ID R9NVY0_PSEHS Unreviewed; 1680 AA.
AC R9NVY0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=PHSY_000198 {ECO:0000313|EMBL:GAC92644.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC92644.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(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|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}.
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DR EMBL; DF238767; GAC92644.1; -; Genomic_DNA.
DR RefSeq; XP_012186231.1; XM_012330841.1.
DR STRING; 1305764.R9NVY0; -.
DR GeneID; 24105510; -.
DR eggNOG; KOG0968; Eukaryota.
DR HOGENOM; CLU_000203_3_1_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000014071; 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:UP000014071};
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 798..970
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1037..1483
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1563..1632
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1680 AA; 189427 MW; 6BFEC161B51AD3EF CRC64;
MTTMESAEQS EPTPQRTEKT DSASSDPFFR VRLINIDHIL TAPTPLDRTQ CAFNAEGHTL
RKVPILRIFG ATPAGQRVCV HIHNVYPYCY IQYKGSLEPD DVLRYIHRLG RELNAAMAAS
LRRNPHDPEL NQFVAAIHLC KGVNFYGYHV GYAYFLKISF VDPAHNYRIA AILESGGVMK
TGFQPFEIHI RYQLQFMLDY NIFGCDYLDL DDVRFRLPIP DGSAIASDEP SPLDFRSKIW
NRNSIPYAHV QAQDVHRGTH CELEADASAP WIINRRRLKE RDIHSDFDEM SPASPDQNIL
VPSLSGLWDD EKNRRNAAGL PPSIPTADPT RDPRLYATGE SPPWMSEDRM RLLLEKRIID
EKQKTLPRER SAGHFTDRPG LDQYIMTTFD AVEVFHPYQD QIHAADPYSQ RTGPSASSKL
YDLQHAISQT QRGESHPTEP TQLTQQLNQE TDDFDTKYFK SQNFHHLLQQ AEKEDIAANQ
DPPSDQEDDA NDIDPNEPID AQPDGPGTPR KWHRTDSSRS NMSTSSNFSK SPLSTPKKRQ
HTDFLGNGAT TPQASPSSRL TKDVHEDSVR KFKQAKHDHS AGSTGGSNGY RSAHVIDSSR
SARVRFVEAG SPTPVSKTRR PEMLPLLPSS APRKRLIAFH EPAPSLRTVV ETFPLFSIVR
QVHPEPFFSD PNDIPTRPRE YAGRMFQFQS RTLPFLRTFE HWNQSGEPAP STQPGKPPRR
LHWQFGPPPP TVLEARAWRQ KEKVVEKQRS KRRRARLLSQ IERLTQANDF GFKISQHKAT
TLVMRDKQHM TTLAVEVLTT TRGNLFPDPA FDAVQSIIYS FQNEDEKLQD TGSRADLRTG
LIIVAGDDDV HVDRLGLSHL ALEVVEDELE LFNTLIDLVR AFDPEIMVGW EIHSSSWGYI
IERASKEYDF DLVPQIGRAI VHNTGRAGGK SDNYAYTQSS ALRITGRHTL NLWRLMKGEL
TLNLYTLENV CYHLLHRRIP KFSHQTLTQW FKSGRAELIR KALLYYIDMV ELELEIIAES
EFVMRTAEFA RIYGIDFFSV ISRGSQFKVE SIMLRIAKPE NFVLISPSRA QVGKQNAAEC
LPLIMEPQSA FYKGPLIVLD FQSLYPSIMI AYNLCYSTCL GRVSGFKGTS KFGVTEYSPP
KGLLSLLQDD VNISSNGLLF VKPSVRKSLL AKMLSEILDT RVMVKGSMKG TKADKSFQRI
QNARQLSLKL LANVTYGYTS ASFSGRMPCV EIADAIVQTG RETLEKAMDL INGTEEWGAQ
VVYGDTDSLF VYLPGRTKEE AFRLGNTIAD KVTSLNPRPV KLKFEKVYLP SVLLAKKRYV
GFKYETLDER EPGFDAKGIE TVRRDFHPAI QRMLEACIRI LFRSRDLSLV KSYLQRQWRK
ILEGRVSPQD FIFAKEVRLG SYSDKVAPPP GAAVSSRRML ADPRSEPQYG ERVPYIISQG
EPRAKLNQQA VSPEAFLKNP QLQINALYYI TRTIIPPLAR VFNLLGADVE AWFHEMPKPN
NAYWNKRPTV ALLSAVLAQQ EEIEAEAAEN ADGGVSSQRL ATGKGTSSAA IATLNSHYAT
ETCLLCSSRT EALVCLDCRQ SPQQSIHAIS SKLHKLQSQA AAIDRICSTC AGMERPGPVE
CVSLDCPYTY QKTKVHKSLE DAALVNAYVS RLFGSDMQRQ AGVEDAWVGT EGEGSGMDSY
//