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Conserved domains on  [gi|767917132|ref|XP_011509074|]
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von Willebrand factor A domain-containing protein 3B isoform X4 [Homo sapiens]

Protein Classification

vWFA and TUDOR domain-containing protein( domain architecture ID 10076988)

vWFA and TUDOR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-658 1.53e-19

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


:

Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 90.00  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 586
Cdd:COG1240    95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  587 LSALKTA------FADKETQAIYLLTDGRPDQPPETVIDQVKRFQE--IPIYTISFNyNDEIANRFLKEVAALTGGEFHF 658
Cdd:COG1240   169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
DUF4537 super family cl48268
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 1037-1117 1.61e-19

Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.


The actual alignment was detected with superfamily member pfam15057:

Pssm-ID: 464475 [Multi-domain]  Cd Length: 124  Bit Score: 85.44  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  1037 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMPCPL------------------------ 1092
Cdd:pfam15057    1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAMEHPLrvgdkvlalhdpysqsyapgivla 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767917132  1093 -------------------LQEFCPRSALIKISQNKYALSCSHI 1117
Cdd:pfam15057   81 gperrvdadeeltvrfydgKTATVPREEVYKLSQAYYEKAVAYI 124
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-658 1.53e-19

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 90.00  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 586
Cdd:COG1240    95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  587 LSALKTA------FADKETQAIYLLTDGRPDQPPETVIDQVKRFQE--IPIYTISFNyNDEIANRFLKEVAALTGGEFHF 658
Cdd:COG1240   169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
DUF4537 pfam15057
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 1037-1117 1.61e-19

Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.


Pssm-ID: 464475 [Multi-domain]  Cd Length: 124  Bit Score: 85.44  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  1037 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMPCPL------------------------ 1092
Cdd:pfam15057    1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAMEHPLrvgdkvlalhdpysqsyapgivla 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767917132  1093 -------------------LQEFCPRSALIKISQNKYALSCSHI 1117
Cdd:pfam15057   81 gperrvdadeeltvrfydgKTATVPREEVYKLSQAYYEKAVAYI 124
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-659 3.94e-19

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 85.70  E-value: 3.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 584
Cdd:cd00198     2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  585 NTLSALKTAFA-------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGeFH 657
Cdd:cd00198    81 NIGAALRLALEllksakrPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG-GA 159


                  ..
gi 767917132  658 FY 659
Cdd:cd00198   160 VF 161
VWA_3 pfam13768
von Willebrand factor type A domain;
509-658 2.71e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.66  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   509 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSS-TNTL 587
Cdd:pfam13768    3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917132   588 SALKTAFADKETQA----IYLLTDGRPDQPPETVIDQVKRFQE-IPIYTISFnyNDEIANRFLKEVAALTGGEFHF 658
Cdd:pfam13768   82 GALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLISRAPGkIRFFAYGL--GASISAPMLQLLAEASNGTYEF 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 509-661 6.67e-11

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 62.47  E-value: 6.67e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132    509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKI--GSS 583
Cdd:smart00327    2 VVFLLDGSGSMgGNRFELAKEFVLKLVEqlDIGPDGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYklGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132    584 TNTLSALKTAFA----------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTG 653
Cdd:smart00327   79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158


                    ....*...
gi 767917132    654 GEFHFYNF 661
Cdd:smart00327  159 GVYVFLPE 166
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 511-660 9.01e-05

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 45.76  E-value: 9.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   511 ILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKSKFNFVKFDGQAV------AWREQLaevnEDNLEQAQSWIRDIKIGSST 584
Cdd:TIGR03436   58 LVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRllqdftSDPRLL----EAALNRLKPPLRTDYNSSGA 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   585 NTLSALKTAFADketqAIYL---------------------LTDG---RPDQPPETVIDQVKRfQEIPIYTISF---NYN 637
Cdd:TIGR03436  134 FVRDGGGTALYD----AITLaaleqlanalagipgrkalivISDGgdnRSRDTLERAIDAAQR-ADVAIYSIDArglRAP 208

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767917132   638 DEIANR--------FLKEVAALTGGEFHFYN 660
Cdd:TIGR03436  209 DLGAGAkaglggpeALERLAEETGGRAFYVN 239
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1037-1077 3.31e-03

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 36.86  E-value: 3.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767917132 1037 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVS 1077
Cdd:cd20383     2 GTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFDDGYERDVK 42
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-658 1.53e-19

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 90.00  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 586
Cdd:COG1240    95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  587 LSALKTA------FADKETQAIYLLTDGRPDQPPETVIDQVKRFQE--IPIYTISFNyNDEIANRFLKEVAALTGGEFHF 658
Cdd:COG1240   169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
DUF4537 pfam15057
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 1037-1117 1.61e-19

Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.


Pssm-ID: 464475 [Multi-domain]  Cd Length: 124  Bit Score: 85.44  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  1037 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMPCPL------------------------ 1092
Cdd:pfam15057    1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAMEHPLrvgdkvlalhdpysqsyapgivla 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767917132  1093 -------------------LQEFCPRSALIKISQNKYALSCSHI 1117
Cdd:pfam15057   81 gperrvdadeeltvrfydgKTATVPREEVYKLSQAYYEKAVAYI 124
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-659 3.94e-19

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 85.70  E-value: 3.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 584
Cdd:cd00198     2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  585 NTLSALKTAFA-------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGeFH 657
Cdd:cd00198    81 NIGAALRLALEllksakrPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG-GA 159


                  ..
gi 767917132  658 FY 659
Cdd:cd00198   160 VF 161
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 511-658 9.66e-17

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 82.07  E-value: 9.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  511 ILIDTSHSMK-SKLDLVKDKIIQFIqEQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSA 589
Cdd:COG2304    96 FVIDVSGSMSgDKLELAKEAAKLLV-DQLRPGDRVSIVTFAGDA---RVLLPPTPATDRAKILAAIDRLQAGGGTALGAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  590 LKTA-------FADKETQAIYLLTDGRPD---QPPETVIDQVKRFQE--IPIYTISF--NYNDEianrFLKEVAALTGGE 655
Cdd:COG2304   172 LELAyelarkhFIPGRVNRVILLTDGDANvgiTDPEELLKLAEEAREegITLTTLGVgsDYNED----LLERLADAGGGN 247


                  ...
gi 767917132  656 FHF 658
Cdd:COG2304   248 YYY 250
VWA_3 pfam13768
von Willebrand factor type A domain;
509-658 2.71e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.66  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   509 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSS-TNTL 587
Cdd:pfam13768    3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917132   588 SALKTAFADKETQA----IYLLTDGRPDQPPETVIDQVKRFQE-IPIYTISFnyNDEIANRFLKEVAALTGGEFHF 658
Cdd:pfam13768   82 GALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLISRAPGkIRFFAYGL--GASISAPMLQLLAEASNGTYEF 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 512-657 5.95e-12

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 65.31  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  512 LIDTSHSMKS-KLDLVKDKIIQFIQEqLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSAL 590
Cdd:cd01461     8 VIDTSGSMSGtKIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917132  591 KTAFADKET-----QAIYLLTDGRPDQpPETVIDQVKRF--QEIPIYTISFNyNDeiANRFLKEVAALTGGEFH 657
Cdd:cd01461    87 EAALELLNSspgsvPQIILLTDGEVTN-ESQILKNVREAlsGRIRLFTFGIG-SD--VNTYLLERLAREGRGIA 156
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 509-649 8.85e-12

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 67.01  E-value: 8.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  509 IYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAVawrEQLAEVNEDNLEQAQSWIRDIKIGSSTNTL 587
Cdd:COG2425   121 VVLCVDTSGSMAgSKEAAAKAAALALLRALRP-NRRFGVILFDTEVV---EDLPLTADDGLEDAIEFLSGLFAGGGTDIA 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767917132  588 SALKTAFADKETQA-----IYLLTDGRPDQPPETVIDQVK-RFQEIPIYTISFnyNDEIANRFLKEVA 649
Cdd:COG2425   197 PALRAALELLEEPDyrnadIVLITDGEAGVSPEELLREVRaKESGVRLFTVAI--GDAGNPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 509-661 6.67e-11

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 62.47  E-value: 6.67e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132    509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKI--GSS 583
Cdd:smart00327    2 VVFLLDGSGSMgGNRFELAKEFVLKLVEqlDIGPDGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYklGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132    584 TNTLSALKTAFA----------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTG 653
Cdd:smart00327   79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158


                    ....*...
gi 767917132    654 GEFHFYNF 661
Cdd:smart00327  159 GVYVFLPE 166
VWA pfam00092
von Willebrand factor type A domain;
509-661 2.47e-10

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 60.75  E-value: 2.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawrEQLAEVNED-NLEQAQSWIRDIKI--GS 582
Cdd:pfam00092    2 IVFLLDGSGSIgGDNFEKVKEFLKKLVEslDIGPDGTRVGLVQYSSDV----RTEFPLNDYsSKEELLSAVDNLRYlgGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   583 STNTLSALKTA----FADKE------TQAIYLLTDGRP-DQPPETVIDQVKRFQeIPIYTISFNYNDeiaNRFLKEVaAL 651
Cdd:pfam00092   78 TTNTGKALKYAlenlFSSAAgarpgaPKVVVLLTDGRSqDGDPEEVARELKSAG-VTVFAVGVGNAD---DEELRKI-AS 152

                          170
                   ....*....|
gi 767917132   652 TGGEFHFYNF 661
Cdd:pfam00092  153 EPGEGHVFTV 162
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
503-632 3.24e-06

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.15  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  503 RLHndcIYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKYKS-----KFNFVKFDGQAvawrEQLAEVNEdnLEQAQswIR 576
Cdd:COG4245     5 RLP---VYLLLDTSGSMSgEPIEALNEGLQALIDELRQDPYaletvEVSVITFDGEA----KVLLPLTD--LEDFQ--PP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917132  577 DIKIGSSTNTLSALKTAFA--DKETQA------------IYLLTDGRP-DQPPETVIDQVKRFQEIPIYTI 632
Cdd:COG4245    74 DLSASGGTPLGAALELLLDliERRVQKytaegkgdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANI 144
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 512-659 3.37e-06

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 48.42  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  512 LIDTSHSMKS-KLDLVKDKIIQFIqEQLKYKSKFNFVKFDG--------QAVAWREQLAEVnednleqaqswIRDIKIGS 582
Cdd:cd01465     6 VIDRSGSMDGpKLPLVKSALKLLV-DQLRPDDRLAIVTYDGaaetvlpaTPVRDKAAILAA-----------IDRLTAGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  583 STNTLSALKTA-------FADKETQAIYLLTDGRP---DQPPETVIDQV--KRFQEIPIYTISF--NYNDEianrfLKEV 648
Cdd:cd01465    74 STAGGAGIQLGyqeaqkhFVPGGVNRILLATDGDFnvgETDPDELARLVaqKRESGITLSTLGFgdNYNED-----LMEA 148

                         170
                  ....*....|.
gi 767917132  649 AALTGGEFHFY 659
Cdd:cd01465   149 IADAGNGNTAY 159
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 509-659 1.90e-05

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 46.90  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKSKFNF--VKFDGQAV-------AWREQLAEVNEdNLEQAQSWIRDI 578
Cdd:cd01470     3 IYIALDASDSIgEEDFDEAKNAIKTLIEKISSYEVSPRYeiISYASDPKeivsirdFNSNDADDVIK-RLEDFNYDDHGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  579 KIGssTNTLSALKTAF------------ADKETQ-AIYLLTDGRPDQ--PPETVIDQVKRFqeIPIYTIS---------- 633
Cdd:cd01470    82 KTG--TNTAAALKKVYermalekvrnkeAFNETRhVIILFTDGKSNMggSPLPTVDKIKNL--VYKNNKSdnpredyldv 157

                         170       180
                  ....*....|....*....|....*...
gi 767917132  634 --FNYNDEIANRFLKEVAALTGGEFHFY 659
Cdd:cd01470   158 yvFGVGDDVNKEELNDLASKKDNERHFF 185
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 512-658 5.02e-05

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 44.69  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  512 LIDTSHSMKS-KLDLVKDKIiQFIQEQLKYKSKFNFVKFDGQAvAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSAL 590
Cdd:cd01466     6 VLDVSGSMAGdKLQLVKHAL-RFVISSLGDADRLSIVTFSTSA-KRLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVGGL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917132  591 KTAFA---DKETQ----AIYLLTDGRPDQppetvIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGEFHF 658
Cdd:cd01466    84 KKALKvlgDRRQKnpvaSIMLLSDGQDNH-----GAVVLRADNAPIPIHTFGLGASHDPALLAFIAEITGGTFSY 153
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 511-660 9.01e-05

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 45.76  E-value: 9.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   511 ILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKSKFNFVKFDGQAV------AWREQLaevnEDNLEQAQSWIRDIKIGSST 584
Cdd:TIGR03436   58 LVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRllqdftSDPRLL----EAALNRLKPPLRTDYNSSGA 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132   585 NTLSALKTAFADketqAIYL---------------------LTDG---RPDQPPETVIDQVKRfQEIPIYTISF---NYN 637
Cdd:TIGR03436  134 FVRDGGGTALYD----AITLaaleqlanalagipgrkalivISDGgdnRSRDTLERAIDAAQR-ADVAIYSIDArglRAP 208

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767917132   638 DEIANR--------FLKEVAALTGGEFHFYN 660
Cdd:TIGR03436  209 DLGAGAkaglggpeALERLAEETGGRAFYVN 239
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 509-659 4.77e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 42.28  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAqswIRDIKI--GSS 583
Cdd:cd01450     3 IVFLLDGSESVgPENFEKVKDFIEKLVEklDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA---VKNLKYlgGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917132  584 TNTLSALKTAFA---------DKETQAIYLLTDGRP--DQPPETVIDQVKRFQeIPIYTISFNYNDEianRFLKEVAAlT 652
Cdd:cd01450    80 TNTGKALQYALEqlfsesnarENVPKVIIVLTDGRSddGGDPKEAAAKLKDEG-IKVFVVGVGPADE---EELREIAS-C 154


                  ....*..
gi 767917132  653 GGEFHFY 659
Cdd:cd01450   155 PSERHVF 161
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1037-1077 3.31e-03

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 36.86  E-value: 3.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767917132 1037 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVS 1077
Cdd:cd20383     2 GTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFDDGYERDVK 42
 
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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