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P12689 (REV1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein REV1

EC=2.7.7.-
Alternative name(s):
Reversionless protein 1
Gene names
Name:REV1
Ordered Locus Names:YOR346W
ORF Names:O6339
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length985 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.9

Cofactor

Binds 2 magnesium ions. Ref.10 Ref.11

Subcellular location

Nucleus. Mitochondrion Ref.7 Ref.9.

Miscellaneous

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

Sequence similarities

Belongs to the DNA polymerase type-Y family.

Contains 1 BRCT domain.

Contains 1 umuC domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

REV7P389273EBI-14951,EBI-14960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 985985DNA repair protein REV1
PRO_0000173995

Regions

Domain161 – 24989BRCT
Domain358 – 554197UmuC
Nucleotide binding362 – 3665dCTP binding
Nucleotide binding402 – 4087dCTP binding
Region319 – 32911Interaction with target DNA
Region395 – 3973Interaction with target DNA
Region554 – 5574Interaction with target DNA
Region620 – 6289Interaction with target DNA

Sites

Metal binding3621Magnesium 1
Metal binding3621Magnesium 2
Metal binding3631Magnesium 2; via carbonyl oxygen
Metal binding4671Magnesium 1
Metal binding4681Magnesium 1
Binding site3241dCTP
Binding site4141dCTP
Binding site4671dCTP
Site6811Interaction with target DNA
Site6921Interaction with target DNA
Site6941Interaction with target DNA

Experimental info

Mutagenesis1931G → R: Loss of activity. Ref.1 Ref.6
Mutagenesis467 – 4682DE → AA: Loss of dCTP transferase activity. Ref.6
Sequence conflict6461G → S in AAA34967. Ref.1
Sequence conflict8161Q → H in AAA34967. Ref.1

Secondary structure

......................................................................................... 985
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12689 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 330E30A27F8300BE

FASTA985112,227
        10         20         30         40         50         60 
MGEHGGLVDL LDSDLEYSIN RETPDKNNCL SQQSVNDSHL TAKTGGLNAR SFLSTLSDDS 

        70         80         90        100        110        120 
LIEYVNQLSQ TNKNNSNPTA GTLRFTTKNI SCDELHADLG GGEDSPIARS VIEIQESDSN 

       130        140        150        160        170        180 
GDDVKKNTVY TREAYFHEKA HGQTLQDQIL KDQYKDQISS QSSKIFKNCV IYINGYTKPG 

       190        200        210        220        230        240 
RLQLHEMIVL HGGKFLHYLS SKKTVTHIVA SNLPLKKRIE FANYKVVSPD WIVDSVKEAR 

       250        260        270        280        290        300 
LLPWQNYSLT SKLDEQQKKL DNCKTVNSIP LPSETSLHKG SKCVGSALLP VEQQSPVNLN 

       310        320        330        340        350        360 
NLEAKRIVAC DDPDFLTSYF AHSRLHHLSA WKANLKDKFL NENIHKYTKI TDKDTYIIFH 

       370        380        390        400        410        420 
IDFDCFFATV AYLCRSSSFS ACDFKRDPIV VCHGTKNSDI ASCNYVARSY GIKNGMWVSQ 

       430        440        450        460        470        480 
AEKMLPNGIK LISLPYTFEQ FQLKSEAFYS TLKRLNIFNL ILPISIDEAV CVRIIPDNIH 

       490        500        510        520        530        540 
NTNTLNARLC EEIRQEIFQG TNGCTVSIGC SDSLVLARLA LKMAKPNGYN ITFKSNLSEE 

       550        560        570        580        590        600 
FWSSFKLDDL PGVGHSTLSR LESTFDSPHS LNDLRKRYTL DALKASVGSK LGMKIHLALQ 

       610        620        630        640        650        660 
GQDDEESLKI LYDPKEVLQR KSLSIDINWG IRFKNITQVD LFIERGCQYL LEKLNEINKT 

       670        680        690        700        710        720 
TSQITLKLMR RCKDAPIEPP KYMGMGRCDS FSRSSRLGIP TNEFGIIATE MKSLYRTLGC 

       730        740        750        760        770        780 
PPMELRGLAL QFNKLVDVGP DNNQLKLRLP FKTIVTNRAF EALPEDVKND INNEFEKRNY 

       790        800        810        820        830        840 
KRKESGLTSN SLSSKKKGFA ISRLEVNDLP STMEEQFMNE LPTQIRAEVR HDLRIQKKIQ 

       850        860        870        880        890        900 
QTKLGNLQEK IKRREESLQN EKNHFMGQNS IFQPIKFQNL TRFKKICQLV KQWVAETLGD 

       910        920        930        940        950        960 
GGPHEKDVKL FVKYLIKLCD SNRVHLVLHL SNLISRELNL CAFLNQDHSG FQTWERILLN 

       970        980 
DIIPLLNRNK HTYQTVRKLD MDFEV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22222 Genomic DNA. Translation: AAA34967.1.
X95720 Genomic DNA. Translation: CAA65033.1.
Z75253 Genomic DNA. Translation: CAA99674.1.
BK006948 Genomic DNA. Translation: DAA11107.1.
PIRS67255.
RefSeqNP_014991.1. NM_001183766.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AQ4X-ray2.32A305-738[»]
2M2INMR-A158-251[»]
3BJYX-ray2.41A305-738[»]
3OSPX-ray2.50A305-738[»]
4ID3X-ray1.97A/B159-250[»]
ProteinModelPortalP12689.
SMRP12689. Positions 158-251, 305-738.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34731. 54 interactions.
DIPDIP-1000N.
IntActP12689. 4 interactions.
MINTMINT-2732340.
STRING4932.YOR346W.

Proteomic databases

MaxQBP12689.
PaxDbP12689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR346W; YOR346W; YOR346W.
GeneID854527.
KEGGsce:YOR346W.

Organism-specific databases

CYGDYOR346w.
SGDS000005873. REV1.

Phylogenomic databases

eggNOGCOG0389.
GeneTreeENSGT00530000062942.
HOGENOMHOG000141717.
KOK03515.
OMADCFFATV.
OrthoDBEOG783N3S.

Enzyme and pathway databases

BioCycYEAST:G3O-33819-MONOMER.

Gene expression databases

GenevestigatorP12689.

Family and domain databases

Gene3D3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. 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]
PfamPF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFPIRSF036573. REV1. 1 hit.
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF100879. SSF100879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12689.
NextBio976907.
PROP12689.

Entry information

Entry nameREV1_YEAST
AccessionPrimary (citable) accession number: P12689
Secondary accession number(s): D6W341, Q12323
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references