UniProt: A0A151I399

Database: UniProt
Entry: A0A151I399_9HYME

LinkDB:  A0A151I399_9HYME 
Original site:  A0A151I399_9HYME

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (25)   

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ID   A0A151I399_9HYME        Unreviewed;      1125 AA.
AC   A0A151I399;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=ALC53_05866 {ECO:0000313|EMBL:KYM83690.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM83690.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM83690.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM83690.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM83690.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-2015) 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}.
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DR   EMBL; KQ976484; KYM83690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151I399; -.
DR   STRING; 520822.A0A151I399; -.
DR   Proteomes; UP000078540; 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; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 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:UP000078540};
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          193..498
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          563..992
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1030..1103
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
SQ   SEQUENCE   1125 AA;  128059 MW;  E05BB9A815F16E25 CRC64;
     MYPVPCSNRK KCEIENYRGI YMSRQTLMGE PHHSHASQSA RCFAAYWIAL AFECDEDEEK
     PSSFEAELAI MDLADEDFLD ETLLIGEGPE QENTSAKWSR APPPPLNPKI DTLSFQQIEI
     DHYIGKPLPG MPGSKVGPVP IMRMFGVTEQ GNSVCCHVHG FCPYLFVSAP SNFTNDHCRP
     FKEALNQAVK KDMKSNPNNI QDAILAIELV HKQSMYGYGG NDKLPFLKIT VAVPKLIAPC
     KRLLEQGTVY TAFNYHYRAF ESNIDFDIRF MVDTSVVGCS WIELLPGSWK LRGQYGHMLE
     LTTRCQLEVD VAWDAFVTHA PEGEWSKIAP FRILSFDIEC AGREGIFPEA KHDPVIQIAN
     MVIRQGESEP FLRNIFTLDT CAPIVGCQVL SFEKESLMLE KWADFVRQLD PDIFTGYNIN
     NFDFPYLINR AQHLNVKNFN FLGRIKNIKS VIKDHVLQSK QLGRRENKSI NFEGRVPFDL
     LLVLVRDYKL RSYTLNAVSY HFLQEQKEDV QHKDITGLQN GNAQTRRRLA VYCLKDAYLP
     LRLLDKLMCI IIYMEMARVT GVSISSLLTR GQQIKIVSQL LRKTKENDYL MPVHQGHGTD
     EQFEGATVIE PKRGYYNDPI ATLDFSSLYP SIIMAHNLCY TTLLTIAKKK ELNIQEDQIT
     TTPSKSLFIK NSIRKGILPE ILENLLAARK KAKAELKQET DPLKQKVLDG RQYALKVSAN
     SVYGFTGAQM GKLPCLEISA SVTAYGRTMI EQTKQEVEDH FRIENGYKND ALVIYGDTDS
     VMVKFGVKDI EDAMKLGKEA ADYVTSKFIK PIKLEFEKVY FPYLLINKKR YAGLYFTKPD
     KYDKMDCKGL ETVRRDNCPL VANMMNTCLQ ILLIERNPHA AVDYAKQIIS DLLCNRIDLS
     QLVITKELTK TDYAAKQAHV ELATKMKKRD AGNAPKLGDR VAYVFISAAK GTPAYQKAED
     PVYALQNSIP IDTNYYLENQ LAKPLVRIFE PILGDKAESL LLKGDHTRTR CIATSQVGAL
     AAFTRKKETC LGCKAVLPPD REDKAVCKHC EPQEAELFHN ELQAQHKLEE KFSRLWAECQ
     RCQGSLHQEV ICSNRDCPIF YMRVKSRLDM DAKIKRIKRF GALEW
//

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