ID W6AQI8_BOMMO Unreviewed; 1085 AA.
AC W6AQI8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=101735729 {ECO:0000313|EnsemblMetazoa:NP_001296480.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:AHI59988.1};
RN [1] {ECO:0000313|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [2] {ECO:0000313|EMBL:AHI59988.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=306 {ECO:0000313|EMBL:AHI59988.1};
RC TISSUE=Midgut {ECO:0000313|EMBL:AHI59988.1};
RA Chen H., Zhou Y., Mai W., Li G.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001296480.1}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001296480.1};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
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}.
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DR EMBL; KF878074; AHI59988.1; -; mRNA.
DR RefSeq; NP_001296480.1; NM_001309551.1.
DR AlphaFoldDB; W6AQI8; -.
DR SMR; W6AQI8; -.
DR EnsemblMetazoa; NM_001309551.1; NP_001296480.1; LOC101735729.
DR GeneID; 101735729; -.
DR KEGG; bmor:101735729; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:UniProt.
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 2: Evidence at transcript level;
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:UP000005204};
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 162..459
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 524..953
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 991..1063
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 123836 MW; 6D0FC5D1848820BE CRC64;
MDRNKTKGPP PKRFKSGDDD DENDTPFSFE EQLACMDTGD IDSQEIFEGE GPENQSSNMK
WSRPPPPILT PNRETLIFQQ LDIDHYYGSP MNGMPGSQLA PVPIMRMYGI TSEGNSVCCH
VHGFTPYFYV TVPVNFTESS CNEMKTNLNK AILEDLRGNK DNIKECVLEV RLVQAKSIMY
YKGDSNITFA RVSVALPKLI AAAKRLIERQ PLSFGLMDPQ FYETNIDFDI RFMVDTSIVG
CSWIELPVGK WFLRTIDSKV KPESRCQIEV DVAWNAFIFH PPEGEWSKVA PFRILSFDIE
CAGRKGIFPE AKHDPVIQIA SMVIRQGETE PYLRNVFTLN TCAPIVGSQV LSFQSESEML
SKWSDFFRKL DPDIITGYNI SNFDWPYLIN RAKHLNVQKF DFLGRIKNVR SVIKDTVLQS
KQMGRRENKT INFEGRVPFD LLLVLVRDYK LRSYTLNAVS YHFLQEQKED VHHSIITDLQ
NESEQTRRRL AMYCLKDAYL PLKLLNKLMC IINHMEMARV TGVPLLCLLT RGQQIKVVSQ
LLRKAKEAGY LMPVYHSQGS DDQYEGATVI EPKRGYYADP ISTLDFASLY PSIMMAHNLC
YTTLVPPNAQ NQFNVADNDV TITPSKNMFV KNHIRKGLLP EILESLLAAR KKAKADLKDE
KDPFKRSVLD GRQLALKISA NSVYGFTGAQ VGKLPCLEIS GSITAYGRTM IEFTKSEVEK
KYTKANGYKE DAVVIYGDTD SVMVKFGVKT LEESMELGKE AAEFVTAKFV KPIKLEFEKV
YYPYLLINKK RYAGLYFTRP DKYDKMDCKG IETVRRDNCP LVSNVMSTCL QKLLIDRDPD
GAINYAKQII ADLLCNRIDI SQLVITKELT KNDYAAKQAH VELAKKMKKR DEGTAPKLGD
RVPYVLCCAT KNTPAYMKAE DPIYVLENSV PIDFNYYLEN QLSKPLLRIF EPILGEKAES
LLLKGEHTRT KAMVTSKVGA LAAFTKKKEK CLGCKTVMPS ETKKALCDHC MKKEGQLYIT
EVFKLRQLQQ NFSRLWTECQ RCQGSLHEEV LCTNRDCTIF YMRKKMGMEL DTQENTILRF
GQPIW
//
