ID A0A2S6C8A2_9PEZI Unreviewed; 1719 AA.
AC A0A2S6C8A2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=CBER1_03596 {ECO:0000313|EMBL:PPJ55955.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ55955.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPJ55955.1}.
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DR EMBL; PNEN01000528; PPJ55955.1; -; Genomic_DNA.
DR STRING; 357750.A0A2S6C8A2; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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 {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 Reference proteome {ECO:0000313|Proteomes:UP000237631};
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 855..1033
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1100..1546
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1599..1683
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 481..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 195236 MW; 2347F398EDC9B7D4 CRC64;
MDRKDVFRIR LNCVDHAQYA PNTMDTPIWG PRSLSATQRV QLPDVPVIRV WGSTETGQKA
CVHIHGAFPY LYVPYTESLG DSHVSQYMST LRHSIDHAMC LSYRRNPYEN PRNATFVAHL
SLVKGVPFFG YNVGYKYYLK IYLLNPLHMT RFADLLQQGA ILRQHFQPHE AHLQYLLQWM
CDFNLYGCAY IEIAKAKFRS PVPVWEELDD LAHLWHDRSI DANDILDAER FPRQSHCQLE
LDIRVEDILN RHSIEPRPLH HSFIERLASL ENLPPEEKLV HSMAGLWKDE TRRRKLRMGM
TDPTSSPFPP EVLVSMSADP RNDSKAGWIH EEEFREAIND LAEQEKRQRG GAALSFETFG
SQNKDHDDSV PTVLDSVSEL FHSTLEQKWA TLAREAKARQ QEPYEMSFNE FVSTQRPGDQ
APLIDENSIA RVADDEGYLN DEEEAKLLAL AQKQRLKDTG LAAMGESKLN DEPAQLEADA
EQLEGAKVPR STVEETSESL LKRPAPVSSQ LPFKKARLDS QHKSPRAERR HFRIKDVKPT
THIDGASSRP GGDGFHAPPA AQIQKIVAVA VDDGADLPPA TQPPLSQRSI QSSQGDKISF
PTAKHPHDPA TLQRLSQRGD LAHLPHRASR ASQKEALISS DNSGTLKSVT SMPSPRKTMP
TISADAAQAY ARAFGVTAGC HVRVLAALPP TRDEVVATIE PSVIYQDAYY SNEKDVPERV
REYAGREFRL ESTTLPYLPA FDKYGSIGQP ERLSKVDAEF SLNRRIWQCS HKVWEIMKPA
PSYEEVNAWL QSESPSEPDD LQVLDFDGPP VASQLKRKNR APRELSQIEG PTQRNRHGFK
YSQKKASTSV QHETGYMSIM SLEVHVNNRG DLAPDPEIDE VNMIVWCVAD EQMDDETKLG
ILVLEQDNDD LPGKIRKVLG NDVQIDSEDN ELDLINRMVD IVREYDIDIL TGYEVHNNSW
GYLIERARLQ YEFNLPDEFS RMKSHSKGRF GKDADRWGFT HTSTVSITGR HTINIWRAMR
SELNLLQYTM ENVVFHLLHR RIPHYSYATL TRWYKSDKPR DFAKALDHLI TRTRLDLEIL
DANELIPRTS EQARLLGVDF FSVFSRGSQF KVESLMFRIA KPESFVLVSP SRKQVGGQNA
LECLPLVMEP QSAFYNSPLL VLDFQSLYPS VMIAYNYCYS TCLGRITNWR GTNKMGFADF
KRHPGLLELT KEKLNIAPNG MMYVKPEMRK SLLAKMLGEI LETRVMVKSG MKVDKDDKTL
QQLLNNRQLA LKLIANVTYG YTSASFSGRM PCSEIADSIV QTGRETLEKA IALIHSIERW
GAEVVYGDTD SLFVYLKGRT KDDAFRIGDE IAKAVTDMNP RPIKLKFEKV YHPCVLLAKK
RYVGFKYETP SQKEPDFDAK GIETVRRDGT PAEQKIEEKA LKLLFRTSDL SQVKSYFQAQ
CTKILTGRFS VQDFCFAKEV KLGTYADKGA PPPGALIATR RMLRDPRQEP QYGERVPYVV
IAGAPGARLW ERCVEPEQLI RDENADLDAE YYINKNLIPP LERIFNLVGA NVRSWWDELP
KVQRIRQLGG VGEGSLEGAK DMTTNARKTM ESYMGSSLCL ICRTKLVPPG QNPLEHEEEI
QLPLCETCRH VHTSTTLLVL RRKLQAAEMK AKDMHDVCRS CAGLAFDEEV KCDSRDCPVF
YSRVKADTQL RVARRGVGSV LEALEEEAVE QETAEDLEW
//
