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Conserved domains on  [gi|1061899850|ref|NP_001317949|]
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RNA-binding protein RO60 isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TROVE super family cl05344
TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding ...
 1-94 1.55e-28

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.


The actual alignment was detected with superfamily member pfam05731:

Pssm-ID: 461724  Cd Length: 361  Bit Score: 111.33  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850   1 MPLTALLRNLGKMTANSVLEPGNseVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDA 80
Cdd:pfam05731 270 LPMMAMLRNLCNLLRVGVSARHH--EDLVLQRLQNPKSVIHSRQHPFRFLNAHVVYEQGKGEKGKLQWKPDPEISQALEA 347

                          90
                  ....*....|....
gi 1061899850  81 AFYKTFKTVEPTGK 94
Cdd:pfam05731 348 AFYLAVKNLPPTPG 361
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 88-214 2.12e-11

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


:

Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 62.39  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  88 TVEPTGKRFLLAVDVSASMNqrvlGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMV-PCPVTTDMTLQQVLMAMSQIP 166
Cdd:COG2425   113 AVPLLEGPVVLCVDTSGSMA----GSKEAAAKAAALALLRALRPNRRFGVILFDTEVVeDLPLTADDGLEDAIEFLSGLF 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1061899850 167 A-GGTDCSLPMIWA----QKTNTPADVFIVFTDNEtfAGGVHPAIaLREYRKK 214
Cdd:COG2425   189 AgGGTDIAPALRAAlellEEPDYRNADIVLITDGE--AGVSPEEL-LREVRAK 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 ...
 1-94 1.55e-28

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: 111.33  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850   1 MPLTALLRNLGKMTANSVLEPGNseVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDA 80
Cdd:pfam05731 270 LPMMAMLRNLCNLLRVGVSARHH--EDLVLQRLQNPKSVIHSRQHPFRFLNAHVVYEQGKGEKGKLQWKPDPEISQALEA 347

                          90
                  ....*....|....
gi 1061899850  81 AFYKTFKTVEPTGK 94
Cdd:pfam05731 348 AFYLAVKNLPPTPG 361
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 88-214 2.12e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 62.39  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  88 TVEPTGKRFLLAVDVSASMNqrvlGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMV-PCPVTTDMTLQQVLMAMSQIP 166
Cdd:COG2425   113 AVPLLEGPVVLCVDTSGSMA----GSKEAAAKAAALALLRALRPNRRFGVILFDTEVVeDLPLTADDGLEDAIEFLSGLF 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1061899850 167 A-GGTDCSLPMIWA----QKTNTPADVFIVFTDNEtfAGGVHPAIaLREYRKK 214
Cdd:COG2425   189 AgGGTDIAPALRAAlellEEPDYRNADIVLITDGE--AGVSPEEL-LREVRAK 238
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 97-214 2.19e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 40.63  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  97 LLAVDVSASMNQRVLGSILNAstVAAAMCMVVTRTEKDSY-VVAFSDE-MVPCPVTTDMTLQQVLMAMSQIPA---GGTD 171
Cdd:cd00198     4 VFLLDVSGSMGGEKLDKAKEA--LKALVSSLSASPPGDRVgLVTFGSNaRVVLPLTTDTDKADLLEAIDALKKglgGGTN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1061899850 172 ------CSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKK 214
Cdd:cd00198    82 igaalrLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL 130
DUF2201 pfam09967
VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has ...
 98-206 1.53e-03

VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has no known function. However, it is clearly related to the VWA domain.


Pssm-ID: 401806  Cd Length: 123  Bit Score: 37.75  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  98 LAVDVSASMNQRVLgsilnaSTVAAAMCMVVTRTEKDSYVVAFSDEMVPCP-VTTDMTLQQVLMAmsqiPAGGTDCSLPM 176
Cdd:pfam09967   3 LAVDTSGSITDPLL------ARFAAEIAGILRRYPAEVHVLAFDETVQSVQrIEPASYLAELQFT----GGGGTDLVPVL 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 1061899850 177 IWAQKtNTPaDVFIVFTDNETFAGGVHPAI 206
Cdd:pfam09967  73 EWASR-LRP-DAAVVLTDLEGWPMEPRPGI 100
 
Name Accession Description Interval E-value
TROVE pfam05731
TROVE domain; This presumed domain is found in TEP1 and Ro60 proteins, that are RNA-binding ...
 1-94 1.55e-28

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: 111.33  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850   1 MPLTALLRNLGKMTANSVLEPGNseVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDA 80
Cdd:pfam05731 270 LPMMAMLRNLCNLLRVGVSARHH--EDLVLQRLQNPKSVIHSRQHPFRFLNAHVVYEQGKGEKGKLQWKPDPEISQALEA 347

                          90
                  ....*....|....
gi 1061899850  81 AFYKTFKTVEPTGK 94
Cdd:pfam05731 348 AFYLAVKNLPPTPG 361
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 88-214 2.12e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 62.39  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  88 TVEPTGKRFLLAVDVSASMNqrvlGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMV-PCPVTTDMTLQQVLMAMSQIP 166
Cdd:COG2425   113 AVPLLEGPVVLCVDTSGSMA----GSKEAAAKAAALALLRALRPNRRFGVILFDTEVVeDLPLTADDGLEDAIEFLSGLF 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1061899850 167 A-GGTDCSLPMIWA----QKTNTPADVFIVFTDNEtfAGGVHPAIaLREYRKK 214
Cdd:COG2425   189 AgGGTDIAPALRAAlellEEPDYRNADIVLITDGE--AGVSPEEL-LREVRAK 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 62-242 7.98e-05

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: 43.00  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  62 LRGKLKWRPDEEILKALDAAFYKTFKTVEPTGKRFLLAVDVSASMNQRvlgSILNASTVAAAmcMVVTRTEKDSYV--VA 139
Cdd:COG1240    61 LLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAE---NRLEAAKGALL--DFLDDYRPRDRVglVA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850 140 FSDE-MVPCPVTTDmtLQQVLMAMSQIPAGG-TDCSLPMIWAQKT---NTPAD--VFIVFTDNETFAGGVHPAIALREYR 212
Cdd:COG1240   136 FGGEaEVLLPLTRD--REALKRALDELPPGGgTPLGDALALALELlkrADPARrkVIVLLTDGRDNAGRIDPLEAAELAA 213

                         170       180       190
                  ....*....|....*....|....*....|
gi 1061899850 213 KKmDIPAKLIVCGmtsngftiADPDDRGML 242
Cdd:COG1240   214 AA-GIRIYTIGVG--------TEAVDEGLL 234
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 97-214 2.19e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 40.63  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  97 LLAVDVSASMNQRVLGSILNAstVAAAMCMVVTRTEKDSY-VVAFSDE-MVPCPVTTDMTLQQVLMAMSQIPA---GGTD 171
Cdd:cd00198     4 VFLLDVSGSMGGEKLDKAKEA--LKALVSSLSASPPGDRVgLVTFGSNaRVVLPLTTDTDKADLLEAIDALKKglgGGTN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1061899850 172 ------CSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKK 214
Cdd:cd00198    82 igaalrLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL 130
DUF2201 pfam09967
VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has ...
 98-206 1.53e-03

VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has no known function. However, it is clearly related to the VWA domain.


Pssm-ID: 401806  Cd Length: 123  Bit Score: 37.75  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  98 LAVDVSASMNQRVLgsilnaSTVAAAMCMVVTRTEKDSYVVAFSDEMVPCP-VTTDMTLQQVLMAmsqiPAGGTDCSLPM 176
Cdd:pfam09967   3 LAVDTSGSITDPLL------ARFAAEIAGILRRYPAEVHVLAFDETVQSVQrIEPASYLAELQFT----GGGGTDLVPVL 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 1061899850 177 IWAQKtNTPaDVFIVFTDNETFAGGVHPAI 206
Cdd:pfam09967  73 EWASR-LRP-DAAVVLTDLEGWPMEPRPGI 100
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 96-194 3.25e-03

VWA YIEM 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 have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 37.33  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  96 FLLAVDVSASMnqrVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVT-TDMTLQQVLMAMSQIPAGGTDCSL 174
Cdd:cd01462     3 VILLVDQSGSM---YGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDkTDDLEEPVEFLSGVQLGGGTDINK 79

                          90       100
                  ....*....|....*....|....
gi 1061899850 175 PMIWAQ---KTNTPADVFIVF-TD 194
Cdd:cd01462    80 ALRYALeliERRDPRKADIVLiTD 103
VWA_2 pfam13519
von Willebrand factor type A domain;
96-191 4.77e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 35.73  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899850  96 FLLAVDVSASMNQRVLGsILNASTVAAAMCMVVTRTEKDSY-VVAFSDEM-VPCPVTTDmtLQQVLMAMSQIPA--GGTD 171
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYG-PTRLEAAKDAVLALLKSLPGDRVgLVTFGDGPeVLIPLTKD--RAKILRALRRLEPkgGGTN 77

                          90       100
                  ....*....|....*....|....*.
gi 1061899850 172 CSLPM------IWAQKTNTPADVFIV 191
Cdd:pfam13519  78 LAAALqlaraaLKHRRKNQPRRIVLI 103
 
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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