P12689 (REV1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	985 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA synthesis
Cellular component	Mitochondrion Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW error-free translesion synthesis Inferred from direct assay Ref.5. Source: SGD error-prone translesion synthesis Inferred from direct assay Ref.5. Source: SGD
Cellular_component	mitochondrion Inferred from direct assay Ref.9. Source: SGD nucleus Inferred from direct assay PubMed 22842922. Source: SGD replication fork Inferred from physical interaction PubMed 17517887. Source: SGD
Molecular_function	DNA-directed DNA polymerase activity Inferred from direct assay Ref.5. Source: SGD damaged DNA binding Inferred from electronic annotation. Source: InterPro deoxycytidyl transferase activity Inferred from direct assay Ref.5. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
REV7	P38927	3	EBI-14951,EBI-14960

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 985

985

DNA repair protein REV1

PRO_0000173995

Regions

Domain

161 – 249

89

BRCT

Domain

358 – 554

197

UmuC

Nucleotide binding

362 – 366

5

dCTP binding

Nucleotide binding

402 – 408

7

dCTP binding

Region

319 – 329

11

Interaction with target DNA

Region

395 – 397

3

Interaction with target DNA

Region

554 – 557

4

Interaction with target DNA

Region

620 – 628

9

Interaction with target DNA

Sites

Metal binding

362

1

Magnesium 1

Metal binding

362

1

Magnesium 2

Metal binding

363

1

Magnesium 2; via carbonyl oxygen

Metal binding

467

1

Magnesium 1

Metal binding

468

1

Magnesium 1

Binding site

324

1

dCTP

Binding site

414

1

dCTP

Binding site

467

1

dCTP

Site

681

1

Interaction with target DNA

Site

692

1

Interaction with target DNA

Site

694

1

Interaction with target DNA

Experimental info

Mutagenesis

193

1

G → R: Loss of activity. Ref.1 Ref.6

Mutagenesis

467 – 468

2

DE → AA: Loss of dCTP transferase activity. Ref.6

Sequence conflict

646

1

G → S in AAA34967. Ref.1

Sequence conflict

816

1

Q → H in AAA34967. Ref.1

Secondary structure

1

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985

Helix Strand Turn

Details...

Turn

165 – 168

4

Beta strand

170 – 173

4

Helix

181 – 190

10

Beta strand

194 – 198

5

Turn

202 – 204

3

Beta strand

207 – 209

3

Helix

215 – 220

6

Turn

221 – 223

3

Beta strand

224 – 227

4

Helix

230 – 238

9

Helix

244 – 247

4

Helix

315 – 322

8

Helix

324 – 342

19

Turn

343 – 345

3

Beta strand

355 – 363

9

Turn

364 – 367

4

Helix

368 – 373

6

Helix

377 – 379

3

Turn

384 – 386

3

Beta strand

389 – 391

3

Beta strand

395 – 397

3

Beta strand

401 – 403

3

Helix

405 – 409

5

Helix

418 – 422

5

Beta strand

432 – 434

3

Helix

438 – 454

17

Beta strand

459 – 465

7

Beta strand

468 – 475

8

Helix

485 – 501

17

Beta strand

506 – 513

8

Helix

514 – 524

11

Helix

534 – 536

3

Helix

539 – 542

4

Helix

547 – 549

3

Helix

555 – 564

10

Helix

571 – 577

7

Helix

580 – 587

8

Helix

591 – 598

8

Turn

599 – 601

3

Helix

605 – 612

8

Helix

614 – 618

5

Beta strand

623 – 627

5

Helix

636 – 656

21

Beta strand

659 – 671

13

Beta strand

687 – 701

15

Helix

704 – 718

15

Helix

722 – 724

3

Beta strand

725 – 737

13

Sequences

	Sequence		Length	Mass (Da)
	P12689 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 330E30A27F8300BE	FASTA	985	112,227
	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

References

	« Hide 'large scale' referencesShow '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. , 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 90843 / S288c / FY73.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.

PIR

S67255.

RefSeq

NP_014991.1. NM_001183766.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P12689.

SMR

P12689. Positions 164-250, 305-738.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1000N.

IntAct

P12689. 4 interactions.

MINT

MINT-2732340.

STRING

4932.YOR346W.

Proteomic databases

PaxDb

P12689.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR346W; YOR346W; YOR346W.

GeneID

854527.

KEGG

sce:YOR346W.

Organism-specific databases

CYGD

YOR346w.

SGD

S000005873. REV1.

Phylogenomic databases

eggNOG

COG0389.

GeneTree

ENSGT00530000062942.

HOGENOM

HOG000141717.

KO

K03515.

OMA

FHIDFDC.

OrthoDB

EOG49PF6V.

Gene expression databases

Genevestigator

P12689.

GermOnline

YOR346W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.1490.100. 1 hit.

InterPro

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]

Pfam

PF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]

PIRSF

PIRSF036573. REV1. 1 hit.

SMART

SM00292. BRCT. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF100879. DNA_pol_Y-fam_little_finger. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12689.

NextBio

976907.

Entry information

Entry name

REV1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program