ID   REV3_ARATH              Reviewed;        1890 AA.
AC   Q766Z3; O64795; Q9CAG6;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=DNA polymerase zeta catalytic subunit;
DE            EC=2.7.7.7;
DE   AltName: Full=Protein reversionless 3-like;
DE            Short=AtREV3;
GN   Name=REV3; OrderedLocusNames=At1g67500; ORFNames=F12B7.5, T1F15.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=12953110; DOI=10.1105/tpc.012369;
RA   Sakamoto A., Vo L.T., Hase Y., Shikazono N., Matsunaga T., Tanaka A.;
RT   "Disruption of the AtREV3 gene causes hypersensitivity to ultraviolet B
RT   light and gamma-rays in Arabidopsis: implication of the presence of a
RT   translesion synthesis mechanism in plants.";
RL   Plant Cell 15:2042-2057(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION.
RX   PubMed=15908599; DOI=10.1104/pp.105.060236;
RA   Takahashi S., Sakamoto A., Sato S., Kato T., Tabata S., Tanaka A.;
RT   "Roles of Arabidopsis AtREV1 and AtREV7 in translesion synthesis.";
RL   Plant Physiol. 138:870-881(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=21030509; DOI=10.1104/pp.110.166082;
RA   Nakagawa M., Takahashi S., Tanaka A., Narumi I., Sakamoto A.N.;
RT   "Role of AtPolzeta, AtRev1, and AtPoleta in UV light-induced mutagenesis in
RT   Arabidopsis.";
RL   Plant Physiol. 155:414-420(2011).
RN   [6]
RP   FUNCTION.
RX   PubMed=21549648; DOI=10.1016/j.dnarep.2011.04.009;
RA   Wang S., Wen R., Shi X., Lambrecht A., Wang H., Xiao W.;
RT   "RAD5a and REV3 function in two alternative pathways of DNA-damage
RT   tolerance in Arabidopsis.";
RL   DNA Repair 10:620-628(2011).
CC   -!- FUNCTION: Catalytic subunit of the error prone DNA polymerase zeta.
CC       Involved in damage-tolerance mechanisms through translesion DNA
CC       synthesis. {ECO:0000269|PubMed:12953110, ECO:0000269|PubMed:15908599,
CC       ECO:0000269|PubMed:21030509, ECO:0000269|PubMed:21549648}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- SUBUNIT: Forms DNA polymerase zeta with REV7. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q766Z3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC       {ECO:0000269|PubMed:12953110}.
CC   -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC       formation of polymerase complexes. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants are hypersensitive to UV-B light and
CC       gamma rays. {ECO:0000269|PubMed:12953110}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC18785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB114052; BAC82450.1; -; mRNA.
DR   EMBL; AC004393; AAC18785.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011020; AAG52299.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34655.1; -; Genomic_DNA.
DR   PIR; D96698; D96698.
DR   PIR; T02155; T02155.
DR   RefSeq; NP_176917.2; NM_105417.4. [Q766Z3-1]
DR   AlphaFoldDB; Q766Z3; -.
DR   SMR; Q766Z3; -.
DR   STRING; 3702.Q766Z3; -.
DR   iPTMnet; Q766Z3; -.
DR   PaxDb; 3702-AT1G67500-2; -.
DR   ProteomicsDB; 236920; -. [Q766Z3-1]
DR   EnsemblPlants; AT1G67500.1; AT1G67500.1; AT1G67500. [Q766Z3-1]
DR   GeneID; 843071; -.
DR   Gramene; AT1G67500.1; AT1G67500.1; AT1G67500. [Q766Z3-1]
DR   KEGG; ath:AT1G67500; -.
DR   Araport; AT1G67500; -.
DR   TAIR; AT1G67500; REV3.
DR   eggNOG; KOG0968; Eukaryota.
DR   HOGENOM; CLU_000203_3_0_1; -.
DR   InParanoid; Q766Z3; -.
DR   PhylomeDB; Q766Z3; -.
DR   PRO; PR:Q766Z3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q766Z3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0071494; P:cellular response to UV-C; IMP:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IMP:UniProtKB.
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:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
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; 2.
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.
DR   Genevisible; Q766Z3; AT.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Alternative splicing; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1890
FT                   /note="DNA polymerase zeta catalytic subunit"
FT                   /id="PRO_0000424418"
FT   ZN_FING         1789..1806
FT                   /note="CysA-type"
FT                   /evidence="ECO:0000250"
FT   REGION          508..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1835..1856
FT                   /note="CysB motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        508..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..941
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1789
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1792
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1803
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1806
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1835
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         1838
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         1851
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         1856
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1890 AA;  210848 MW;  7E3E5BF3C140C105 CRC64;
     MADSQSGSNV FSLRIVSIDY YMASPIPGYN ICYSSFQGSE VNEVPVIRIY GSTPAGQKTC
     LHIHRALPYL YIPCSEIPLE HHKGVDGSTL ALSLELEKAL KLKGNAASKR QHIHDCEIVR
     AKKFYGYHST EEAFVKIYLS YHPPDVARAA SLLLAGAVLG KSLQPYESHI PFILQFLVDY
     NLYGMGHVHI SKMKFRSPVP HHFRPRRFDL DDCPGQRIDE VAITKANSSA AASVSFPVWS
     LSTIPGQWMW NLSEESDTPL SQSQHRHQHH YRRQSLCELE GDATSSDILN QQFKMYNSLS
     QAQSDTNMVQ SLVAIWEEEY ERTGVHDAPI PPDPGKPSAA DVLQTMSDYV GFGNMLKEML
     NKVELSPPGM KPTAVSSAGP DMHAKPEITD LQALNHMVGT CSEFPASEQL SPLGEKSEEA
     SMENDEYMKT PTDRDTPAQI QDAEALGLFK WFASSQAAED INSDDEILRE TILSPLLPLA
     SINKVLEMAS TDYVSQSQKE CQDILDSQEN LPDFGSSTKR ALPSNPDSQN LRTSSDKQSL
     EIEVASDVPD SSTSNGASEN SFRRYRKSDL HTSEVMEYKN RSFSKSNKPS NSVWGPLPFT
     LTKNLQKDFD STNASDKLGL TKISSYPMNE MTDNYIVPVK EHQADVCNTI DRNVLAGCSL
     RDLMRKKRLC HGESPVSQHM KSRKVRDSRH GEKNECTLRC EAKKQGPALS AEFSEFVCGD
     TPNLSPIDSG NCECNISTES SELHSVDRCS AKETASQNSD EVLRNLSSTT VPFGKDPQTV
     ESGTLVSSNI HVGIEIDSVQ KSGREQESTA NETDETGRLI CLTLSKKPPS LDCLSAGLQD
     SAHSHEIHAR EKQHDEYEGN SNDIPFFPLE DNKEEKKHFF QGTSLGIPLH HLNDGSNLYL
     LTPAFSPPSV DSVLQWISND KGDSNIDSEK QPLRDNHNDR GASFTDLASA SNVVSVSEHV
     EQHNNLFVNS ESNAYTESEI DLKPKGTFLN LNLQASVSQE LSQISGPDGK SGPTPLSQMG
     FRDPASMGAG QQLTILSIEV HAESRGDLRP DPRFDSVNVI ALVVQNDDSF VAEVFVLLFS
     PDSIDQRNVD GLSGCKLSVF LEERQLFRYF IETLCKWDPD VLLGWDIQGG SIGFLAERAA
     QLGIRFLNNI SRTPSPTTTN NSDNKRKLGN NLLPDPLVAN PAQVEEVVIE DEWGRTHASG
     VHVGGRIVLN AWRLIRGEVK LNMYTIEAVS EAVLRQKVPS IPYKVLTEWF SSGPAGARYR
     CIEYVIRRAN LNLEIMSQLD MINRTSELAR VFGIDFFSVL SRGSQYRVES MLLRLAHTQN
     YLAISPGNQQ VASQPAMECV PLVMEPESAF YDDPVIVLDF QSLYPSMIIA YNLCFSTCLG
     KLAHLKMNTL GVSSYSLDLD VLQDLNQILQ TPNSVMYVPP EVRRGILPRL LEEILSTRIM
     VKKAMKKLTP SEAVLHRIFN ARQLALKLIA NVTYGYTAAG FSGRMPCAEL ADSIVQCGRS
     TLEKAISFVN ANDNWNARVV YGDTDSMFVL LKGRTVKEAF VVGQEIASAI TEMNPHPVTL
     KMEKVYHPCF LLTKKRYVGY SYESPNQREP IFDAKGIETV RRDTCEAVAK TMEQSLRLFF
     EQKNISKVKS YLYRQWKRIL SGRVSLQDFI FAKEVRLGTY STRDSSLLPP AAIVATKSMK
     ADPRTEPRYA ERVPYVVIHG EPGARLVDMV VDPLVLLDVD TPYRLNDLYY INKQIIPALQ
     RVFGLVGADL NQWFLEMPRL TRSSLGQRPL NSKNSHKTRI DYFYLSKHCI LCGEVVQESA
     QLCNRCLQNK SAAAATIVWK TSKLEREMQH LATICRHCGG GDWVVQSGVK CNSLACSVFY
     ERRKVQKELR GLSSIATESE LYPKCMAEWF
//