ID E9RHQ4_GYNFI Unreviewed; 1091 AA.
AC E9RHQ4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, 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=DPD1 {ECO:0000313|EMBL:BAJ78758.1};
OS Gynaikothrips ficorum (Cuban laurel thrips).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Thysanoptera; Tubulifera; Phlaeothripoidea;
OC Phlaeothripidae; Phlaeothripinae; Gynaikothrips.
OX NCBI_TaxID=59752 {ECO:0000313|EMBL:BAJ78758.1};
RN [1] {ECO:0000313|EMBL:BAJ78758.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=O-26 {ECO:0000313|EMBL:BAJ78758.1};
RA Su Z., Ishiwata K.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAJ78758.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=O-26 {ECO:0000313|EMBL:BAJ78758.1};
RX PubMed=21075208; DOI=10.1016/j.ympev.2010.11.001;
RA Ishiwata K., Sasaki G., Ogawa J., Miyata T., Su Z.-H.;
RT "Phylogenetic relationships among insect orders based on three nuclear
RT protein-coding gene sequences.";
RL Mol. Phylogenet. Evol. 58:169-180(2011).
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; AB598718; BAJ78758.1; -; mRNA.
DR AlphaFoldDB; E9RHQ4; -.
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 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 156..464
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 529..958
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 996..1069
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 123304 MW; 8A9660AEAEB9CF64 CRC64;
MSNKRKPPPS KTNGTSKKPR VENEDDDAPG TFEDELAFMV QNGDFDTDVL MGEGPDTHQT
SNKWSRPALP SLRPSDDNLV FQQIDVDHYT GQPLPGMPGA KVGPVPVMRL FGVTSSGNSV
CCHVHGFTPY FFVSAPPNFT NPNCHDFQKA LSKAIMADMK GNKDNVTEPV LAVEIVRKQN
LYGYHGDDMH NYLKITLALP RLIAPAKRLL ERGGVYPADG GHAYTAFECN IDFDIRFMVD
THMVGCSWVE LPAGSWTIRQ PHGSLPIVSR CQLEVDVAYD KLISHQPEGE WSKVAPFRIL
SFDIECAGRK GIFPEPNHDP VIQIANMVIR QGEADPFIRN VFTLDTCAPI VGCQVISCKT
EAEMFTKWSD FVREVDPDIF TGYNIGNFDF PYLINRAEHL KVKPFPFLGR IKNIQSVVKE
SQFFSKQMGR RENKSINTEG RVAFDLLLIL VRDYKLRSYT LNSVSYHFLQ EQKEDVHHSV
ITDLQNGTPQ TRRRLAVYCL KDAYLPIRLL EKLMCIINYM EMARVTGVTL ASLLTRGQQI
KVMSQLLRKA REKDFIMPTY QSTGGDDQYE GATVIEPKRG YYADPISTLD FSSLYPSIMM
AHNLCYTTLL LGNAKERLGL SADQYSKTPA NNFFVKPSVR KGLLPEILDD LLSARKKAKS
DLKNEKDPFK QRVLDGRQLA LKISANSVYG FTGAQVGKLP CLEISGSVTA YGRTMIEQTK
TNVEEKYRIE NGYKHDAVVI YGDTDSVMVK FGVKTLEEAM ELGREAAEFV TSKFIKPIKL
EFEKVYFPYL LINKKRYAGL YFTRPDKYDK MDCKGLETVR RDNSPLVANM MNTCLQKLLI
DRNPDDAVAY AKSVISDLLC NRIDISQLVI TKELTKSDYA AKQAHVELAA KMKKRDPGNA
PKLGDRVPFV LISASKGTPA YMKAEDPIYV LENSIPIDFS YYLENQLSKP LLRIFTPILG
DKAESILLRG DHTRTRAVMT SRVGALSAFT KKKETCLGCK AVLPNGQENN PLCQHCAKDG
AKLYLTQLQR YRSMEERFSR LWTECQRCQG SLHEEVLCTS RDCPIFYMRK KVQMELISQD
KNIQRFGCPS W
//
