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Conserved domains on  [gi|1370454141|ref|XP_024304632|]
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replication protein A 32 kDa subunit isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RPA_C pfam08784
Replication protein A C terminal; This domain corresponds to the C terminal of the single ...
 141-237 1.75e-30

Replication protein A C terminal; This domain corresponds to the C terminal of the single stranded DNA binding protein RPA (replication protein A). RPA is involved in many DNA metabolic pathways including DNA replication, DNA repair, recombination, cell cycle and DNA damage checkpoints.


:

Pssm-ID: 400920  Cd Length: 106  Bit Score: 109.00  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 141 HMVLSKANSQPSAGRAPISNP-----GMSEAGNFGGNSFMPAN----GLTVAQNQVLNLIK-ACPRPEGLNFQDLKNQLk 210
Cdd:pfam08784   1 HLFLTKGASGSSGGGATTPAVsnggsSMGTQGAYSGGDASVVNanngGLTPLQDQVLNLIKqPPNGNEGVHVDEIAQRL- 79

                          90       100
                  ....*....|....*....|....*..
gi 1370454141 211 HMSVSSIKQAVDFLSNEGHIYSTVDDD 237
Cdd:pfam08784  80 GLPVNDVKQAVDFLSNEGHIYSTIDDD 106
RPA2_DBD_D cd04478
RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding ...
 73-142 4.27e-28

RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B; RPA2 DBD-D is a weak ssDNA-binding domain. RPA2 DBD-D is also involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. N-terminal to human RPA2 DBD-D is a domain containing all the known phosphorylation sites of RPA. Human RPA2 is phosphorylated in a cell cycle dependent manner in response to DNA damage. RPA2 interacts physically with menin; the gene encoding menin is a tumor suppressor gene disrupted in multiple endocrine neoplasia type I. This subfamily also includes RPA2 from Cryptosporidium parvum (CpRPA2). CpRPA2 is an SSB, which can be phosphorylated by DNA-PK in vitro.


:

Pssm-ID: 239924  Cd Length: 95  Bit Score: 102.68  E-value: 4.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141  73 QVTIVGIIRHAEKAPTNIVYKIDDMTAaPMDVRQWVDTDN--------------------------KKSLVAFKIMPLED 126
Cdd:cd04478     1 QVTLVGVVRNVEEQSTNITYTIDDGTG-TIEVRQWLDDDNddssevepieegtyvrvfgnlksfqgKKSIMAFSIRPVTD 79

                          90
                  ....*....|....*.
gi 1370454141 127 MNEFTTHILEVINAHM 142
Cdd:cd04478    80 FNEVTYHLLEVIYVHL 95
 
Name Accession Description Interval E-value
RPA_C pfam08784
Replication protein A C terminal; This domain corresponds to the C terminal of the single ...
 141-237 1.75e-30

Replication protein A C terminal; This domain corresponds to the C terminal of the single stranded DNA binding protein RPA (replication protein A). RPA is involved in many DNA metabolic pathways including DNA replication, DNA repair, recombination, cell cycle and DNA damage checkpoints.


Pssm-ID: 400920  Cd Length: 106  Bit Score: 109.00  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 141 HMVLSKANSQPSAGRAPISNP-----GMSEAGNFGGNSFMPAN----GLTVAQNQVLNLIK-ACPRPEGLNFQDLKNQLk 210
Cdd:pfam08784   1 HLFLTKGASGSSGGGATTPAVsnggsSMGTQGAYSGGDASVVNanngGLTPLQDQVLNLIKqPPNGNEGVHVDEIAQRL- 79

                          90       100
                  ....*....|....*....|....*..
gi 1370454141 211 HMSVSSIKQAVDFLSNEGHIYSTVDDD 237
Cdd:pfam08784  80 GLPVNDVKQAVDFLSNEGHIYSTIDDD 106
RPA2_DBD_D cd04478
RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding ...
 73-142 4.27e-28

RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B; RPA2 DBD-D is a weak ssDNA-binding domain. RPA2 DBD-D is also involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. N-terminal to human RPA2 DBD-D is a domain containing all the known phosphorylation sites of RPA. Human RPA2 is phosphorylated in a cell cycle dependent manner in response to DNA damage. RPA2 interacts physically with menin; the gene encoding menin is a tumor suppressor gene disrupted in multiple endocrine neoplasia type I. This subfamily also includes RPA2 from Cryptosporidium parvum (CpRPA2). CpRPA2 is an SSB, which can be phosphorylated by DNA-PK in vitro.


Pssm-ID: 239924  Cd Length: 95  Bit Score: 102.68  E-value: 4.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141  73 QVTIVGIIRHAEKAPTNIVYKIDDMTAaPMDVRQWVDTDN--------------------------KKSLVAFKIMPLED 126
Cdd:cd04478     1 QVTLVGVVRNVEEQSTNITYTIDDGTG-TIEVRQWLDDDNddssevepieegtyvrvfgnlksfqgKKSIMAFSIRPVTD 79

                          90
                  ....*....|....*.
gi 1370454141 127 MNEFTTHILEVINAHM 142
Cdd:cd04478    80 FNEVTYHLLEVIYVHL 95
RFA2 COG5235
Single-stranded DNA-binding replication protein A (RPA), medium (30 kD) subunit [DNA ...
 25-242 4.83e-28

Single-stranded DNA-binding replication protein A (RPA), medium (30 kD) subunit [DNA replication, recombination, and repair];


Pssm-ID: 227560 [Multi-domain]  Cd Length: 258  Bit Score: 107.37  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141  25 GGF---GSPaPSQAEKKSRARAQHIVPCTISQLLSATLV--DEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTA 99
Cdd:COG5235    16 GQIfgtGSP-PPMDRSEGGYIVNTLRPVTIKQILSCDQDetDSTFLVDSAEVTNVQFVGVVRNIKTSTTNSMFVIEDGTG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 100 ApMDVRQWVDTDN-------------------------KKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAG 154
Cdd:COG5235    95 S-IEVRFWPGNSYeeeqckdleeqnyvkvngslktfngKRSISASHISAIEDSNEVTYHFLECIYQHLFYTRQLQRPLEE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 155 RAPisNPGMSEAGNFGGNSFMPANGLTVAQNQVLnliKACPRPEGLNFQDLKNQL-KHMSVSSIKQAVDFLSNEGHIYST 233
Cdd:COG5235   174 EVK--NDGQSLFAKLDNDTSSGSSRLQEDILECY---RRNQDENGLHINVVIKMLsQSYSEDETRVNIDVLLRDGHIYPT 248


                  ....*....
gi 1370454141 234 VDDDHFKST 242
Cdd:COG5235   249 VDGNEFKTT 257
 
Name Accession Description Interval E-value
RPA_C pfam08784
Replication protein A C terminal; This domain corresponds to the C terminal of the single ...
 141-237 1.75e-30

Replication protein A C terminal; This domain corresponds to the C terminal of the single stranded DNA binding protein RPA (replication protein A). RPA is involved in many DNA metabolic pathways including DNA replication, DNA repair, recombination, cell cycle and DNA damage checkpoints.


Pssm-ID: 400920  Cd Length: 106  Bit Score: 109.00  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 141 HMVLSKANSQPSAGRAPISNP-----GMSEAGNFGGNSFMPAN----GLTVAQNQVLNLIK-ACPRPEGLNFQDLKNQLk 210
Cdd:pfam08784   1 HLFLTKGASGSSGGGATTPAVsnggsSMGTQGAYSGGDASVVNanngGLTPLQDQVLNLIKqPPNGNEGVHVDEIAQRL- 79

                          90       100
                  ....*....|....*....|....*..
gi 1370454141 211 HMSVSSIKQAVDFLSNEGHIYSTVDDD 237
Cdd:pfam08784  80 GLPVNDVKQAVDFLSNEGHIYSTIDDD 106
RPA2_DBD_D cd04478
RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding ...
 73-142 4.27e-28

RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B; RPA2 DBD-D is a weak ssDNA-binding domain. RPA2 DBD-D is also involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. N-terminal to human RPA2 DBD-D is a domain containing all the known phosphorylation sites of RPA. Human RPA2 is phosphorylated in a cell cycle dependent manner in response to DNA damage. RPA2 interacts physically with menin; the gene encoding menin is a tumor suppressor gene disrupted in multiple endocrine neoplasia type I. This subfamily also includes RPA2 from Cryptosporidium parvum (CpRPA2). CpRPA2 is an SSB, which can be phosphorylated by DNA-PK in vitro.


Pssm-ID: 239924  Cd Length: 95  Bit Score: 102.68  E-value: 4.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141  73 QVTIVGIIRHAEKAPTNIVYKIDDMTAaPMDVRQWVDTDN--------------------------KKSLVAFKIMPLED 126
Cdd:cd04478     1 QVTLVGVVRNVEEQSTNITYTIDDGTG-TIEVRQWLDDDNddssevepieegtyvrvfgnlksfqgKKSIMAFSIRPVTD 79

                          90
                  ....*....|....*.
gi 1370454141 127 MNEFTTHILEVINAHM 142
Cdd:cd04478    80 FNEVTYHLLEVIYVHL 95
RFA2 COG5235
Single-stranded DNA-binding replication protein A (RPA), medium (30 kD) subunit [DNA ...
 25-242 4.83e-28

Single-stranded DNA-binding replication protein A (RPA), medium (30 kD) subunit [DNA replication, recombination, and repair];


Pssm-ID: 227560 [Multi-domain]  Cd Length: 258  Bit Score: 107.37  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141  25 GGF---GSPaPSQAEKKSRARAQHIVPCTISQLLSATLV--DEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTA 99
Cdd:COG5235    16 GQIfgtGSP-PPMDRSEGGYIVNTLRPVTIKQILSCDQDetDSTFLVDSAEVTNVQFVGVVRNIKTSTTNSMFVIEDGTG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 100 ApMDVRQWVDTDN-------------------------KKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAG 154
Cdd:COG5235    95 S-IEVRFWPGNSYeeeqckdleeqnyvkvngslktfngKRSISASHISAIEDSNEVTYHFLECIYQHLFYTRQLQRPLEE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370454141 155 RAPisNPGMSEAGNFGGNSFMPANGLTVAQNQVLnliKACPRPEGLNFQDLKNQL-KHMSVSSIKQAVDFLSNEGHIYST 233
Cdd:COG5235   174 EVK--NDGQSLFAKLDNDTSSGSSRLQEDILECY---RRNQDENGLHINVVIKMLsQSYSEDETRVNIDVLLRDGHIYPT 248


                  ....*....
gi 1370454141 234 VDDDHFKST 242
Cdd:COG5235   249 VDGNEFKTT 257
 
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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