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P12689

- REV1_YEAST

UniProt

P12689 - REV1_YEAST

Protein

DNA repair protein REV1

Gene

REV1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.3 Publications

    Cofactori

    Binds 2 magnesium ions.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei324 – 3241dCTP2 Publications
    Metal bindingi362 – 3621Magnesium 11 PublicationPROSITE-ProRule annotation
    Metal bindingi362 – 3621Magnesium 21 PublicationPROSITE-ProRule annotation
    Metal bindingi363 – 3631Magnesium 2; via carbonyl oxygen1 PublicationPROSITE-ProRule annotation
    Binding sitei414 – 4141dCTP2 Publications
    Metal bindingi467 – 4671Magnesium 11 PublicationPROSITE-ProRule annotation
    Binding sitei467 – 4671dCTP2 Publications
    Metal bindingi468 – 4681Magnesium 11 PublicationPROSITE-ProRule annotation
    Sitei681 – 6811Interaction with target DNA
    Sitei692 – 6921Interaction with target DNA
    Sitei694 – 6941Interaction with target DNA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi362 – 3665dCTP binding2 Publications
    Nucleotide bindingi402 – 4087dCTP binding2 Publications

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. deoxycytidyl transferase activity Source: SGD
    3. DNA-directed DNA polymerase activity Source: SGD
    4. magnesium ion binding Source: InterPro
    5. protein binding Source: IntAct

    GO - Biological processi

    1. DNA-dependent DNA replication Source: GOC
    2. error-free translesion synthesis Source: SGD
    3. error-prone translesion synthesis Source: SGD

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA synthesis

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33819-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein REV1 (EC:2.7.7.-)
    Alternative name(s):
    Reversionless protein 1
    Gene namesi
    Name:REV1
    Ordered Locus Names:YOR346W
    ORF Names:O6339
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR346w.
    SGDiS000005873. REV1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: SGD
    2. nucleus Source: UniProtKB-SubCell
    3. replication fork Source: SGD

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi193 – 1931G → R: Loss of activity. 2 Publications
    Mutagenesisi467 – 4682DE → AA: Loss of dCTP transferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 985985DNA repair protein REV1PRO_0000173995Add
    BLAST

    Proteomic databases

    MaxQBiP12689.
    PaxDbiP12689.

    Expressioni

    Gene expression databases

    GenevestigatoriP12689.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    REV7P389273EBI-14951,EBI-14960

    Protein-protein interaction databases

    BioGridi34731. 55 interactions.
    DIPiDIP-1000N.
    IntActiP12689. 4 interactions.
    MINTiMINT-2732340.
    STRINGi4932.YOR346W.

    Structurei

    Secondary structure

    1
    985
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni165 – 1684
    Beta strandi170 – 1734
    Helixi181 – 19010
    Beta strandi194 – 1985
    Turni202 – 2043
    Beta strandi207 – 2093
    Helixi215 – 2206
    Turni221 – 2233
    Beta strandi224 – 2274
    Helixi230 – 2389
    Helixi244 – 2474
    Helixi315 – 3228
    Helixi324 – 34219
    Turni343 – 3453
    Beta strandi355 – 3639
    Turni364 – 3674
    Helixi368 – 3736
    Helixi377 – 3793
    Turni384 – 3863
    Beta strandi389 – 3913
    Beta strandi395 – 3973
    Beta strandi401 – 4033
    Helixi405 – 4095
    Helixi418 – 4225
    Beta strandi432 – 4343
    Helixi438 – 45417
    Beta strandi459 – 4657
    Beta strandi468 – 4758
    Helixi485 – 50117
    Beta strandi506 – 5138
    Helixi514 – 52411
    Helixi534 – 5363
    Helixi539 – 5424
    Helixi547 – 5493
    Helixi555 – 56410
    Helixi571 – 5777
    Helixi580 – 5878
    Helixi591 – 5988
    Turni599 – 6013
    Helixi605 – 6128
    Helixi614 – 6185
    Beta strandi623 – 6275
    Helixi636 – 65621
    Beta strandi659 – 67113
    Beta strandi687 – 70115
    Helixi704 – 71815
    Helixi722 – 7243
    Beta strandi725 – 73713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AQ4X-ray2.32A305-738[»]
    2M2INMR-A158-251[»]
    3BJYX-ray2.41A305-738[»]
    3OSPX-ray2.50A305-738[»]
    4ID3X-ray1.97A/B159-250[»]
    ProteinModelPortaliP12689.
    SMRiP12689. Positions 158-251, 305-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12689.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini161 – 24989BRCTPROSITE-ProRule annotationAdd
    BLAST
    Domaini358 – 554197UmuCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni319 – 32911Interaction with target DNAAdd
    BLAST
    Regioni395 – 3973Interaction with target DNA
    Regioni554 – 5574Interaction with target DNA
    Regioni620 – 6289Interaction with target DNA

    Sequence similaritiesi

    Belongs to the DNA polymerase type-Y family.Curated
    Contains 1 BRCT domain.PROSITE-ProRule annotation
    Contains 1 umuC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0389.
    GeneTreeiENSGT00530000062942.
    HOGENOMiHOG000141717.
    KOiK03515.
    OMAiDCFFATV.
    OrthoDBiEOG783N3S.

    Family and domain databases

    Gene3Di3.30.1490.100. 1 hit.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR017961. DNA_pol_Y-fam_little_finger.
    IPR001126. DNA_repair_prot_UmuC-like.
    IPR017963. DNA_repair_prot_UmuC-like_N.
    IPR012112. REV1.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF00817. IMS. 1 hit.
    PF11799. IMS_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036573. REV1. 1 hit.
    SMARTiSM00292. BRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF100879. SSF100879. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS50173. UMUC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P12689-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGEHGGLVDL LDSDLEYSIN RETPDKNNCL SQQSVNDSHL TAKTGGLNAR    50
    SFLSTLSDDS LIEYVNQLSQ TNKNNSNPTA GTLRFTTKNI SCDELHADLG 100
    GGEDSPIARS VIEIQESDSN GDDVKKNTVY TREAYFHEKA HGQTLQDQIL 150
    KDQYKDQISS QSSKIFKNCV IYINGYTKPG RLQLHEMIVL HGGKFLHYLS 200
    SKKTVTHIVA SNLPLKKRIE FANYKVVSPD WIVDSVKEAR LLPWQNYSLT 250
    SKLDEQQKKL DNCKTVNSIP LPSETSLHKG SKCVGSALLP VEQQSPVNLN 300
    NLEAKRIVAC DDPDFLTSYF AHSRLHHLSA WKANLKDKFL NENIHKYTKI 350
    TDKDTYIIFH IDFDCFFATV AYLCRSSSFS ACDFKRDPIV VCHGTKNSDI 400
    ASCNYVARSY GIKNGMWVSQ AEKMLPNGIK LISLPYTFEQ FQLKSEAFYS 450
    TLKRLNIFNL ILPISIDEAV CVRIIPDNIH NTNTLNARLC EEIRQEIFQG 500
    TNGCTVSIGC SDSLVLARLA LKMAKPNGYN ITFKSNLSEE FWSSFKLDDL 550
    PGVGHSTLSR LESTFDSPHS LNDLRKRYTL DALKASVGSK LGMKIHLALQ 600
    GQDDEESLKI LYDPKEVLQR KSLSIDINWG IRFKNITQVD LFIERGCQYL 650
    LEKLNEINKT TSQITLKLMR RCKDAPIEPP KYMGMGRCDS FSRSSRLGIP 700
    TNEFGIIATE MKSLYRTLGC PPMELRGLAL QFNKLVDVGP DNNQLKLRLP 750
    FKTIVTNRAF EALPEDVKND INNEFEKRNY KRKESGLTSN SLSSKKKGFA 800
    ISRLEVNDLP STMEEQFMNE LPTQIRAEVR HDLRIQKKIQ QTKLGNLQEK 850
    IKRREESLQN EKNHFMGQNS IFQPIKFQNL TRFKKICQLV KQWVAETLGD 900
    GGPHEKDVKL FVKYLIKLCD SNRVHLVLHL SNLISRELNL CAFLNQDHSG 950
    FQTWERILLN DIIPLLNRNK HTYQTVRKLD MDFEV 985
    Length:985
    Mass (Da):112,227
    Last modified:November 1, 1997 - v2
    Checksum:i330E30A27F8300BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti646 – 6461G → S in AAA34967. (PubMed:2492497)Curated
    Sequence conflicti816 – 8161Q → H in AAA34967. (PubMed:2492497)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22222 Genomic DNA. Translation: AAA34967.1.
    X95720 Genomic DNA. Translation: CAA65033.1.
    Z75253 Genomic DNA. Translation: CAA99674.1.
    BK006948 Genomic DNA. Translation: DAA11107.1.
    PIRiS67255.
    RefSeqiNP_014991.1. NM_001183766.1.

    Genome annotation databases

    EnsemblFungiiYOR346W; YOR346W; YOR346W.
    GeneIDi854527.
    KEGGisce:YOR346W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22222 Genomic DNA. Translation: AAA34967.1 .
    X95720 Genomic DNA. Translation: CAA65033.1 .
    Z75253 Genomic DNA. Translation: CAA99674.1 .
    BK006948 Genomic DNA. Translation: DAA11107.1 .
    PIRi S67255.
    RefSeqi NP_014991.1. NM_001183766.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AQ4 X-ray 2.32 A 305-738 [» ]
    2M2I NMR - A 158-251 [» ]
    3BJY X-ray 2.41 A 305-738 [» ]
    3OSP X-ray 2.50 A 305-738 [» ]
    4ID3 X-ray 1.97 A/B 159-250 [» ]
    ProteinModelPortali P12689.
    SMRi P12689. Positions 158-251, 305-738.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34731. 55 interactions.
    DIPi DIP-1000N.
    IntActi P12689. 4 interactions.
    MINTi MINT-2732340.
    STRINGi 4932.YOR346W.

    Proteomic databases

    MaxQBi P12689.
    PaxDbi P12689.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR346W ; YOR346W ; YOR346W .
    GeneIDi 854527.
    KEGGi sce:YOR346W.

    Organism-specific databases

    CYGDi YOR346w.
    SGDi S000005873. REV1.

    Phylogenomic databases

    eggNOGi COG0389.
    GeneTreei ENSGT00530000062942.
    HOGENOMi HOG000141717.
    KOi K03515.
    OMAi DCFFATV.
    OrthoDBi EOG783N3S.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33819-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P12689.
    NextBioi 976907.
    PROi P12689.

    Gene expression databases

    Genevestigatori P12689.

    Family and domain databases

    Gene3Di 3.30.1490.100. 1 hit.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR017961. DNA_pol_Y-fam_little_finger.
    IPR001126. DNA_repair_prot_UmuC-like.
    IPR017963. DNA_repair_prot_UmuC-like_N.
    IPR012112. REV1.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF00817. IMS. 1 hit.
    PF11799. IMS_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036573. REV1. 1 hit.
    SMARTi SM00292. BRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100879. SSF100879. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS50173. UMUC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The REV1 gene of Saccharomyces cerevisiae: isolation, sequence, and functional analysis."
      Larimer F.W., Perry J.R., Hardigree A.A.
      J. Bacteriol. 171:230-237(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-193.
    2. "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast chromosome XV reveals 18 open reading frames including a new pyruvate kinase and three homologues to chromosome I genes."
      Purnelle B., Goffeau A.
      Yeast 12:1475-1481(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 90843 / S288c / FY73.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Deoxycytidyl transferase activity of yeast REV1 protein."
      Nelson J.R., Lawrence C.W., Hinkle D.C.
      Nature 382:729-731(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Roles of yeast DNA polymerases delta and zeta and of Rev1 in the bypass of abasic sites."
      Haracska L., Unk I., Johnson R.E., Johansson E., Burgers P.M.J., Prakash S., Prakash L.
      Genes Dev. 15:945-954(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 467-ASP-GLU-468.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Saccharomyces cerevisiae polymerase zeta functions in mitochondria."
      Zhang H., Chatterjee A., Singh K.K.
      Genetics 172:2683-2688(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Rev1 employs a novel mechanism of DNA synthesis using a protein template."
      Nair D.T., Johnson R.E., Prakash L., Prakash S., Aggarwal A.K.
      Science 309:2219-2222(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 305-738 IN COMPLEX WITH MAGNESIUM IONS; DNA AND DCTP, COFACTOR.
    11. "Protein-template-directed synthesis across an acrolein-derived DNA adduct by yeast Rev1 DNA polymerase."
      Nair D.T., Johnson R.E., Prakash L., Prakash S., Aggarwal A.K.
      Structure 16:239-245(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 305-738 IN COMPLEX WITH MAGNESIUM; DCTP AND TARGET DNA, COFACTOR.

    Entry informationi

    Entry nameiREV1_YEAST
    AccessioniPrimary (citable) accession number: P12689
    Secondary accession number(s): D6W341, Q12323
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 521 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3