ID A0A074SDA2_9AGAM Unreviewed; 1461 AA.
AC A0A074SDA2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=V565_012630 {ECO:0000313|EMBL:KEP54793.1};
OS Rhizoctonia solani 123E.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP54793.1, ECO:0000313|Proteomes:UP000027456};
RN [1] {ECO:0000313|EMBL:KEP54793.1, ECO:0000313|Proteomes:UP000027456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123E {ECO:0000313|EMBL:KEP54793.1,
RC ECO:0000313|Proteomes:UP000027456};
RA Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA Zafar N., Nierman W.;
RL Submitted (DEC-2013) 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}.
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:KEP54793.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZST01000018; KEP54793.1; -; Genomic_DNA.
DR STRING; 1423351.A0A074SDA2; -.
DR HOGENOM; CLU_001718_1_0_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000027456; 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; 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:UP000027456};
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 13..76
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 419..719
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 787..1233
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1269..1452
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 164212 MW; 3C44501A15FDA241 CRC64;
MSRRALKPNK DRLADLRAAR EAGGRSKQWK SKEDEDLYEE VSEDDYKKLV KSRLDRDDFI
VDDDGSGYVD NGMDAFEAGG DYESDDNEED EEERRKRKAE RKKTKAALAA QRAKDQAHAE
KSISDYRPAV STEKEQDFMN SLLGTLDSMP SKPAAPSKRK LAPTYGGPTR PFNPSGSLKR
KPAAMNVFRS DAPSSDPPSD AGYGHFTSDA NDTSENEWAM GSASPTKKPK REPSSSPARR
LSSLAVEDGD EYEDGDADFW EEAAGMDLDE PEIAKGKAKL LNPANVLPNG RAAKVEPKPE
LVDTKPPAWL DLHASLNASA VTEPETLGSD KPGTIVSNDV KALEEDGSLR IFWLDYLELD
SRLYLVGKVI DKAQSTAKVT KWASCCVAVE GIERNLFVLP RKFRMEFGHE TDAPPEEDDV
YDEFDRLRQK HGIKKWAAKF VPRKYAFGES GIPEGESQWM KVVYGYDEPA LPMELSGATF
GRVLGTNTSA FELFVLKRKI MGPCWLEIKG CELSNKGFSW CKLEVIVRDP KTVNPLSEDV
TMPVPPLTIV SLATRTVVNH KENKREIVCA SMRIWENTNI EDATSPEKQP SVVHTVVRPL
GKLPTGFEAK IRSEKSAVKP MANEKMMLNN LMATLHKHDP DVIVGHEFSG FTLDILLLRM
KELKLEHWSR LGRFRRSRWM NIGKQGTNVK FLQGRLLCDL ASDGAKSMIQ STSWSLTEMC
QSQLKITRED IDPDDTASFF DATVSSPDRL LHFVQHCELD AFLQMALAHK IQMLPLTRQL
TNLAGNSWNK TLNGGRAERN EYILLHEFHR LKYVPPDKTW AKKSGPAVVK AEVVDDEGGA
APVVAKSKRD KYKGGLVFEP KRGLWDKYIL VMDFNSLYPS IIQEYNIDFT TVDKTDDDTG
EGKIPAVPDS DVPQGVLPRL IATLVNRRKQ VKSLMKDRNA TQSQLVQWDI KQKALKLTAN
SMYGCLGFEY SRFYARPLAA LTTFKGREIL THTRELAESL TLDVIYGDTD SIFVNSNVTD
LPEALKIANE LKKAVNDRYR LLEIDLDGIF RRMLLLQKKK YAAVKVEEMN ASSVEIKGLD
MKRREYCMLS KNISEYILEQ ILSGDDAETV VERIHDYLRL MGENIRSGRV DMEDFIVFKR
LGKAPEDYPK DNSLPHVHVA KRMKERGGHA RIGDVIPYIF CLGGDGTSVK TGQADRAYHP
DELRKTDSEL KIDFEYYIAQ QILPPVERLC DPIEGTDRAR LAECLGLDPS RFQTSVAAVD
SDPYRTLDSQ IPDKERFREA AQFLIRCRKC EGSAVFSPVG TTEVPIITSA GVRCPGCSEE
LSSASVQVQL ETQLRQQINQ YYSGWMVCED ATCGHRARSM SVYGKRCLNP GCVAKGPVSY
EYTDLKLYNQ LLYYTSLFDG HKAIEKAAGT PRHGEVIALV GLNNEFLTTM TNCVEKYLNQ
CARRWVEMGT LFSFMQITKK A
//
