ID A0A074S7U0_9AGAM Unreviewed; 1097 AA.
AC A0A074S7U0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=V565_007510 {ECO:0000313|EMBL:KEP55244.1};
OS Rhizoctonia solani 123E.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP55244.1, ECO:0000313|Proteomes:UP000027456};
RN [1] {ECO:0000313|EMBL:KEP55244.1, ECO:0000313|Proteomes:UP000027456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123E {ECO:0000313|EMBL:KEP55244.1,
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|ARBA:ARBA00024632,
CC 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}.
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:KEP55244.1}.
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DR EMBL; AZST01000009; KEP55244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074S7U0; -.
DR STRING; 1423351.A0A074S7U0; -.
DR HOGENOM; CLU_000203_2_0_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000027456; Unassembled WGS sequence.
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:0004527; F:exonuclease 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 CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 1.
DR Gene3D; 2.40.50.730; -; 2.
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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA 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|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, 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, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 150..462
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 526..963
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1001..1075
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 123466 MW; EB54A81020993066 CRC64;
MAKDAVGSSR KRSEDDTQAN TKKRKVDNGV SAKKSLMGSQ SLANTQGSSF VDILEQFEDG
DAQAEGGRNL WPRPEVKKFD PENTSIVFQQ IDIDMFPGAN GLDFGLFGVT AEGHSVLARV
TDFLPYLYIA TPRGYDPNES QAFMDHINGQ IAAGTVVKIE TVQKRSLWSY RLNARGEDET
SPFLKLTLAE ARNVPKVRDK YISSFWSITT YQCAYQGLFN GPITTYESNM PFELRFMVDR
QIIGMNWVEA PAGAYQLRTG KQKISNCQIE LDIRHDLLVS HPAEGEWSKA APLRILSFDI
ECAGRKGIFP EATIDPVIQI ANMVTVQGET SPFVRNVFTL DDCAHIVGTD VISFKKEDAM
LLAWRNFVEE VDPDVVIGYN IAGFDLPYLL DRARALKGDA EGFPYLGRVK HYKTTTKDTH
FSSKAFGQRD SKETQLHGRL QLDMLQYMQR EQKLRSYTLN AVCAHFLGEQ KEDVHHSVIT
DLQNGSPETR RRLAVYCLKD AYLPQRLMDK LMCFVNYMEM ARVTGVPFNY LLQKGQQIKV
VSQLYRKANA DGYVIPNMKA EGVDEQYEGA TVIEPKRGYY DVPIATLDFS SLYPSIMMAH
NLCYTTLVYK DTIDQYGLVK GVDYVQTPNN DFFVTANRRK GLLPTVLEDL ISARKRAKAD
LKNETDPFKR AVLDGRQLAL KACPRSIISA NSVYGFTGAT IGRLPCLAIS SSVTAYGREM
IERTKHEVET EYCIKNGREH DAEVIYGDTD SVMIKFGTTD LESTMALGAE AAESVTAKFV
RPIKLEFEKI YFPYLLINKK RYAGLYWTNP KKYDKMDTKG IETVRRDNCR LVQTVIDTCL
RKMLVDRDVK GAEDYTKQVI SDLLQNRIDM SQLVITKALA KADYAAKQAH VELAERMKKR
DAGSAPALGD RVAYVIVKAA KGAAAYEKSE DPLYVLENSI PIDTKYYLDN QLSKPLMRIF
EPILGEKAAA TLLSGSHTRT IQIATPTIGG LMKFAVKTVT CLGCKTPLKS SNSSMGAVCN
NCRPRLMELY YKQTRQTSDL QVAFARLWTQ CQRCQGSLHQ EVLCTSKDCP IFYMRKKAQK
DVEDSVAVLD RFTDESW
//
