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Conserved domains on  [gi|1938949930|pdb|5VHH|b]
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Protein Classification

26S proteasome regulatory subunit RPN10( domain architecture ID 10106897)

26S proteasome regulatory subunit RPN10 is a multiubiquitin binding protein

CATH:  3.40.50.410
Gene Ontology:  GO:0008540|GO:0006511|GO:0043130|GO:0031593
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 1-187 4.97e-119

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


:

Pssm-ID: 238729  Cd Length: 187  Bit Score: 334.72  E-value: 4.97e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        1 MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLAND-CEVLTTLTPDTGRILSKLHTVQ 79
Cdd:cd01452   1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNsPEVLVTLTNDQGKILSKLHDVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b       80 PKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNT 159
Cdd:cd01452  81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNTEKLTAFIDA 160

                       170       180
                ....*....|....*....|....*....
5VHH_b      160 LNGKDgtGSHLVTVPPGPSLA-DALISSP 187
Cdd:cd01452 161 VNGKD--GSHLVSVPPGENLLsDALLSSP 187
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 1-187 4.97e-119

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 334.72  E-value: 4.97e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        1 MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLAND-CEVLTTLTPDTGRILSKLHTVQ 79
Cdd:cd01452   1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNsPEVLVTLTNDQGKILSKLHDVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b       80 PKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNT 159
Cdd:cd01452  81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNTEKLTAFIDA 160

                       170       180
                ....*....|....*....|....*....
5VHH_b      160 LNGKDgtGSHLVTVPPGPSLA-DALISSP 187
Cdd:cd01452 161 VNGKD--GSHLVSVPPGENLLsDALLSSP 187
VWA_2 pfam13519
von Willebrand factor type A domain;
6-112 4.34e-29

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 103.91  E-value: 4.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b          6 TMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHsktrSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKIT 85
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALLK----SLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPKGGGT 76

                          90       100
                  ....*....|....*....|....*...
5VHH_b         86 -FCTGIRVAHLALKHRQgKNHKMRIIAF 112
Cdd:pfam13519  77 nLAAALQLARAALKHRR-KNQPRRIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 7-187 2.40e-16

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: 72.87  E-value: 2.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b           7 MVCVDNSEYMRngdflPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTL--TPDTGRILSKLHTVQPK-GK 83
Cdd:smart00327   3 VFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYKlGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b          84 IT-FCTGIRVAHLALKHRQGKNHKMR---IIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGeeevnTEKLTAFVNT 159
Cdd:smart00327  78 GTnLGAALQYALENLFSKSAGSRRGApkvVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG-----NDVDEEELKK 152

                          170       180
                   ....*....|....*....|....*...
5VHH_b         160 LNGKDGTGSHLVtvppgPSLADALISSP 187
Cdd:smart00327 153 LASAPGGVYVFL-----PELLDLLIDLL 175
PRK13685 PRK13685
hypothetical protein; Provisional
 7-67 1.07e-03

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 38.91  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
5VHH_b         7 MVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTrsnPENNVGLITLANDCEVLTTLTPD 67
Cdd:PRK13685  92 MLVIDVSQSMRATDVEPNRLAAAQEAAKQFADELT---PGINLGLIAFAGTATVLVSPTTN 149
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
 2-146 4.57e-03

RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227480 [Multi-domain]  Cd Length: 421  Bit Score: 36.90  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        2 VLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTT-LTPDTGRILSKLHTV-Q 79
Cdd:COG5151  86 IIRHLHLILDVSEAMDESDFLPTRRANVIKYAEGFVPEFFSQNPISQLSIISIRDGCAKYTSsMDGNPQAHIGQLKSKrD 165

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VHH_b       80 PKGKITFCTGIRVAHLALKHRqgKNHKMR-IIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEE 146
Cdd:COG5151 166 CSGNFSLQNALEMARIELMKN--TMHGTReVLIIFGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAE 231
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 1-187 4.97e-119

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 334.72  E-value: 4.97e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        1 MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLAND-CEVLTTLTPDTGRILSKLHTVQ 79
Cdd:cd01452   1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNsPEVLVTLTNDQGKILSKLHDVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b       80 PKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNT 159
Cdd:cd01452  81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNTEKLTAFIDA 160

                       170       180
                ....*....|....*....|....*....
5VHH_b      160 LNGKDgtGSHLVTVPPGPSLA-DALISSP 187
Cdd:cd01452 161 VNGKD--GSHLVSVPPGENLLsDALLSSP 187
VWA_2 pfam13519
von Willebrand factor type A domain;
6-112 4.34e-29

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 103.91  E-value: 4.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b          6 TMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHsktrSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKIT 85
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALLK----SLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPKGGGT 76

                          90       100
                  ....*....|....*....|....*...
5VHH_b         86 -FCTGIRVAHLALKHRQgKNHKMRIIAF 112
Cdd:pfam13519  77 nLAAALQLARAALKHRR-KNQPRRIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 7-187 2.40e-16

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: 72.87  E-value: 2.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b           7 MVCVDNSEYMRngdflPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTL--TPDTGRILSKLHTVQPK-GK 83
Cdd:smart00327   3 VFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYKlGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b          84 IT-FCTGIRVAHLALKHRQGKNHKMR---IIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGeeevnTEKLTAFVNT 159
Cdd:smart00327  78 GTnLGAALQYALENLFSKSAGSRRGApkvVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG-----NDVDEEELKK 152

                          170       180
                   ....*....|....*....|....*...
5VHH_b         160 LNGKDGTGSHLVtvppgPSLADALISSP 187
Cdd:smart00327 153 LASAPGGVYVFL-----PELLDLLIDLL 175
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 7-162 3.65e-10

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: 56.03  E-value: 3.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        7 MVCVDNSEYMRngdflPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTG-----RILSKLHTvQPK 81
Cdd:cd00198   4 VFLLDVSGSMG-----GEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDkadllEAIDALKK-GLG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b       82 GKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGeEEVNTEKLTAFVNTLN 161
Cdd:cd00198  78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIG-DDANEDELKEIADKTT 156


                .
5VHH_b      162 G 162
Cdd:cd00198 157 G 157
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
 7-141 2.92e-07

Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.


Pssm-ID: 238730  Cd Length: 183  Bit Score: 48.48  E-value: 2.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        7 MVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDC-EVLTTLTPDTGRILSKLHTVQ-PKGKI 84
Cdd:cd01453   7 IIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRaEKLTDLTGNPRKHIQALKTAReCSGEP 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
5VHH_b       85 TFCTGIRVAHLALKHRQGKNHKMRIIAFvGSPVEDNEKDLVKLAKRLKKEKVNVDII 141
Cdd:cd01453  87 SLQNGLEMALESLKHMPSHGSREVLIIF-SSLSTCDPGNIYETIDKLKKENIRVSVI 142
PRK13685 PRK13685
hypothetical protein; Provisional
 7-67 1.07e-03

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 38.91  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
5VHH_b         7 MVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTrsnPENNVGLITLANDCEVLTTLTPD 67
Cdd:PRK13685  92 MLVIDVSQSMRATDVEPNRLAAAQEAAKQFADELT---PGINLGLIAFAGTATVLVSPTTN 149
VWA pfam00092
von Willebrand factor type A domain;
10-145 1.89e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 37.25  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b         10 VDNSEYMRNGDFlptrlQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGR--ILSKLHTVQPKGKITFC 87
Cdd:pfam00092   6 LDGSGSIGGDNF-----EKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
5VHH_b         88 TG---IRVAHLALKHRQG--KNHKMRIIAFVGSpvEDNEKDLVKLAKRLKKEKVNVDIINFGE 145
Cdd:pfam00092  81 TGkalKYALENLFSSAAGarPGAPKVVVLLTDG--RSQDGDPEEVARELKSAGVTVFAVGVGN 141
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 7-148 2.42e-03

VWA BatA 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 37.31  E-value: 2.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        7 MVCVDNSEYMRNGDF-LPTRLQAQQDAV-NIVchsKTRSNpeNNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPK--G 82
Cdd:cd01467   6 MIALDVSGSMLAQDFvKPSRLEAAKEVLsDFI---DRREN--DRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGlaG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
5VHH_b       83 KIT-FCTGIRVAHLALKHRQGKNhkmRIIAFVgSPVEDNEKDLVKL-AKRLKKEK-VNVDIINFGEEEV 148
Cdd:cd01467  81 QGTaIGDAIGLAIKRLKNSEAKE---RVIVLL-TDGENNAGEIDPAtAAELAKNKgVRIYTIGVGKSGS 145
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
 2-146 4.57e-03

RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227480 [Multi-domain]  Cd Length: 421  Bit Score: 36.90  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VHH_b        2 VLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTT-LTPDTGRILSKLHTV-Q 79
Cdd:COG5151  86 IIRHLHLILDVSEAMDESDFLPTRRANVIKYAEGFVPEFFSQNPISQLSIISIRDGCAKYTSsMDGNPQAHIGQLKSKrD 165

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VHH_b       80 PKGKITFCTGIRVAHLALKHRqgKNHKMR-IIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEE 146
Cdd:COG5151 166 CSGNFSLQNALEMARIELMKN--TMHGTReVLIIFGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAE 231
vWA_BABAM1 cd21502
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ...
 9-80 9.48e-03

Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and BRCA1 A complex member 1 (BABAM1) is also known as Mediator of RAP80 interactions and targeting subunit of 40 kDa (MERIT40), New component of the BRCA1-A complex (NBA1), HSPC142, or C19orf620. It is a core component of the BRCA1-A and BRISC complexes that function in DNA double-strand break repair and immune signaling, and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits Abraxas and ABRO1, respectively. BABAM1 interacts with Rap80, BRCC36, BRCC45, and Abraxas to form the BRCA1-A complex, a lysine-63-Ub specific deubiquitinating enzyme (DUB) which specifically recognizes lysine-63-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). BRISC is a DUB complex containing three other subunits, BRCC36, ABRO1 and BRCC45. It specifically hydrolyzes lysine-63 polyubiquitin chains, and is involved in multiple biological processes, including IFN-mediated antiviral immune regulation and inflammatory reaction. BABAM1 likely serves as a scaffold protein by integrating other components to form a functional complex. Furthermore, BABAM1 has been shown to play a critical role in BRISC-mediated regulation of Tankyrase1 (TNKS1) function during spindle assembly; it directly binds to the ankyrin repeat cluster V (ARC-V) domain of TNKS1 via its RXXPEG motif. BABAM1 contains a Von-Willebrand factor A (vWA) domain that is distantly related to classical vWA domains.


Pssm-ID: 411071  Cd Length: 216  Bit Score: 35.69  E-value: 9.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VHH_b        9 CVD-----NSEYMRNGDFLP-TRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQP 80
Cdd:cd21502   8 CIDlseemNTTPFESTNGSKyTRLDMLKRALELFVHTKSRINPRHEFALVVLNESASWLQDFTSDPKDILSALDDLEP 85
 
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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