ID DPOZ_SCHPO Reviewed; 1480 AA.
AC Q9P6L6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 151.
DE RecName: Full=DNA polymerase zeta catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=Protein reversionless 3;
GN Name=rev3; ORFNames=SPAC688.10;
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:CAB90776.1}
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: Nonessential DNA polymerase. Required for DNA damage induced
CC mutagenesis. Involved in DNA repair, mitochondrial DNA repair and
CC translesion synthesis. Has a role in the bypass of abasic (AP) sites
CC (By similarity). {ECO:0000250|UniProtKB:P14284}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000250|UniProtKB:P14284};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Forms DNA polymerase zeta with rev7.
CC {ECO:0000250|UniProtKB:P14284}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000255}.
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DR EMBL; CU329670; CAB90776.1; -; Genomic_DNA.
DR RefSeq; NP_594068.1; NM_001019492.2.
DR AlphaFoldDB; Q9P6L6; -.
DR SMR; Q9P6L6; -.
DR BioGRID; 279780; 29.
DR STRING; 284812.Q9P6L6; -.
DR iPTMnet; Q9P6L6; -.
DR PaxDb; 4896-SPAC688-10-1; -.
DR EnsemblFungi; SPAC688.10.1; SPAC688.10.1:pep; SPAC688.10.
DR GeneID; 2543358; -.
DR KEGG; spo:SPAC688.10; -.
DR PomBase; SPAC688.10; rev3.
DR VEuPathDB; FungiDB:SPAC688.10; -.
DR eggNOG; KOG0968; Eukaryota.
DR HOGENOM; CLU_000203_3_1_1; -.
DR InParanoid; Q9P6L6; -.
DR OMA; RYILNLW; -.
DR PhylomeDB; Q9P6L6; -.
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:Q9P6L6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; NAS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISO:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; ISM: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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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 CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1480
FT /note="DNA polymerase zeta catalytic subunit"
FT /id="PRO_0000361055"
FT ZN_FING 1381..1403
FT /note="CysA-type"
FT REGION 403..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1432..1451
FT /note="CysB motif"
FT COMPBIAS 407..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1432
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1435
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1446
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1480 AA; 168290 MW; 0490869066988AE0 CRC64;
MRFSIEYIDW ELSPCDPAYD FVGKDLPTAN EELTTVPVIR VFGLNEEAET VCCFIHNVFP
YIYVEYSSFA ETLDLEVPDF LSQLQTSINY ALALAARANP ETYKPAVQSV QLVKGIPFYG
YSFCFQKFLK ICLFSPKNRD RLVDLFRQGA ILNKVIQVYE SHLPYLLQFM VDHNLYGCAP
IDLDDSIIKR DDLLSFCNVE VHVSPNAILN ACWLSERNIH TDLYETHASS PNSLLVTSLA
EIWKSEASRR NLTSSDETNS FSKLHQSQFG LKEESSHEPR SSQHWKNEVA MKDLLKNLIK
SKLESSSDVN TPLIFDPWPE LPTIYSAIHT KDYVRPSQND ISVSQISVDE KICTSYESLP
KIQLEQNTAP VIESSFEQLD SELERILGDT LFDSFPYVEP NVDRSKFPKS PLNSSQEVTI
HSSQDRQSPP SSPLKDVPSQ INPFSPSLRL KGGSPITKRE IEFCRDLPNR PTSSEPNQGD
TRKAGKRLKY SRNLDDYHIC TQIPEDYSPK FLSQHESFVY KQQPPSTDDL YGTMKKLKIP
FSIPTNVHYS SEKDIPSYSQ EYLGKSHYPI GVSSRYLPEF QSDGSVSEKV RLNPLKLSNF
HGERTWQYIK PAPLAVDLSN LESKEAVSEE IQSPQRLSRS KVFRKDPYSC VRILALELFC
CSHGGLTPDP TKDSIECCFW AYQEDVNSSM IDRVGFIVVD KSASNSSFGR SFPSCTVLVV
NSELELINEV IGLNRQLDPT IVCGYEVHNS SWGYLIERAS YRFNYDLPEQ LSRLKCTSKA
NFAKKENAWK YTTTSSINIV GRHVLNIWRI LRGEVNLLNY SLENVVLNIF KKQTPYYNQA
DKVHLWQSSR FHEKQILLNY MLNRTRYCLE ILSACAIVTK IREQARIIGI DFMSVISRGS
QFKVESIMFR IAKPENYIFP SPSAKQVAEQ NALEALPLVM EPKSDLYNNP VVVLDFQSLY
PSIIIAYNLC YSTCLGPVKI VNGKVKLGFM FHSSNPNIVN LIKNDVYISP NGYAYVKENV
RKSLLAKMLE ELIETRNMVK RGMKDCDSDY VNKVLNSRQL ALKLIANVTY GYTSASFSGR
MPCSEIADTI VETGREILSY SLEYINTLDF CHAKVVYGDT DSLFVELPGA TKEQAFDIGQ
QLANNITSRF PSPIRLKFEK IYFPCFLLAK KRYVGFKFES VSQKAPIFEA KGIETVRRDG
TPVQQQLLRR CLEILFKTKD LSTVKKEFQN VCYQIMSGNV PVMDFCFSKE VRLEKYKELS
TAPPGAVMAR RLMTKDPRRE PQYGERVPYL IIAAAPGTTL ANRSVAPEEF LSSSFSQLDI
NYYINNSLIP PLDRFLNLLG ASAQSWYHEM PKPRTSLKLT ETVKGGIQKK TLDTFLMEKL
CSSCLKNNIE IIPDKINSLC SDCLKNPCAT ISKAVTQHNA YNKKLSLLFD ICRGCSKLSS
SDPVLCKSNS CKVYYDRAKT ENYAKVQAEM LTKTLGSLDW
//
