPSP------------------WDPADPPAAVLAPAAAL 2818
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
453-644 9.05e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 42.67  E-value: 9.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   453 VSATHPTLPSAHQPPVIPATHPALSRDHQIPVIAANYPDLPSAYQPGILSVS--HSAQPPAHQP---PMISTKYPElfPA 527
Cdd:PRK12727  62 TPATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMAlrQPVSVPRQAPaaaPVRAASIPS--PA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   528 HQSPMFPDTRVAGTQTTTHLPGIPPN-HAPLVTTLGAQLPPQAPDALVLRTQAtqlPIIPTAQPSLTTTSR------SPV 600
Cdd:PRK12727 140 AQALAHAAAVRTAPRQEHALSAVPEQlFADFLTTAPVPRAPVQAPVVAAPAPV---PAIAAALAAHAAYAQdddeqlDDD 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 9966885   601 SPAHQISVPAATQPAALPTLL--PSQSPTNqtSPISPTHPhskAPQ 644
Cdd:PRK12727 217 GFDLDDALPQILPPAALPPIVvaPAAPAAL--AAVAAAAP---APQ 257
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 575-674 2.56e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.07  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   575 LRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISP-------THPHSKAPQIPR 647
Cdd:PLN03209 380 LKPPTSPIPTPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPyaryedlKPPTSPSPTAPT 459

                         90       100
                 ....*....|....*....|....*..
gi 9966885   648 EDGPSPKLALWLPSPAPTAAPTALGEA 674
Cdd:PLN03209 460 GVSPSVSSTSSVPAVPDTAPATAATDA 486
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 255-273 2.90e-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: 35.46  E-value: 2.90e-03
                          10
                  ....*....|....*....
gi 9966885    255 SCRCTEGFRLAADGRSCED 273
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVD 19
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 548-679 3.43e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   548 PGIPPNHAPLVTTLGAQLPPQAPdalVLRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPT 627
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAP---VAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL 447

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 9966885   628 NQTSPISPThPHSKAPQIPREDGPSPKLALWLPSPAPTAAPTALGEAGLAEH 679
Cdd:PRK14951 448 APAPPAQAA-PETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDVWH 498
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 446-672 3.45e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    446 SVTRPVVVSATHPTLPSAHQPPVIPATH----PALSRDHQIPVIAANYPDLPSAYQPGIL-------SVSHSAQPPAHQP 514
Cdd:PRK10263  315 PITEPVAVAAAATTATQSWAAPVEPVTQtppvASVDVPPAQPTVAWQPVPGPQTGEPVIApapegypQQSQYAQPAVQYN 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    515 PMISTKYPELFPAHQSPMFPDTRVAGTQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDA-LVLRTQATQLPIIPTAQPSLT 593
Cdd:PRK10263  395 EPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQqSTFAPQSTYQTEQTYQQPAAQ 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    594 TTSRSPVSPAHQIS------VPAATQPAALPTLL--------------------PSQSPTNQTSPISPTHPHSKAPQIPR 647
Cdd:PRK10263  475 EPLYQQPQPVEQQPvvepepVVEETKPARPPLYYfeeveekrarereqlaawyqPIPEPVKEPEPIKSSLKAPSVAAVPP 554

                         250       260
                  ....*....|....*....|....*
gi 9966885    648 EDgpspklalwlpsPAPTAAPTALG 672
Cdd:PRK10263  555 VE------------AAAAVSPLASG 567
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 389-647 8.27e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.68  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    389 WTEMPGILWMEPTQPPDfALAYRPSfPEDREPQIPYPEPTWPPPlsAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPV 468
Cdd:PRK10263  360 WQPVPGPQTGEPVIAPA-PEGYPQQ-SQYAQPAVQYNEPLQQPV--QPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYA 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    469 IPATHPALSRDHQIPVIAANYPDLPSaYQPGILSVSHSAQPPAHQPPMISTKYPELFPahqSPMFPDTRvagtqttthlP 548
Cdd:PRK10263  436 PAPEQPVAGNAWQAEEQQSTFAPQST-YQTEQTYQQPAAQEPLYQQPQPVEQQPVVEP---EPVVEETK----------P 501

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885    549 GIPP---------NHAPLVTTLGA--QLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATqpAAL 617
Cdd:PRK10263  502 ARPPlyyfeeveeKRAREREQLAAwyQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATG--AAA 579

                         250       260       270
                  ....*....|....*....|....*....|
gi 9966885    618 PTLLPSQSPTNQTSPiSPTHPHSKAPQIPR 647
Cdd:PRK10263  580 TVAAPVFSLANSGGP-RPQVKEGIGPQLPR 608
PHA03378 PHA03378
EBNA-3B; Provisional
 402-668 8.50e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   402 QPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRdhq 481
Cdd:PHA03378 639 QPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQ--- 715

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   482 iPVIAANYPDLPSAYQPGILSVSHSAQPPAhQPPMISTKYPELFPAHQSPMFPDTRVAGTQTTTHLPGIPPnhAPLVTTL 561
Cdd:PHA03378 716 -RPAAATGRARPPAAAPGRARPPAAAPGRA-RPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPP--APQQRPR 791

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966885   562 GA---QLPPQAPDA---LVLRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISP 635
Cdd:PHA03378 792 GAptpQPPPQAGPTsmqLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIVQAPV 871

                        250       260       270
                 ....*....|....*....|....*....|....
gi 9966885   636 THPHSKAP-QIPREDGPSPKLALWLPSPAPTAAP 668
Cdd:PHA03378 872 FYPPVLQPiQVMRQLGSVRAAAASTVTQAPTEYT 905
 
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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