ID A0A1M8A8Q1_MALS4 Unreviewed; 1400 AA.
AC A0A1M8A8Q1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=MSYG_3178 {ECO:0000313|EMBL:SHO78830.1};
OS Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO78830.1, ECO:0000313|Proteomes:UP000186303};
RN [1] {ECO:0000313|Proteomes:UP000186303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX PubMed=28100699; DOI=10.1093/nar/gkx006;
RA Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA Lehtioe J.;
RT "Proteogenomics produces comprehensive and highly accurate protein-coding
RT gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL Nucleic Acids Res. 45:2629-2643(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 -!- 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; LT671825; SHO78830.1; -; Genomic_DNA.
DR STRING; 1230383.A0A1M8A8Q1; -.
DR VEuPathDB; FungiDB:MSYG_3178; -.
DR OMA; MTKMNVG; -.
DR Proteomes; UP000186303; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000186303};
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 11..74
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 409..692
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 761..1184
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1217..1395
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 13..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 156488 MW; BAC08D6F4FCA34B2 CRC64;
MASRAKRLEA LAALKASRSG GPRVHPQAEE DDRIYDEVSA EVYQSIVRGR MMEDDFIEDD
DGSGYVDHGQ DEWENGPQSE SESEDEHEYY ERTGRRKPKK GARRQAQRAA PTDYMGRTRP
SERAADAPAR RVPAAAAAPS KDAEEAFMSQ LFGGLAPMST PARPMASLAL DDSQDSPSLT
MARKRKQTHT PSAMPALVPD LSSSAEPSSD PLELSWSPEA SAKKQKSDDA EPMDDADDDF
AHVSVGAKRA TKLVSTGASQ PAIAPAPAPA KAVPAGAEAP AAESPSVLPS WRRVHESLAA
VAAPETSAPT AATSTQIYEA DRSVSFYWLD YADVHGKIYL FGKVLDQASQ RYVSASVAID
GIERCVFLQP RTRTLVHGHE TDMVPSEDDV FEEFDALRSR HGISAWLGKW VTRRYAFELP
DVPAEGRYLK IKYGFDEPAL PTDVSGATFV RAFGTQTSAF ELFVVKRRIM GPCWLKLDQV
SVPSGPPQTW CKLELAVDDP KCVSPYSDAD ANAPKEPPPL TVMSLALRSV VNFKENKREI
VAASARVWPD MALESATPVE QLPSSSFTAV RPLGPSFPPR FEAEVAQSST PVKAFKYERM
VLNSLLAQIQ RHDVDVLVSH DFVGSTLDVL LHRLRDLKCE QATRLGRLRH EGTRPTKYSQ
AMRLLAGRLV ADLSSDMAKG MISSTTWSLS EMCRTHLQVQ REDMDPEDVP SYFDSTAPTP
ARLLTFVRHL EVDSFFQMAL ASKVQLLALT KQLTNLAGHA WSRTLNGGRA ERNEYILLHE
FHKKKYLCPD KPLAWEKKKD DAGKKETFKG GLVLDPKRGL WDKYVLVMDF NSLYPSIIQE
FNIDFTTVER HGGDDVPDVP SSDVAQGVLP HLIATLVNRR RQVKALLKDK NAPTLKRVQW
DIKQRALKLT ANSMYGCLGF EHSRFYARPL AALTTFKGRE ILSMTCELAE SMELDVIYGD
TDSVMINTRC IDYQAALRIG HAFRRAVNER YRLLEIDIDG VFQRMLLLQK KKYAALLVND
AGETHTEIKG LDMKRREYCQ LNKQVSTYVL EQILSGEATE TVVERIHTYL QGVADDVREG
RVPLDDYVIF KRLGKRPQDY PDAQHQPHVQ VALRMLAKNE PVRSGDVIPY VFCVGADEKS
AQAQRAFHPD EVRRHAGDPA YKIDVHHYLS LQLLPSIERL ADCIEGTDRM RLAECLGLDV
HTYTHDPVDQ RFAPLDSQVP SVVRYAHCEP FTVRCRACRH ATPLQPPSRT RADAPWLACE
ACRAPFPRAT LVVQLELAIR AHVARYYEGQ TTCTEPACRA VTRQAGVYSG RCVVPSCRGQ
VQRMYSDKTL YTQLCYYAYL FDAAQALEEV SETSQRHALR DRLETHKADM EVLRATVDAF
LARNGRRYVG LGKLFSFLRV
//
