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Database: UniProt
Entry: A0A061F9Y3_THECC
LinkDB: A0A061F9Y3_THECC
Original site: A0A061F9Y3_THECC 
ID   A0A061F9Y3_THECC        Unreviewed;      2035 AA.
AC   A0A061F9Y3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=TCM_026537 {ECO:0000313|EMBL:EOY11309.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY11309.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY11309.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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|ARBA:ARBA00024632};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
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DR   EMBL; CM001883; EOY11309.1; -; Genomic_DNA.
DR   STRING; 3641.A0A061F9Y3; -.
DR   EnsemblPlants; EOY11309; EOY11309; TCM_026537.
DR   Gramene; EOY11309; EOY11309; TCM_026537.
DR   eggNOG; KOG0968; Eukaryota.
DR   InParanoid; A0A061F9Y3; -.
DR   OMA; CYSELRG; -.
DR   Proteomes; UP000026915; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
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: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; 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   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1173..1309
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1441..1888
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1934..2007
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          545..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          823..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..844
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2035 AA;  225289 MW;  90B42F488EF9DC48 CRC64;
     MSNSQPDSNV FSVRIVSIDH YMARPISGYD TCYSSFQGER VNEVPVIRIY GSTPAGQKTC
     LHIHRALPYL YVPLVDILPQ GSHTHQEDHA CADALALALE KALKLKVGAG SKRQHVHGCS
     LVRAKKFYGY RSSEELFVKI YLYYPHDVSR AANLLLAGAV LDKSSQPHES HIPFILQFLV
     DYNLYGMGHL HLSRMKFRNP IPDLSHPRKI NNCGQHGQKM DDLTLKAAGF QADSSRDVCI
     NSPVWISSTI PGEWMWHVSA ELDVSSDQDI CHVKRQSLCE LEGDATLDDI LNQQFKIYTS
     LSQTCSDVKM VQSLIPIWEE ECERTGMHEM ALPSYPDRPL SEDVLKALSL GVGFEDELMK
     LCSKVEETLS HNELGFEQSV IPSANEENLV GPTHINLNHT VPQALSCSKE QSLLGSLSQH
     CKPCEKEMNA ASSEKKDVCP ELLSVGEILS SQTATDTEAL GLLAWLANSH AADDINSDDE
     LVRETILTPL LPATTIDKVL EKASIDYESE SQKECQDILD SVGDLIEFDG LKERNSHSYD
     HIQISSGKHI PQTDGSSDDL GLSPSAGSVA NSSKADMKTE LKRSSQDTSK TFSTKRKRKK
     LLWGSLPLSV TGKGKDNSDS VSFNITEACA DEIKECLGTS FSAENDLGKA SDPLNKNAHA
     SDDKQEAGIL VECTVRDLMR RKRSRRIEPA DCGSVRSENV HLKMEKGKDS FFCPKQLNFH
     GSHNELDKKG PGSLNHSPSL ANEQKEFPEA VGFKPTHSDS VYCTLPQLSG ISNPAQANTG
     HPEQMGKKLV LNFYPKKHDS AISIGHCETY KGKEFDFRVT SAESRNSDAH TSKAHKEIDS
     PDERLQQTDT NGSWCLSASP RTHKMLGMDG YIHETYYEGE ISLSADKPVG IDATTDKSYP
     QNEDCGGGKQ GCITGLVVDV EAKPVELIGM TFCKKPPTAD WNDGATENVT HLPTTQHSPS
     LFNEENCQGT SGRALDEVLP FFSRGCEEEK EVQNKCLGNN NSNFHQEAAL GVPIHYQNDG
     SFLYLLTPVS SPPSPDSVYR WLSCDEEGSH RQSNAVSAES PSLTGSTECL IASENSSPVN
     CNEALTKSSS KYHMTSMLEQ GHPEKNMVLG SEVKSCSNES RTPCQSEENI RTVNACADGS
     QDMSQISGPD GKSRPTPLSQ IGFRDPASVG AGQQLTLLSL EVHTESRGDL RPDPRFDAVN
     VVALAIQNDN DSETEVHVLL YSKTGFYQRN LDGIFGLKVF VFSEEKHLFG QFMKILCSLD
     PDILMGWDVQ GGSLGFLAER AAYLGIGLLN KISRTPSETK IKAEETNISQ KGSQEELLSK
     PLIADSIVME DAIIEDEWGR THASGVHVGG RIVLNVWRLM RGEVKLNMYT VEAVAESVLR
     QKIPSIPYKV LTKWFSSGPA QARYRCVEYV VERAKLNLQI MNKLDMINRT SELARVFGID
     FFSVLSRGSQ FRVESMFLRL AHTQNYLAIS PGNQQVASQP AMECLPLVME PESGFYADPV
     VVLDFQSLYP SMIIAYNLCF CTCLGKIANS KVNTLGVSSY APDPNVLRNL KDQVLLTPNG
     VMYVPSKVRK GVLPRLLEEI LSTRIMVKQA MKKLTPSQQV LQRIFNARQL ALKLIANVTY
     GYTAAGFSGR MPCAELADSI VQCGRSTLEK AISYVNAHEK WRANVIYGDT DSMFVLLKGR
     TVKESFKIGH EIASAITAMN PNPVTLKMEK VYHPCFLLTK KRYVGYSYES PDQVKPVFDA
     KGIETVRRDT CGAVAKTMEQ SLRLFFEHQD IPKVKAYLHR QWTRILSGRV SLQDFVFAKE
     VRLGTYSTKV GSLPPAAIVA TKAMRADPRA EPRYAERVPY VVIHGEPGAR LVDMVVDPLE
     LLAINSPYRL NDLYYINKQI IPALQRVFGL VGADLNRWFS EMPRLAREAF GKCGVHALNP
     QRTRIDYYYL SKHCILCGDL VQASAHLCGK CSENKTAAAT AIVGRTSKSE REMQHLVAIC
     RHCGGGDWLV ESGVKCNSLA CSVFYERRKV QKELQGLSAV ATDKGLYPKC MVEWF
//
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