ID A0A1X7GHM4_9SPHN Unreviewed; 1080 AA.
AC A0A1X7GHM4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN06295910_1784 {ECO:0000313|EMBL:SMF69900.1};
OS Allosphingosinicella indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Allosphingosinicella.
OX NCBI_TaxID=941907 {ECO:0000313|EMBL:SMF69900.1, ECO:0000313|Proteomes:UP000192934};
RN [1] {ECO:0000313|Proteomes:UP000192934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dd16 {ECO:0000313|Proteomes:UP000192934};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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}.
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DR EMBL; LT840185; SMF69900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7GHM4; -.
DR STRING; 941907.SAMN06295910_1784; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000192934; Chromosome i.
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 CDD; cd07434; PHP_PolIIIA_DnaE2; 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; 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 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.
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:UP000192934};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 5..84
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1043..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 120710 MW; 977A081EF1543C47 CRC64;
MTGFAELVAA TNYSFLRGAS HPSDMVGQAI DLGYAGIGIA DRNTVAGVVR AWAALREKNE
EARHLFGHGV DLKLIVGARL VFSDGTPDIV AYPANRRGWG HLCRMLTQGN RRAAKGDCLL
TLADLVEYGD DLLLIAMADD ADEDVLRRLL WRARGSLWLG ATMPCNGDDR RRLKRQEALA
DRLGIPLIAT NDALYAEAGD RPLQDVVTCI RAGVTVRQAG RRLLANAERH LKSPDEMARL
FRDAPAAIAE TLAFLARVEF DLSQLQYEYP HEPVPEGWEP QEWLEHLVRT KLPERYPDGL
TAAGEHKLQT EFDLIRAKNY AYYFLTVHDV VAHACKEGIL CQGRGSAANS IVCYVLGVTA
IDPIKEKLLF TRFLSEERDE PPDIDVDFEH ERREIVMQYI YDRYGRDRAG IAATVIHYRP
RSAVREVAKA LGISEDVVQR LTGTVWGSFS GSMEPERYQQ AGIDPGNSEI VRLRALVDRL
LNFPRHLSQH VGGFVLTEGR LDEMVPIHNA AMPDRTFIEW DKDDIDALGL MKVDILALGM
LTCIRKAFSL LREWGAGDYA LHTIPQDDPD TYAMLQKGDS IGVFQVESRA QINMLPRLKP
KELYDLVIQV AIVRPGPIEG DMVHPYLRRR AGKEKVEWPS PNPPHDPNEL REVLGKTLGV
PLFQEQAMNL AITAAEFSNA DANRLRHSMA TFRNVGKMER FEEKLVEGMV RRGYARDFAE
RCFKQIEGFG SYGFPESHAQ SFAILVYASS WIKCHHPAIF ACAILNSQPM GFYAPAQLVR
DAREHDVDVR PIDVNCSGWD HSIERADDGV LALRLGFRLI GGFREEWAAS IAAAREAKPF
ASIEQLARAA RLPSRALRLL ADADALQSFG MGRRDALWEV RRTPKGSLPL FDHADARELG
EEPDAHLPAL EAWEEVTTDY QTTRLSLNGH PMQFLRPLFR AEGVLSCQEI GGARNGRIVR
TAGVVLVRQR PGKGNAIFVT LEDESGIANV LIWARLFESF RREVMAARLM LVEGEVQRSE
EGVVHLMARR IVDRTSELNG LMLENTLKPP PPGSPDPRSA ASLGGHPRNV RIVPPSRDFH
//
