ID G9PNC2_9ACTO Unreviewed; 1134 AA.
AC G9PNC2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273, ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=HMPREF0975_01834 {ECO:0000313|EMBL:EHM93545.1};
OS Actinomyces sp. oral taxon 849 str. F0330.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=653386 {ECO:0000313|EMBL:EHM93545.1, ECO:0000313|Proteomes:UP000003600};
RN [1] {ECO:0000313|EMBL:EHM93545.1, ECO:0000313|Proteomes:UP000003600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0330 {ECO:0000313|EMBL:EHM93545.1,
RC ECO:0000313|Proteomes:UP000003600};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces sp. oral taxon 849 str. F0330.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC translesion synthesis (TLS). It is not the major replicative DNA
CC polymerase. {ECO:0000256|HAMAP-Rule:MF_01902}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01902};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391, ECO:0000256|HAMAP-
CC Rule:MF_01902}.
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:EHM93545.1}.
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DR EMBL; ACTB01000102; EHM93545.1; -; Genomic_DNA.
DR RefSeq; WP_009233816.1; NZ_JH470353.1.
DR AlphaFoldDB; G9PNC2; -.
DR STRING; 653386.HMPREF0975_01834; -.
DR PATRIC; fig|653386.3.peg.1708; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_11; -.
DR Proteomes; UP000003600; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01902; DNApol_error_prone; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DnaE2.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR010994; RuvA_2-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01902};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_01902};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01902}; Reference proteome {ECO:0000313|Proteomes:UP000003600};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 851..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 122406 MW; 43EEB239FC8D5A7F CRC64;
MTSRHRYAEL HAHSAYSFLD GANEPDDLAS AAVELGLEAL ALTDHDGVPG IVKHAQAGRA
HGLPTIHGTE LTLADGSHLP VLARNPVGYH RLVSAISQHN LDAGERRDPA HDLPALASAL
RAAPTGQTGG AAGTCLVLTG TANGPLRRAL GDPLRPGTWD LAAAGDCLGR LTDLFAAPDR
GRPSGTSTMA GGAQVEGDAV VGLAVELTLD GGPTDAALTE VLTRLAHDHR LPLVATGAVR
CARPADARLA DVLTATRLVT DLEGARGHLP AIGRWLRGAQ DMARLHRRSP DAIDLAADLA
ADLAFDLSLI APDLPEADVP AGHTPASWLR ELTRQGAVRR YGAPQEHPRV WEVLNHELDV
IESLGFPGYF LIVHSIVEFC RQSGILCQGR GSAANSAVCY ALGITAVDAV RHQMLFERFL
SPGRAGYPDI DLDIEACRRE EVIQHVYSRY GRDRAAQVAN VISYRPRSAV RDAARALGYS
AGVQDSWARQ MDRWTTVRPG GLTGQGDEVP EPVLEIAEKL LRLPRHLGIH SGGMVLCGRP
VTEVCPVRWA AMDNRSVLQW DKDDCAEAGL VKFDLLGLGE LTALRLAFTT LGERGQTVPD
VVEEGELRTS QTGRPWGLHT LPEEDPAVYR LLTAADTVGV FQVESRAQMA TLPRLRPKEF
YDIVVEVALI RPGPIQGDAV NPYIRRRLKR EEVTYLHDSL KPALAKTLGV PLFQEQLMQI
AVDSAGFSPA EADTLRQAMG AKRSIERMEA LHDRLIAGMR GRGIDETTAE KIYSKLRSFA
EFGFPESHAF SFAYLVYASA WLKVRKPEDF YAGVLAAQPM GFWSPQSLVA DARRHGVRVL
PADINRSLSQ ATVEQKGKHQ VAEPPEQWRT LTPHPAAPTP LDVHEDLAVR LGLAPIKGLG
ERAAQAIVAE RRAHGPYRDL ADLARRVSLS RPNLETLAAS GALDSLGVER RRALWAAAVL
SDEHGRRRGA SHQDPGAWFQ PTLPGTVAGA VAPALPAMTS REQQVADLSL TGVSTHGSPL
TLLRPGLSAE GVLTTADLSD QEHGRRVRVA GVITHRQRPH TASGMIFLNL EDETGLLNVV
CRAGMWRRYR SIGRRAGALI VRGTVERGDG VIALMAEHLQ ALPGVPVTGS RDWC
//
