ID F4HTM5_ARATH Unreviewed; 1915 AA.
AC F4HTM5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 2.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=REV3 {ECO:0000313|EMBL:AEE34656.2, ECO:0000313|TAIR:AT1G67500};
GN Synonyms=ATREV3 {ECO:0000313|EMBL:AEE34656.2}, recovery protein 3
GN {ECO:0000313|EMBL:AEE34656.2};
GN OrderedLocusNames=At1g67500 {ECO:0000313|Araport:AT1G67500,
GN ECO:0000313|EMBL:AEE34656.2};
GN ORFNames=T1F15.3 {ECO:0000313|EMBL:AEE34656.2}, T1F15_3
GN {ECO:0000313|EMBL:AEE34656.2};
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 {ECO:0000313|EMBL:AEE34656.2, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AEE34656.2, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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., 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., 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 [2] {ECO:0000313|EMBL:AEE34656.2}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEE34656.2}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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:0000256|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002684; AEE34656.2; -; Genomic_DNA.
DR EMBL; CP002684; ANM57916.1; -; Genomic_DNA.
DR RefSeq; NP_001319333.1; NM_001334301.1.
DR RefSeq; NP_001320392.1; NM_001334306.1.
DR SMR; F4HTM5; -.
DR ProteomicsDB; 181794; -.
DR EnsemblPlants; AT1G67500.2; AT1G67500.2; AT1G67500.
DR EnsemblPlants; AT1G67500.7; AT1G67500.7; AT1G67500.
DR GeneID; 843071; -.
DR Gramene; AT1G67500.2; AT1G67500.2; AT1G67500.
DR Gramene; AT1G67500.7; AT1G67500.7; AT1G67500.
DR Araport; AT1G67500; -.
DR TAIR; AT1G67500; REV3.
DR HOGENOM; CLU_000203_3_1_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HTM5; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISS:TAIR.
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; ISS:TAIR.
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; IDA:TAIR.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0009411; P:response to UV; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
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.
PE 1: Evidence at protein level;
KW 4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4HTM5,
KW ECO:0007829|ProteomicsDB:F4HTM5};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 103..198
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1056..1189
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1321..1768
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1814..1887
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 533..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1915 AA; 213748 MW; 7F997481922E264F CRC64;
MADSQSGSNV FSLRIVSIDY YMASPIPGYN ICYSSFQGSE VNEVPVIRIY GSTPAGQKTC
LHIHRALPYL YIPCSEIPLE HHKGVDGSTL ALSLELEKAL KLKGNAASKR QHIHDCEIVR
AKKFYGYHST EEAFVKIYLY HPPDVARAAS LLLAGAVLGK SLQPYESHIP FILQFLVDYN
LYGMGHVHIS KMKFRSPVPH HFRPRRFDLD DCPGQRIDEV AITKANSSAA ASVSFPVWSL
STIPGQWMWN LSEESDTPLS QSQHRHQHHY RRQSLCELEG DATSSGNFPD SKFNCLCFMY
DRTFELASSL VDILNQQFKM YNSLSQAQSD TNMVQSLVAI WEEEYERTGV HDAPIPPDPG
KPSAADVLQT MSDYVGFGNM LKEMLNKVEL SPPGMKPTAV SSAGPDMHAK PEITDLQALN
HMVGTCSEFP ASEQLSPLGE KSEEASMEND EYMKTPTDRD TPAQIQDAEA LGLFKWFASS
QAAEDINSDD EILRETILSP LLPLASINKV LEMASTDYVS QSQKECQDIL DSQENLPDFG
SSTKRALPSN PDSQNLRTSS DKQSLEIEVA SDVPDSSTSN GASENSFRRY RKSDLHTSEV
MEYKNRSFSK SNKPSNSVWG PLPFTLTKNL QKDFDSTNAS DKLGLTKISS YPMNEMTDNY
IVPVKEHQAD VCNTIDRNVL AGCSLRDLMR KKRLCHGESP VSQHMKSRKV RDSRHGEKNE
CTLRCEAKKQ GPALSAEFSE FVCGDTPNLS PIDSGNCECN ISTESSELHS VDRCSAKETA
SQNSDEVLRN LSSTTVPFGK DPQTVESGTL VSSNIHVGIE IDSVQKSGRE QESTANETDE
TGRLICLTLS KKPPSLDCLS AGLQDSAHSH EIHAREKQHD EYEGNSNDIP FFPLEDNKEE
KKHFFQGTSL GIPLHHLNDG SNLYLLTPAF SPPSVDSVLQ WISNDKGDSN IDSEKQPLRD
NHNDRGASFT DLASASNVVS VSEHVEQHNN LFVNSESNAY TESEIDLKPK GTFLNLNLQA
SVSQELSQIS GPDGKSGPTP LSQMGFRDPA SMGAGQQLTI LSIEVHAESR GDLRPDPRFD
SVNVIALVVQ NDDSFVAEVF VLLFSPDSID QRNVDGLSGC KLSVFLEERQ LFRYFIETLC
KWDPDVLLGW DIQGGSIGFL AERAAQLGIR FLNNISRTPS PTTTNNSDNK RKLGNNLLPD
PLVANPAQVE EVVIEDEWGR THASGVHVGG RIVLNAWRLI RGEVKLNMYT IEAVSEAVLR
QKVPSIPYKV LTEWFSSGPA GARYRCIEYV IRRANLNLEI MSQLDMINRT SELARVFGID
FFSVLSRGSQ YRVESMLLRL AHTQNYLAIS PGNQQVASQP AMECVPLVME PESAFYDDPV
IVLDFQSLYP SMIIAYNLCF STCLGKLAHL KMNTLGVSSY SLDLDVLQDL NQILQTPNSV
MYVPPEVRRG ILPRLLEEIL STRIMVKKAM KKLTPSEAVL HRIFNARQLA LKLIANVTYG
YTAAGFSGRM PCAELADSIV QCGRSTLEKA ISFVNANDNW NARVVYGDTD SMFVLLKGRT
VKEAFVVGQE IASAITEMNP HPVTLKMEKV YHPCFLLTKK RYVGYSYESP NQREPIFDAK
GIETVRRDTC EAVAKTMEQS LRLFFEQKNI SKVKSYLYRQ WKRILSGRVS LQDFIFAKEV
RLGTYSTRDS SLLPPAAIVA TKSMKADPRT EPRYAERVPY VVIHGEPGAR LVDMVVDPLV
LLDVDTPYRL NDLYYINKQI IPALQRVFGL VGADLNQWFL EMPRLTRSSL GQRPLNSKNS
HKTRIDYFYL SKHCILCGEV VQESAQLCNR CLQNKSAAAA TIVWKTSKLE REMQHLATIC
RHCGGGDWVV QSGVKCNSLA CSVFYERRKV QKELRGLSSI ATESELYPKC MAEWF
//
