ID F4W6C8_ACREC Unreviewed; 1447 AA.
AC F4W6C8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=G5I_01022 {ECO:0000313|EMBL:EGI70263.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70263.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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}.
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DR EMBL; GL887707; EGI70263.1; -; Genomic_DNA.
DR STRING; 103372.F4W6C8; -.
DR eggNOG; KOG0970; Eukaryota.
DR InParanoid; F4W6C8; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
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; 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; 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; 2.
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 SUPFAM; SSF90234; Zinc finger domain of DNA polymerase-alpha; 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:UP000007755};
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 44..105
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 452..744
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 795..1198
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1235..1413
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 116..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 165423 MW; 690BB3D2C2034B03 CRC64;
MCIAQIVPVE NVMKFGCLTF GKQASTSGRS RRQKIDKTGR LSALERLKEA RSGNKRKYEV
EELENVYDEV DEKEYSNTVL KRQRDDWIVD DGESGYIEDG REIFDDDLDE ESIREARKQR
NSMAGPRKRK KEDNKKKGDI QSMIRNMPSK KDVNVIQIKD DDILGELLSE ISTNKKTTSS
PKLGSNRNKF CHTVHSNITQ TYQASSMNQK EADKIISEKL VTIVSNFDNI PQSESQIIED
DDDMTLFDAP QKKSTSKPVE LNNYSKIEEN SKSEDQSTKK SMESNKQSAS QIIEEENTPI
MDLSECVEDL STIDFDDGSM DTDFSSSINN VKSQKIDVKT PEIGVKIPAH KTSIKSMKIG
NAIDLTEVAP QLVKTKDEEE VFRFYYLDAY ENPYKNPGTV YLFGKTYVSS HDTYCSCCVM
VHCIPRRIYL LPRKYIKNTE SQLTTMEDVY KEFDEYANKM RIMEFNCKEV KKHYSFEKEG
TPKTSDYLEV RYNARYPAID SNYSGPAIEH VFGTTVNALE LLLIERKIKG PCWLDIKNIS
PTAGRFAWCP QIVVTSDMNN ISLCSQEKAK PPMVIATINV RMSLNAKLQN EVVMVVVLIH
HKYNVDKEPP KPPYERQFCF VTRPRDTPWP RQIRDAFLKV PNTEVIKCET ESDLLEELLT
LIQKVDPDLI IGYDCAFQFD VLMQRMFTLK VSNWNRMGRL KSSTPPLLRG KIILNQAFVG
RPVCDIQVSA KELNLKVRSY DLQSLCSAVL KTKEHEYKEI TPAETPLFFN TADKVLNLMH
VTLKEAKYII TIVMDLNVIP LALQITCLAD GPRRKAAAYT GGLVLEPKKG FYDKLVLLMD
FNSLYPSIIQ EYNLCFTTVP GAAYTDVEQL TIPESNLEPG VVPTEIHKLV KSRQQIKQLM
KTQKNLSPAQ KMDYHIRQMA LKLTANSMYG CLGATHCRFY AKGLAALITA KGREILEDTK
HLVEKLQYEV IYGDTDSLMI NTNILEYDDV FLIGKKIMRE VNNRYKKVEL DIDGVFRYLL
LLQKKKYAAV MMSKIDGQIQ LTQEHKGLDI VRRDWCPLAC DTGKKILDIL LCDQSSETRL
EQVVQILQNV AKSVKEGTTP LSSFVITKQL SKNPDAYPDK KQLSHVMVAL RLNKAGGRMW
KAGDTLPYVI CKDETNASAT ERAYHIDEVK NSEKLKVDVN YYLLSQIFPV VLRICEPIEG
IDDVFLANNL GLQFIYKPKT ISCEATLNLP LAINDDRFNN CLPLTFKCKN ERCNTEIIIK
DTVTEFHSGR QLSLSMCPNQ DCKLPPWKYA NVIQNVVQLA MRKAITKYYN GWLECENPLC
SNRTRRLPLD FTKKFPDCSM CKDVSMNRVY SGTDLYNQLY YYHKMFDITQ PAYKHLLSQC
SRDMIAAYNT LKEAIDRQLK RNKFSCVNIT GIFSSASANS AGMFVNHGTW EDFDELGDIS
DDTDKEV
//
