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Protein

DNA repair protein REV1

Gene

REV1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+2 PublicationsNote: Binds 2 magnesium ions.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei324dCTP2 Publications1
Metal bindingi362Magnesium 1PROSITE-ProRule annotation1 Publication1
Metal bindingi362Magnesium 2PROSITE-ProRule annotation1 Publication1
Metal bindingi363Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation1 Publication1
Binding sitei414dCTP2 Publications1
Metal bindingi467Magnesium 1PROSITE-ProRule annotation1 Publication1
Binding sitei467dCTP2 Publications1
Metal bindingi468Magnesium 1PROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi362 – 366dCTP binding2 Publications5
Nucleotide bindingi402 – 408dCTP binding2 Publications7

GO - Molecular functioni

  • damaged DNA binding Source: InterPro
  • deoxycytidyl transferase activity Source: SGD
  • DNA-directed DNA polymerase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • error-free translesion synthesis Source: SGD
  • error-prone translesion synthesis Source: SGD
Complete GO annotation...

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.
ReactomeiR-SCE-110312. Translesion synthesis by REV1.
R-SCE-110320. Translesion Synthesis by POLH.
R-SCE-5655862. Translesion synthesis by POLK.
R-SCE-5656121. Translesion synthesis by POLI.
R-SCE-5656169. Termination of translesion DNA synthesis.
R-SCE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR346W.
SGDiS000005873. REV1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
  • nucleus Source: UniProtKB-SubCell
  • replication fork Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi193G → R: Loss of activity. 1 Publication1
Mutagenesisi467 – 468DE → AA: Loss of dCTP transferase activity. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001739951 – 985DNA repair protein REV1Add BLAST985

Proteomic databases

MaxQBiP12689.
PRIDEiP12689.

PTM databases

iPTMnetiP12689.

Interactioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei681Interaction with target DNA1
Sitei692Interaction with target DNA1
Sitei694Interaction with target DNA1

Binary interactionsi

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

Protein-protein interaction databases

BioGridi34731. 57 interactors.
DIPiDIP-1000N.
IntActiP12689. 4 interactors.
MINTiMINT-2732340.

Structurei

Secondary structure

1985
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni165 – 168Combined sources4
Beta strandi170 – 173Combined sources4
Helixi181 – 190Combined sources10
Beta strandi194 – 198Combined sources5
Turni202 – 204Combined sources3
Beta strandi207 – 209Combined sources3
Helixi215 – 220Combined sources6
Turni221 – 223Combined sources3
Beta strandi224 – 227Combined sources4
Helixi230 – 238Combined sources9
Helixi244 – 247Combined sources4
Helixi315 – 322Combined sources8
Helixi324 – 342Combined sources19
Turni343 – 345Combined sources3
Beta strandi355 – 363Combined sources9
Turni364 – 367Combined sources4
Helixi368 – 373Combined sources6
Helixi377 – 379Combined sources3
Turni384 – 386Combined sources3
Beta strandi389 – 391Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi401 – 403Combined sources3
Helixi405 – 409Combined sources5
Helixi418 – 422Combined sources5
Beta strandi432 – 434Combined sources3
Helixi438 – 454Combined sources17
Beta strandi459 – 465Combined sources7
Beta strandi468 – 475Combined sources8
Helixi485 – 501Combined sources17
Beta strandi506 – 513Combined sources8
Helixi514 – 524Combined sources11
Helixi534 – 536Combined sources3
Helixi539 – 542Combined sources4
Helixi547 – 549Combined sources3
Helixi555 – 564Combined sources10
Helixi571 – 577Combined sources7
Helixi580 – 587Combined sources8
Helixi591 – 598Combined sources8
Turni599 – 601Combined sources3
Helixi605 – 612Combined sources8
Helixi614 – 618Combined sources5
Beta strandi623 – 627Combined sources5
Helixi636 – 656Combined sources21
Beta strandi659 – 671Combined sources13
Beta strandi687 – 701Combined sources15
Helixi704 – 718Combined sources15
Helixi722 – 724Combined sources3
Beta strandi725 – 737Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12689.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini161 – 249BRCTPROSITE-ProRule annotationAdd BLAST89
Domaini358 – 554UmuCPROSITE-ProRule annotationAdd BLAST197

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni319 – 329Interaction with target DNAAdd BLAST11
Regioni395 – 397Interaction with target DNA3
Regioni554 – 557Interaction with target DNA4
Regioni620 – 628Interaction with target DNA9

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

GeneTreeiENSGT00530000062942.
HOGENOMiHOG000141717.
InParanoidiP12689.
KOiK03515.
OMAiIKNGMWV.
OrthoDBiEOG092C08ZW.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR012112. REV1.
IPR001126. UmuC.
[Graphical view]
PfamiPF16589. BRCT_2. 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

        10         20         30         40         50
MGEHGGLVDL LDSDLEYSIN RETPDKNNCL SQQSVNDSHL TAKTGGLNAR
60 70 80 90 100
SFLSTLSDDS LIEYVNQLSQ TNKNNSNPTA GTLRFTTKNI SCDELHADLG
110 120 130 140 150
GGEDSPIARS VIEIQESDSN GDDVKKNTVY TREAYFHEKA HGQTLQDQIL
160 170 180 190 200
KDQYKDQISS QSSKIFKNCV IYINGYTKPG RLQLHEMIVL HGGKFLHYLS
210 220 230 240 250
SKKTVTHIVA SNLPLKKRIE FANYKVVSPD WIVDSVKEAR LLPWQNYSLT
260 270 280 290 300
SKLDEQQKKL DNCKTVNSIP LPSETSLHKG SKCVGSALLP VEQQSPVNLN
310 320 330 340 350
NLEAKRIVAC DDPDFLTSYF AHSRLHHLSA WKANLKDKFL NENIHKYTKI
360 370 380 390 400
TDKDTYIIFH IDFDCFFATV AYLCRSSSFS ACDFKRDPIV VCHGTKNSDI
410 420 430 440 450
ASCNYVARSY GIKNGMWVSQ AEKMLPNGIK LISLPYTFEQ FQLKSEAFYS
460 470 480 490 500
TLKRLNIFNL ILPISIDEAV CVRIIPDNIH NTNTLNARLC EEIRQEIFQG
510 520 530 540 550
TNGCTVSIGC SDSLVLARLA LKMAKPNGYN ITFKSNLSEE FWSSFKLDDL
560 570 580 590 600
PGVGHSTLSR LESTFDSPHS LNDLRKRYTL DALKASVGSK LGMKIHLALQ
610 620 630 640 650
GQDDEESLKI LYDPKEVLQR KSLSIDINWG IRFKNITQVD LFIERGCQYL
660 670 680 690 700
LEKLNEINKT TSQITLKLMR RCKDAPIEPP KYMGMGRCDS FSRSSRLGIP
710 720 730 740 750
TNEFGIIATE MKSLYRTLGC PPMELRGLAL QFNKLVDVGP DNNQLKLRLP
760 770 780 790 800
FKTIVTNRAF EALPEDVKND INNEFEKRNY KRKESGLTSN SLSSKKKGFA
810 820 830 840 850
ISRLEVNDLP STMEEQFMNE LPTQIRAEVR HDLRIQKKIQ QTKLGNLQEK
860 870 880 890 900
IKRREESLQN EKNHFMGQNS IFQPIKFQNL TRFKKICQLV KQWVAETLGD
910 920 930 940 950
GGPHEKDVKL FVKYLIKLCD SNRVHLVLHL SNLISRELNL CAFLNQDHSG
960 970 980
FQTWERILLN DIIPLLNRNK HTYQTVRKLD MDFEV
Length:985
Mass (Da):112,227
Last modified:November 1, 1997 - v2
Checksum:i330E30A27F8300BE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti646G → S in AAA34967 (PubMed:2492497).Curated1
Sequence conflicti816Q → H in AAA34967 (PubMed:2492497).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34731. 57 interactors.
DIPiDIP-1000N.
IntActiP12689. 4 interactors.
MINTiMINT-2732340.

PTM databases

iPTMnetiP12689.

Proteomic databases

MaxQBiP12689.
PRIDEiP12689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YOR346W.
SGDiS000005873. REV1.

Phylogenomic databases

GeneTreeiENSGT00530000062942.
HOGENOMiHOG000141717.
InParanoidiP12689.
KOiK03515.
OMAiIKNGMWV.
OrthoDBiEOG092C08ZW.

Enzyme and pathway databases

BioCyciYEAST:G3O-33819-MONOMER.
ReactomeiR-SCE-110312. Translesion synthesis by REV1.
R-SCE-110320. Translesion Synthesis by POLH.
R-SCE-5655862. Translesion synthesis by POLK.
R-SCE-5656121. Translesion synthesis by POLI.
R-SCE-5656169. Termination of translesion DNA synthesis.
R-SCE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

EvolutionaryTraceiP12689.
PROiP12689.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR012112. REV1.
IPR001126. UmuC.
[Graphical view]
PfamiPF16589. BRCT_2. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.