NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039728064|ref|XP_017174940|]
View 

RNA-binding protein Ro60 isoform X1 [Mus musculus]

Protein Classification

VWA domain-containing protein; vWA domain-containing protein( domain architecture ID 12065416)

VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein with an extracellular solute-binding protein (SBP) domain; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein with C-terminal prealbumin-like fold domain that is similar to Corynebacterium diphtheriae domain 1 and domain 3 of surface-anchored protein fimbrial subunit SpaA; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein with C-terminal prealbumin-like fold domain that is similar to bacterial pilin adhesin subunit SpaC; von Willebrand factor type A (vWA) domain containing protein, often found at C-terminus of CalY family proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
TROVE pfam05731
TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding ...
16-369 1.65e-101

TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding components of Telomerase, Ro and Vault RNPs. This domain has been named TROVE, (after Telomerase, Ro and Vault). This domain is probably RNA-binding.


:

Pssm-ID: 461724  Cd Length: 361  Bit Score: 310.09  E-value: 1.65e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064  16 VVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIrLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFA 95
Cdd:pfam05731   1 VSNDSGGYPEPTDDVLQEKRFLLLGLLCGTYYTLASEVTMDNAQAIK-IIEDGTGASILETLRELSAAGRAPKEPEFILK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064  96 LAVCSQCADINTKQA----AFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGM--WGRALRKAVADWYNEKGGMAVALVVT 169
Cdd:pfam05731  80 LALYARQQLNIRDVAnhvlAIAAVLPVCRLPTDLFEVAEYCEELAEGDEKKLtgWGRCLRRAMTDWYTSKFAEFLAYQLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 170 KYKQRNGWSHKDLLRLSHLKPSSEG---LAIVTKYITKGWKEVHEEYKEkalsVEAEKLLKYL---EAVEKVKRTKDDLE 243
Cdd:pfam05731 160 KYNTRKHWSHKDPFRLPHPPKFSETsleLKGLFRYATKEQRKFEKAYGA----VPEKKESKRLtlkKLVQRLHISEPAEH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 244 VIHLI-EEHQLVREHLLTNHLKSKEVWKALLQE-MPLTALLRNLGKMTANSVLEPGNseVSLICEKLSNEKLLKKARIHP 321
Cdd:pfam05731 236 VQALIgKRYRLTWEREPSLRGNSAEVWEELIDSkLPMMAMLRNLCNLLRVGVSARHH--EDLVLQRLQNPKSVIHSRQHP 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1039728064 322 FHVLIALETYRAGHGLRGKLKWIPDKDILQALDAAFYTTFKTVEPTGK 369
Cdd:pfam05731 314 FRFLNAHVVYEQGKGEKGKLQWKPDPEISQALEAAFYLAVKNLPPTPG 361
ViaA super family cl27002
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
363-489 5.63e-08

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


The actual alignment was detected with superfamily member COG2425:

Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 54.30  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 363 TVEPTGKRFLLAVDVSASMNqralGSVLNASTVAAAMCMVVTRTEKESSVVAFACDMV-PFPVTTDMTLQQVLTAMNKVP 441
Cdd:COG2425   113 AVPLLEGPVVLCVDTSGSMA----GSKEAAAKAAALALLRALRPNRRFGVILFDTEVVeDLPLTADDGLEDAIEFLSGLF 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039728064 442 A-GNTDCSLPMIWA----QKTDTAADVFVVFTDNETfagQVHPAVALREYRKK 489
Cdd:COG2425   189 AgGGTDIAPALRAAlellEEPDYRNADIVLITDGEA---GVSPEELLREVRAK 238
 
Name Accession Description Interval E-value
TROVE pfam05731
TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding ...
16-369 1.65e-101

TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding components of Telomerase, Ro and Vault RNPs. This domain has been named TROVE, (after Telomerase, Ro and Vault). This domain is probably RNA-binding.


Pssm-ID: 461724  Cd Length: 361  Bit Score: 310.09  E-value: 1.65e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064  16 VVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIrLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFA 95
Cdd:pfam05731   1 VSNDSGGYPEPTDDVLQEKRFLLLGLLCGTYYTLASEVTMDNAQAIK-IIEDGTGASILETLRELSAAGRAPKEPEFILK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064  96 LAVCSQCADINTKQA----AFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGM--WGRALRKAVADWYNEKGGMAVALVVT 169
Cdd:pfam05731  80 LALYARQQLNIRDVAnhvlAIAAVLPVCRLPTDLFEVAEYCEELAEGDEKKLtgWGRCLRRAMTDWYTSKFAEFLAYQLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 170 KYKQRNGWSHKDLLRLSHLKPSSEG---LAIVTKYITKGWKEVHEEYKEkalsVEAEKLLKYL---EAVEKVKRTKDDLE 243
Cdd:pfam05731 160 KYNTRKHWSHKDPFRLPHPPKFSETsleLKGLFRYATKEQRKFEKAYGA----VPEKKESKRLtlkKLVQRLHISEPAEH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 244 VIHLI-EEHQLVREHLLTNHLKSKEVWKALLQE-MPLTALLRNLGKMTANSVLEPGNseVSLICEKLSNEKLLKKARIHP 321
Cdd:pfam05731 236 VQALIgKRYRLTWEREPSLRGNSAEVWEELIDSkLPMMAMLRNLCNLLRVGVSARHH--EDLVLQRLQNPKSVIHSRQHP 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1039728064 322 FHVLIALETYRAGHGLRGKLKWIPDKDILQALDAAFYTTFKTVEPTGK 369
Cdd:pfam05731 314 FRFLNAHVVYEQGKGEKGKLQWKPDPEISQALEAAFYLAVKNLPPTPG 361
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
363-489 5.63e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 54.30  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 363 TVEPTGKRFLLAVDVSASMNqralGSVLNASTVAAAMCMVVTRTEKESSVVAFACDMV-PFPVTTDMTLQQVLTAMNKVP 441
Cdd:COG2425   113 AVPLLEGPVVLCVDTSGSMA----GSKEAAAKAAALALLRALRPNRRFGVILFDTEVVeDLPLTADDGLEDAIEFLSGLF 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039728064 442 A-GNTDCSLPMIWA----QKTDTAADVFVVFTDNETfagQVHPAVALREYRKK 489
Cdd:COG2425   189 AgGGTDIAPALRAAlellEEPDYRNADIVLITDGEA---GVSPEELLREVRAK 238
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
372-489 2.63e-05

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: 44.48  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 372 LLAVDVSASMNQRALGSVLNAstvAAAMcmvVTRTEKES-----SVVAFACD-MVPFPVTTDMTLQQVLTAMNKVPA--- 442
Cdd:cd00198     4 VFLLDVSGSMGGEKLDKAKEA---LKAL---VSSLSASPpgdrvGLVTFGSNaRVVLPLTTDTDKADLLEAIDALKKglg 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039728064 443 GNTD------CSLPMIWAQKTDTAADVFVVFTDNETFAGQVHPAVALREYRKK 489
Cdd:cd00198    78 GGTNigaalrLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL 130
 
Name Accession Description Interval E-value
TROVE pfam05731
TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding ...
16-369 1.65e-101

TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding components of Telomerase, Ro and Vault RNPs. This domain has been named TROVE, (after Telomerase, Ro and Vault). This domain is probably RNA-binding.


Pssm-ID: 461724  Cd Length: 361  Bit Score: 310.09  E-value: 1.65e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064  16 VVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIrLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFA 95
Cdd:pfam05731   1 VSNDSGGYPEPTDDVLQEKRFLLLGLLCGTYYTLASEVTMDNAQAIK-IIEDGTGASILETLRELSAAGRAPKEPEFILK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064  96 LAVCSQCADINTKQA----AFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGM--WGRALRKAVADWYNEKGGMAVALVVT 169
Cdd:pfam05731  80 LALYARQQLNIRDVAnhvlAIAAVLPVCRLPTDLFEVAEYCEELAEGDEKKLtgWGRCLRRAMTDWYTSKFAEFLAYQLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 170 KYKQRNGWSHKDLLRLSHLKPSSEG---LAIVTKYITKGWKEVHEEYKEkalsVEAEKLLKYL---EAVEKVKRTKDDLE 243
Cdd:pfam05731 160 KYNTRKHWSHKDPFRLPHPPKFSETsleLKGLFRYATKEQRKFEKAYGA----VPEKKESKRLtlkKLVQRLHISEPAEH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 244 VIHLI-EEHQLVREHLLTNHLKSKEVWKALLQE-MPLTALLRNLGKMTANSVLEPGNseVSLICEKLSNEKLLKKARIHP 321
Cdd:pfam05731 236 VQALIgKRYRLTWEREPSLRGNSAEVWEELIDSkLPMMAMLRNLCNLLRVGVSARHH--EDLVLQRLQNPKSVIHSRQHP 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1039728064 322 FHVLIALETYRAGHGLRGKLKWIPDKDILQALDAAFYTTFKTVEPTGK 369
Cdd:pfam05731 314 FRFLNAHVVYEQGKGEKGKLQWKPDPEISQALEAAFYLAVKNLPPTPG 361
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
363-489 5.63e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 54.30  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 363 TVEPTGKRFLLAVDVSASMNqralGSVLNASTVAAAMCMVVTRTEKESSVVAFACDMV-PFPVTTDMTLQQVLTAMNKVP 441
Cdd:COG2425   113 AVPLLEGPVVLCVDTSGSMA----GSKEAAAKAAALALLRALRPNRRFGVILFDTEVVeDLPLTADDGLEDAIEFLSGLF 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039728064 442 A-GNTDCSLPMIWA----QKTDTAADVFVVFTDNETfagQVHPAVALREYRKK 489
Cdd:COG2425   189 AgGGTDIAPALRAAlellEEPDYRNADIVLITDGEA---GVSPEELLREVRAK 238
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
372-489 2.63e-05

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: 44.48  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728064 372 LLAVDVSASMNQRALGSVLNAstvAAAMcmvVTRTEKES-----SVVAFACD-MVPFPVTTDMTLQQVLTAMNKVPA--- 442
Cdd:cd00198     4 VFLLDVSGSMGGEKLDKAKEA---LKAL---VSSLSASPpgdrvGLVTFGSNaRVVLPLTTDTDKADLLEAIDALKKglg 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039728064 443 GNTD------CSLPMIWAQKTDTAADVFVVFTDNETFAGQVHPAVALREYRKK 489
Cdd:cd00198    78 GGTNigaalrLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH