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Database: UniProt
Entry: A0A2T9YMH9_9FUNG
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Original site: A0A2T9YMH9_9FUNG 
ID   A0A2T9YMH9_9FUNG        Unreviewed;       708 AA.
AC   A0A2T9YMH9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=BB561_003193 {ECO:0000313|EMBL:PVU93555.1};
OS   Smittium simulii.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU93555.1, ECO:0000313|Proteomes:UP000245383};
RN   [1] {ECO:0000313|EMBL:PVU93555.1, ECO:0000313|Proteomes:UP000245383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU93555.1,
RC   ECO:0000313|Proteomes:UP000245383};
RX   PubMed=29764946;
RA   Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT   "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT   Symbiosis.";
RL   MBio 9:e00636-e00618(2018).
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   -!- 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:PVU93555.1}.
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DR   EMBL; MBFR01000124; PVU93555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T9YMH9; -.
DR   STRING; 133385.A0A2T9YMH9; -.
DR   Proteomes; UP000245383; Unassembled WGS sequence.
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; 6.10.10.100; -; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR045846; POLBc_alpha.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 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:UP000245383};
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          27..143
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          211..684
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          283..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..300
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  79841 MW;  35E3DCBD7028E460 CRC64;
     MVIIRKIENV PLPYNFIDNE SQNSSSGTTV KGKPHITVAT SERNLLMYLV GILARLDPDI
     IVGHNFVEFI LGILLHRMKA AKIPDWSKLG RLKRTEWPKL QSGSGGMRKS TYWESLMMSG
     RMICDSYLTS RDLIKSKSYS LTELSSSELK IKRREFSMEQ INKILISNRS SNLLVDLCEH
     TCVDAYLCTS LILKLQALPL TCQLTNLAGN LWSRTMAGAR AERNEFLLLH EFYNMKFIRP
     DKNYSSNKFS QKLTNSKASG LASNNAASNK NVKVVTTAST ENESIDDIPY EPENSDLEDN
     EALNNENNKN ESKFKRRKPT YAGGLVLEPK KGLHDQYVLL LDFNSLYPSI IQEYNICFTT
     VQRNQNDDSI PQDPDPSLPI GLLPKLLKTL VERRKQVKKL LTSPGLSESD KTALDVRQKA
     LKLTANSMYG CLGFAQSRFF AKALAILITS KGRNILIDTQ GLAESQGLEV LYGDTDSIMI
     NTTSNILNEA YDLGIKFKRQ VNERYKLLEL DIDGIFRRLL LLKKKKYAAL TVSNLSECIR
     KNFENRSNGL NDEKILTKLE TRGLELVRRD WCGLSAEVSS FVLENILSGM DIDIISSTIQ
     NHLTQVANSV RSGNIKLDKY IINKALSKPP ESYSESTSLY HVSVALRVKK FGYYYNTGDT
     VPYIMGLESN IEGPDNKIDL EREPNSANTK AFHPEEIKRS EGKIKIGT
//
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