REV1_SCHPO
ID REV1_SCHPO Reviewed; 935 AA.
AC O94623;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA repair protein rev1 {ECO:0000250|UniProtKB:P12689};
DE EC=2.7.7.-;
DE AltName: Full=Reversionless protein 1 {ECO:0000250|UniProtKB:P12689};
GN Name=rev1 {ECO:0000312|EMBL:CAA22130.2}; ORFNames=SPBC1347.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA22130.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a
CC dCMP residue from dCTP to the 3'-end of a DNA primer in a template-
CC dependent reaction. May assist in the first step in the bypass of
CC abasic lesions by the insertion of a nucleotide opposite the lesion.
CC Required for normal induction of mutations by physical and chemical
CC agents. Involved in mitochondrial DNA mutagenesis (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC Mitochondrion {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000255}.
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DR EMBL; CU329671; CAA22130.2; -; Genomic_DNA.
DR RefSeq; NP_596693.2; NM_001022616.3.
DR AlphaFoldDB; O94623; -.
DR SMR; O94623; -.
DR BioGRID; 276276; 9.
DR IntAct; O94623; 1.
DR STRING; 4896.SPBC1347.01c.1; -.
DR PaxDb; O94623; -.
DR PRIDE; O94623; -.
DR EnsemblFungi; SPBC1347.01c.1; SPBC1347.01c.1:pep; SPBC1347.01c.
DR GeneID; 2539723; -.
DR KEGG; spo:SPBC1347.01c; -.
DR PomBase; SPBC1347.01c; rev1.
DR VEuPathDB; FungiDB:SPBC1347.01c; -.
DR eggNOG; KOG2093; Eukaryota.
DR HOGENOM; CLU_003901_1_0_1; -.
DR InParanoid; O94623; -.
DR OMA; YERSRLH; -.
DR PhylomeDB; O94623; -.
DR Reactome; R-SPO-110312; Translesion synthesis by REV1.
DR Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR Reactome; R-SPO-5656121; Translesion synthesis by POLI.
DR PRO; PR:O94623; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0017125; F:deoxycytidyl transferase activity; ISO:PomBase.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070987; P:error-free translesion synthesis; IGI:PomBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; IMP:PomBase.
DR GO; GO:0043504; P:mitochondrial DNA repair; IC:PomBase.
DR Gene3D; 1.20.58.1280; -; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR012112; REV1.
DR InterPro; IPR031991; Rev1_C.
DR InterPro; IPR038401; Rev1_C_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF16727; REV1_C; 1.
DR PIRSF; PIRSF036573; REV1; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA synthesis;
KW DNA-binding; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..935
FT /note="DNA repair protein rev1"
FT /id="PRO_0000361684"
FT DOMAIN 59..147
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 279..460
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 162..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..245
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 310..312
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 460..463
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 517..525
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 176..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 283..287
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 317..323
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT SITE 578
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 589
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 591
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 935 AA; 106526 MW; B1A472DDA37085FC CRC64;
MAFNQRKRRR PVGIADFDEA NDEAYESVGF HDYADYFSRK QRKLQNQNAA LYKSIDEDSK
SDLFHGLAIA INGYTKPSYT ELRQMIVSNG GTFIQYVDGK TSISYLVCSF LTPSKARQWK
HQKVVKPEWI VDCIKQKKIL PWINYRTFQA SSAQATLSFV ASKPSQPEGN LEDIQTSSQE
EEHDNEKDKT KESKAKGFLD DLSGLSASSL HNYQLLKNPN VRNSTTQNQD FLENFFSSSR
LHHLSTWKAD FKNEIQAMTT ASEPVRPIMK DKSKKSRFLL HVDFDCFFAS VSTRFSHELR
LKPVAVAHGI KNSEIASCNY EARKFGIKNG MYVGTAKNLC PSLRVVDYDF GAYESVSREF
YTILVNTLHD YIKVISIDEA LLDITSSVSS FQDCFEIAES IRSQVREKTN CEVSVGIGPN
VLLARLALRK AKPHNVYSLS IENVFDVLSP LSVQDLPGVG SSQAQKLFNL YGVRTIGQLQ
RIEKFNLQET FGVNYGLHLY NISRGIDTDI INNETPRRSI SVDVNWGVRF VFQEDGIDFL
KRLLHELLSR MGKCQVLLHQ IQLRILKRAD GAPFSPPKYL GAGEVTSFTK SSTFTSATNS
FDLIWKKVTS MYKTINVDPG DVRGIGLQAL KIIKDNSKIR KDYRSIQSIT SRNKVSLKGA
SVDISSKDKE IISQKKQLSP KLIPSTPYDL PSSSQISSSA LAQLPPSMQS DIQQQLRLQK
RSITEYPSQL DPLFMVELPT PIRNEVNDNH EIAMNKRLSL KSHADNKIDE RGKKKIRQEN
AFDKLLQISK KSKTINKPNV DYLTLKELPK DLQKQILKES NLQKSDLISE VKLEKPHIVT
FQHVQSLEDL RGLLTKWYSK ASKGPNIHDV NYFANYVCRV IREEKNLGKA QMMLKWLYQL
NRKECNKPWE KAIDKIIETV QGECLQRNIP PLMIF
