ID A0A2U9RAV1_PICKU Unreviewed; 1515 AA.
AC A0A2U9RAV1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=C5L36_0E00850 {ECO:0000313|EMBL:AWU78018.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU78018.1, ECO:0000313|Proteomes:UP000249293};
RN [1] {ECO:0000313|EMBL:AWU78018.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU78018.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CP028777; AWU78018.1; -; Genomic_DNA.
DR STRING; 4909.A0A2U9RAV1; -.
DR VEuPathDB; FungiDB:C5L36_0E00850; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000249293; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
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; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 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|ARBA:ARBA00022485};
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}; 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 ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000249293};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 7..71
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 448..762
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 827..1279
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1317..1512
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 152..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1515 AA; 171557 MW; 6F11325E5B866B17 CRC64;
MGKTDKLARL RAARSGAKID DFDSEEENVN IYDVVDENQY RKHKRDRVLN DDFIVDDNGA
GYAENGAEDW DAQPNAYTSM DDEEEIEYNK ENGKPKKLKK VKMFKESEPV IPTKKIDSFF
KVQPSQLEQR QKAKKSNDSS ILEDILSDFT SQATSMMKKK PTDAASKRKN PFSSLKSNGL
NTSTPANKKT YVMSMSSNIS DNKPFEFTSP SRKKQKVDSN DETRDTTFYT AHQFEGSIPF
ETPSSPIRSN NFHSKANILD QLENVSMDVS THENIKNEEE EEEDDDDEDD DVIVSSKRNR
NVVMVDRSVM LNGKKSINKA VDSSPLKNLK HIDIGSSPSK ASNISNMSNV SSITFEKLGG
EDVVMKDDDG DDGIQMYWMD YIELDSSLLL FGKIKSKDGR MVSGMVQVNG LCKTLYFLPR
NGQARDQNQK SNPDESIATE SYTAMDVYDE IIPLLMDKFG LDSIKAKPEV KKYAFEHYDI
PHEAEYLKVL LPYNTPKSQG VTIPADLTGE TFSALFGSGT SIFESFVLQR QIMGPCWLNI
TGCDFKSLQN VSHCNVEVAV SSPSDISPNL YTRDPPPPLN VLSINVQSYL NPKTSRQEVG
SVSMALYRDL PQDVPIQPNL EPTEEITLLR PVGGTTSLPI SINALAEKRN IKLRTLNSEK
ILLNCLAGLI KKYDPDVFVG HKLEGVTLDI LLHRMKDLNI SHWSNFGRRS RKVFPDKFSR
SNGRYNLFLI REMLAGRLLC DISNEMGQSL TPKCQNWELA EMFEVVCREK YTPMEVNLAN
PLVAEDPNKL LAAVNENVLS ARIIAKTAFG MQILSISKQL TNLAGNAWSH TLGGTRAGRN
EYILLHEFER EGFISPDREN QQQRQQRLNQ KVNIDVDDEN NDESNTVSNK KAKYQGGLVF
EPEKGLHKNY ILVMDFNSLY PSIIQEYNIC FTTVERANLV GDELPKVPSK RDMGVLPKLL
QQLVTRRREV KSLMKDPKLT PIEKAQLDIK QLALKVTANS MYGCLGYVNS RFYAKPLAML
VTNKGREILM DTRQLAESLG LTVVYGDTDS VMIDTMSDNY KDAIKIGEGF KEKVNERYRL
LEIDIDNVFK RLLLHSKKKY AALNVFFNSN GEESTTLEVK GLDMRRREYC PLSKELSEYV
LNQILNNSDP QEALNEIYTK LQDVREKFSK NAIPMVKLRI NTKLSKDPSK YPNGVSMPAV
QVALRLQDQG KVIKAGSVIT FVITNGEPSE KAPLKNDQSS IASRARALVE VISNNEYTPD
IKYYCEKQLF NPIDRLLTRV EGYDVVRLAD SLGLESQRYE AKARDIVQQN DLQPLESTIP
DSERFRDMKD FSLKCLQCSK NITFGGIQPS NLYQVTFQGI KCKSCNCFLP PLSISSQLEL
FIRKEISKYY ECWLNCDDCG IRTRQISVYG RRCIGSNGTA HECKGVMSIE YNNKAIYNQL
LYLKSIFDVD KAKSKSLKPL AIDDENFKSA SNQGEINALA EQNRSQFQIY QKVIQKYLDV
NGRRFVDLGS IFRNN
//
