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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: -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

Miscellaneous

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

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

Keywordsi

Molecular functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair, DNA synthesis
LigandMagnesium, 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP12689
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

Show more details

Protein-protein interaction databases

BioGridi34731, 120 interactors
DIPiDIP-1000N
IntActiP12689, 6 interactors
MINTiP12689
STRINGi4932.YOR346W

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 – 197Combined sources4
Beta strandi202 – 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
Helixi366 – 373Combined sources8
Helixi377 – 379Combined sources3
Turni384 – 386Combined sources3
Beta strandi389 – 391Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi401 – 403Combined sources3
Helixi405 – 409Combined sources5
Helixi418 – 424Combined sources7
Beta strandi432 – 434Combined sources3
Helixi438 – 454Combined sources17
Beta strandi459 – 465Combined sources7
Beta strandi468 – 475Combined sources8
Helixi482 – 500Combined sources19
Beta strandi506 – 513Combined sources8
Helixi514 – 524Combined sources11
Beta strandi529 – 531Combined sources3
Helixi534 – 536Combined sources3
Helixi539 – 542Combined sources4
Helixi547 – 549Combined sources3
Helixi555 – 564Combined sources10
Helixi571 – 577Combined sources7
Helixi580 – 587Combined sources8
Helixi589 – 598Combined sources10
Turni599 – 601Combined sources3
Helixi605 – 612Combined sources8
Helixi614 – 617Combined sources4
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[»]
5UMVX-ray1.75A162-251[»]
5VX7NMR-A162-251[»]
5WM1X-ray1.85A305-738[»]
5WM8X-ray1.92A305-738[»]
5WMBX-ray2.25A305-738[»]
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

Phylogenomic databases

GeneTreeiENSGT00530000062942
HOGENOMiHOG000141717
InParanoidiP12689
KOiK03515
OMAiYGIKNGM
OrthoDBiEOG092C08ZW

Family and domain databases

CDDicd00027 BRCT, 1 hit
Gene3Di3.30.1490.100, 1 hit
3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR036775 DNA_pol_Y-fam_lit_finger_sf
IPR017961 DNA_pol_Y-fam_little_finger
IPR012112 REV1
IPR001126 UmuC
PfamiView protein in Pfam
PF16589 BRCT_2, 1 hit
PF00817 IMS, 1 hit
PF11799 IMS_C, 1 hit
PIRSFiPIRSF036573 REV1, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 1 hit
SUPFAMiSSF100879 SSF100879, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50172 BRCT, 1 hit
PS50173 UMUC, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiREV1_YEAST
AccessioniPrimary (citable) accession number: P12689
Secondary accession number(s): D6W341, Q12323
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: June 20, 2018
This is version 167 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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