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Database: UniProt
Entry: C0W389_9ACTO
LinkDB: C0W389_9ACTO
Original site: C0W389_9ACTO 
ID   C0W389_9ACTO            Unreviewed;      1110 AA.
AC   C0W389;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Error-prone DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01902};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01902};
GN   Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN   ORFNames=HMPREF0058_0333 {ECO:0000313|EMBL:EEH66806.1};
OS   Actinomyces urogenitalis DSM 15434.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=525246 {ECO:0000313|EMBL:EEH66806.1, ECO:0000313|Proteomes:UP000004778};
RN   [1] {ECO:0000313|EMBL:EEH66806.1, ECO:0000313|Proteomes:UP000004778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15434 {ECO:0000313|EMBL:EEH66806.1,
RC   ECO:0000313|Proteomes:UP000004778};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) 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|HAMAP-Rule:MF_01902}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC       subfamily. {ECO:0000256|HAMAP-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:EEH66806.1}.
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DR   EMBL; ACFH01000015; EEH66806.1; -; Genomic_DNA.
DR   RefSeq; WP_006549637.1; NZ_DS999576.1.
DR   AlphaFoldDB; C0W389; -.
DR   STRING; 103621.GCA_001067145_01539; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_11; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000004778; 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: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   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; 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   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:UP000004778};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01902}.
FT   DOMAIN          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1110 AA;  119861 MW;  6960BA6F34396A3F CRC64;
     MFESSYAELH SHSAYSFLDG ANEPEDLAAA AAELGLTALA LTDHDGMPGI VRHAQAGRAL
     GLPTVHGTEL TMSDGAHLPV LARSPEGYRH LVSAISQHNL QAGRRQEPAH RLEDLAQALR
     GGTGMAAPSS CLVLTGTARG PLRRALGDPA RPHTWDTQAA DICLGRMVEL LGADGVAVEI
     TLNGGPTDAA LTRMLTRLAA SHRLPVLATG AVRCARPADS RLADVLTATR LGTDLEGARG
     HLPAIGRWLR SGAEMARLHR RAPQAVGVTA ELAADLAFDL ALVAPDLPAA QVPPGHTPAS
     WLRELTRQGA LLRYGTREQD PHAWQVLDHE LEVIESLGFP GYFLIVRSIV EFCEESGILC
     QGRGSAANSA VCYALGITAV DAVRHKMLFE RFLSPGRAGY PDIDLDIEAC RREEVIQHVY
     TRYGRHRAAQ VANVISYRPR SAVRDAARAL GYPAGLQDAW ARSIEHGWSR EQDGQAREDA
     VPEQVLDVAD RLLRLPRHLG VHSGGMVLAA QPVTEVCPVR WAAMEGRSVL QWDKDDCAAA
     GLVKFDLLGL GMLTALRLAF TSLGDRGEKV PDLTSRQGDG ILRPAQVGRP WGLHTLPEED
     PAVYRLLQAA DTIGVFQVES RAQMATLPRL RPRVFYDIVV EVALIRPGPI QGDAVNPYIR
     RRLGREEPDY LHDLLRPALE KTLGVPLFQE QLMQIAVDAA GFSPVEADAL RQAMGAKRSV
     ERMEALHLRL VEGMKERGIS QGTAELVFDK LRAFADFGFP ESHAFSFAYL VYASAWLKVR
     RPEDFYAGVL AAQPMGFWSP QTLVADARRH GVQVLAADVS HSEVQASVET VRPGAPSQAC
     VGGAGEEAST ALTHLDTHRD LAVRLGLAPI KGIGRELAER IVTERQSHGA YRDVADLARR
     VRLGRKHLET LAAAGALASL GVSRRQALWS AGVLADEHGR PHLGHRTGGD RTPWCQPPLP
     GTAVGSRAPD LPEMSAQERH VADLRLTGVS TETHPLAFLR TALAEDGVVE VVRVGQQGNG
     AQVRVAGVVT HRQRPYTAAG TVFLNIEDET GLLNVICSSG MWKRYRHVGR RATAVVVWGV
     VESADGVTAL RAQSLQGLEG VVSTGSRDWA
//
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