GenomeNet

Database: UniProt
Entry: F1M8G6_RAT
LinkDB: F1M8G6_RAT
Original site: F1M8G6_RAT 
ID   F1M8G6_RAT              Unreviewed;      3132 AA.
AC   F1M8G6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=Rev3l {ECO:0000313|Ensembl:ENSRNOP00000054053.2,
GN   ECO:0000313|RGD:1307087};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000054053.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000054053.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000054053.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000054053.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000054053.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
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DR   RefSeq; NP_001077435.1; NM_001083966.1.
DR   SMR; F1M8G6; -.
DR   STRING; 10116.ENSRNOP00000054053; -.
DR   PaxDb; 10116-ENSRNOP00000054053; -.
DR   Ensembl; ENSRNOT00000057227.4; ENSRNOP00000054053.2; ENSRNOG00000000593.8.
DR   GeneID; 309812; -.
DR   KEGG; rno:309812; -.
DR   AGR; RGD:1307087; -.
DR   CTD; 5980; -.
DR   RGD; 1307087; Rev3l.
DR   eggNOG; KOG0968; Eukaryota.
DR   GeneTree; ENSGT00940000156226; -.
DR   HOGENOM; CLU_000203_1_0_1; -.
DR   InParanoid; F1M8G6; -.
DR   OMA; DPTSWIR; -.
DR   OrthoDB; 211439at2759; -.
DR   TreeFam; TF101072; -.
DR   Reactome; R-RNO-110312; Translesion synthesis by REV1.
DR   Reactome; R-RNO-5655862; Translesion synthesis by POLK.
DR   Reactome; R-RNO-5656121; Translesion synthesis by POLI.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000593; Expressed in quadriceps femoris and 20 other cell types or tissues.
DR   ExpressionAtlas; F1M8G6; baseline and differential.
DR   Genevisible; F1M8G6; RN.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; ISO:RGD.
DR   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   CDD; cd22287; REV3L_RBD; 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; IPR032757; DUF4683.
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; 2.
DR   Pfam; PF15735; DUF4683; 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   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          95..187
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          746..1132
FT                   /note="DUF4683"
FT                   /evidence="ECO:0000259|Pfam:PF15735"
FT   DOMAIN          2275..2486
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          2552..3002
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          3044..3111
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          425..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1427..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1536..1614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1840..1867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1957..1978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2089..2136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1059
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1536..1554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1569..1583
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2097..2118
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3132 AA;  351898 MW;  8BACCEAEEF6A1CF1 CRC64;
     MFSVRIVTAD YYMASPLPGL DICQSPLTQH PVKKVPVVRV FGATPAGQKT CLHLHGVFPY
     LYVPYDGYGQ QPERYLSQMA LSIDRALNVA LGNPSSTAQH VFKVSLVSGM PFYGYHEKER
     HFMKIYLYNP AMVKRICELL QSGAIMNKFY QPHEAHIPYL LQLFIDYNLY GMNLINLAAV
     KFRKARRKGD ASHATGLFKP QLSGNSPAGT LFRWEEDEIP SSLLLEGVEP LSTCELEVDA
     VAADILNRLD IEAQIGGNPG LQAIWEDEKQ RRRNRNENSQ ISQPESQDCR LVPATESEKI
     FQKRLQEILK QNDFSVTLSG SVDYSSGSQE FSAELTLHSE ILSPEMLPCS PANMIEVHRD
     NDWSKGNTKH KVEEALINEE AILNLIENSQ TFQPLTQRLS ETPVFMDSSP DESLVHLLAG
     LESDGYQGEK NRMPLPRHTF GESQNPQNSD DEENAPQMEK EEMELSVLMS QRWDSDTEEQ
     CAKKRSLCRN AHRSSTEEDD SSSEEEMEWT DNSLLFANLS IPQLDGTADE NSDNPLNNEN
     SRAHSSVIAT SKLSVRPSVF HKDAATLEPP SSAKITFQCK HTSALSSHGL NKDDLIEGLS
     QPNNTEKGRD SSVTFTKEST YSMKYSGSLS STVHSDNSHK EICKKDKSLP VPSCESSVFD
     YEEDIPSVTR QAPSRKYSNM RKIEKDAPFI HANRHTSEST LGKNSFNFAD LNHSKNKLSS
     EGNERGNSTA LNSVFPSSLA ESCDLLSSSG ENRSVAHSLD SITDESGRSK LKIRYEEFQE
     HKMERPSLSQ QAAHYMFFPS VVLSNCLTRP QKLSPVTYKL QPGSKTSRLK LNKKKLISLQ
     ETSTKSSETG AAKDSCTHNH PYSGTPEKES GLSSDLIKAT HGTFENKTPT EHFIDCHFGD
     GSLETEQSFG LYGNKYTLRA KRKVNYETED SESSFVTHNS KISLPHPMEI GENLDGTLKS
     RKRRKMSKKL PPVIIKYIII NRFRGRKNML VKLGKIDSKE KQVILTEEKM ELYKKLAPLK
     DFWPKVPDSP ATKYPIYPLT PKKSHRRKSK HKSAKRKPGK QHRASSENIK RTLSFRKKRT
     HAVLSPPSPS YIAETEDCDL NYSDVMSKLG FLSERSTSPV NSSPPRCWSP TDPRAEEIMA
     AAEKESVLFK GPNVCNTKTV SPRVGKASRA RAQVKKSKAR LAKSSVVTNK RNKRNQTNQL
     VDNGKKKPRA KQKQRANEKG ISRKPVIPTD ETTKPPSEAE LTPSQRSVPE LTSSSGIHTL
     SKQKEMTQTG PAMDHPLPPC QPTGINAQQR LSNCFSSFLE SRKSVQFPTF PSSRGDSRSS
     VYSSIGPGVS KVNTQRSHSQ SAMFTRKETT LIQKSIFDLS NHLSQVAQST QLCSGIISPK
     TEESSNTQKN CGSSIGKLNE YRSSLESKPE KVCAPNFLHC RDSQQQTVNV SEQSKPSETC
     SPGNAASEES QTPNCFVTSL RSPIKQITWE QRQRGCILEM SSFKPEKVKQ RSLSEAISQT
     KALSQCKNQN VSTPSVFGEG QSGLAVLKEL LQKRQQKAQT TNVQDSASSH QPDKDISVSA
     EHKKTNKRTR AVASPRKPRA PRRTKPKEQT PRRLKVDPLN LQTSGHLDNS LSDDSPILFS
     DPGFESCYSL EDSLSPEHNY NFDINTIGQT GFCSLYSGSQ FVPADQNLPQ KFLSDAVQDL
     FPGQAIEKNE LLSHDRQSCT EEKHHVSDSG PWVRASTLNP ELFEKVGIDN NENHRHSQWK
     TSFHPLTSHS NSIMESFCVQ QAESCLPEKS RLNRSSVSKE VFLSLPQASS SDWIQGHNGK
     EIEQSLDSAN TSFTTVLSSP DGELVDAASE DLELYVSRNN DVLTPTPDSS PRSTSSPLQS
     KNGSFTPRTA HILKPLMSPP SREEIVATLL DHDLSEAIYQ EPFCSNPSDV PEKPREIGGR
     LLMVETRLPN DLIEFEGDFS LEGLRLWKTA FSAMTQNPRP GSPLRNGPAV VNKESSNSHK
     TVEDKKIVIM PCRYAPSRQL VQAWLQAKEE YVRSKRLPRT ESTPVIKSAD NVSPSLNPGD
     TRAVAPQMDT CPHTLSSTAH AKEEVCQSQI ALQTSRTGCG QTVSASQTLL PAASAAVPEE
     EEEEEEEEEE EEEDENGYVS YSSPDSPGIP PWQQAASPDF RALNGEHRCS SPVEELCSRA
     VENFLKPIKD GIQKASCCES QVISPIHART RTEKCEPLCL HSTPVMPRKF LEKLPEATGL
     SPLSVEPKTQ KLYNKKGSDT DHLRRVLLTT QVENQFAAVN TPKKETSQID GPSLNNTYGF
     KVSIQNLQEA KALHEIQNLT LISVELHART RRDLQPDPEF DPICALFYCI SSDTPLPDTE
     KTELTGVIVI DKDKTVTHQD IRCQTPLLIR SGVTGLEVTY AADEKALFQE VTNIMKRYDP
     DILLGYEIQM HSWGYLLQRA AALSVDLCQM ISRVPDDKIE NRFAAERDDY GSDTMSEINI
     VGRITLNLWR IMRNEVALTN YTFENVSFHV LHQRFPLFTF RVLSDWFDNK TDLYRWKMVD
     HYVSRVRGNL QMLEQLDLIG KTSEMARLFG IQFLHVLTRG SQYRVESMML RIAKPMNYIP
     VTPSVQQRSQ MRAPQCVPLI MEPESRFYSN SVLVLDFQSL YPSIVIAYNY CFSTCLGHIE
     NLGKYDEFKF GCTSLRVPPD LLYQIRHDIT VSPNGVAFVK PSVRKGVLPR MLEEILKTRF
     MVKQSMKAYR QDRALSRMLN ARQLGLKLIA NVTFGYTSAN FSGRMPCIEV GDSIVHKARE
     TLERAIKLVN DTKKWGARVV YGDTDSMFVL LKGATKEQSF KIGQEIAEAV TATNPKPVKL
     KFEKVYLPCV LQTKKRYVGY MYETLDQKDP VFDAKGIETV RRDSCPAVSK ILERSLKLLF
     ETRDISLIKQ YVQRQCMKLV EGKASIQDFI FAKEYRGSFS YRPGACVPAL ELTRKMLAYD
     RRSEPRVGER VPYVIVYGTP GLPLIQLIRR PAEVLQDPTL RLNATYYITK QILPPLARIF
     SLIGIDVFSW YQELPRIQKA TSSSRSDLEG RKGTISQYFT TLHCPVCDGL TQHGICSQCR
     SQPQHVAIIL NQEIRELERQ QEQLVKICRN CTGSFDRHIP CVSLNCPVLF KLSRVNRELS
     KAPYLRQLLD QF
//
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