ID A0A1H7B4C2_9MICO Unreviewed; 1136 AA.
AC A0A1H7B4C2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05421637_2702 {ECO:0000313|EMBL:SEJ69282.1};
OS Demequina mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Demequinaceae;
OC Demequina.
OX NCBI_TaxID=1043493 {ECO:0000313|EMBL:SEJ69282.1, ECO:0000313|Proteomes:UP000183315};
RN [1] {ECO:0000313|Proteomes:UP000183315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24868 {ECO:0000313|Proteomes:UP000183315};
RA Varghese N.;
RL Submitted (OCT-2016) 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; FNZI01000009; SEJ69282.1; -; Genomic_DNA.
DR RefSeq; WP_042215559.1; NZ_FNZI01000009.1.
DR AlphaFoldDB; A0A1H7B4C2; -.
DR STRING; 1043493.SAMN05421637_2702; -.
DR eggNOG; COG0587; Bacteria.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000183315; 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 CDD; cd07431; PHP_PolIIIA; 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:UP000183315};
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"
SQ SEQUENCE 1136 AA; 122653 MW; 387F7B6C5087631B CRC64;
MTDVPEYAEL HSHSAFSFLD GASQPEEMAA EAGRLGLSAL AITDHDGLYG AVRFAGAARE
IGLPTVFGAE LSLAVEGPGG PPVLDPPTGV PDPRASHLVV LARGASGYSR LSHAIGMAHL
ATGEKGMARY TLESLAEAGG GDLLVLTGCR KGPVRAALTG LGGAGLGGGA RRAGADALAG
GISREGYAAA RGELDRLVAL FGREGVAVEI TDTGSPYDSE VNAALADLAF DASLPLVATT
NAHYATPRDA DLAGALAAVR ARSSLDDMDG WLPGSPGQHL RSAGEMAFRH RRHPQAVATA
ARLGAECAFD LDLVAPNLPP YPVPPGHTEA TWLRELTYRG ARERYGPPDA ERVPGAWRQI
EHELTVIEAL DFPGYFLIVQ DIVAFCRRSD ILCQGRGSAA NSAVCFALGV TAVDAVTHGL
LFERFLAPER DGPPDIDVDI ESDRREEVIQ YVFQRFGRIN AAMVANVIQY RPRSAVRDAA
RALGFDVGQQ DAWSKSIDRW SALRVPPEKQ EEWAAKQRDA MWPEPPPAQE LDHIPENVLD
LADRFMRLPR HLGIHPGGMV LCDRPVIDVC PVEWARMPGR TVLQWDKDDC ADAGLVKFDL
LGLGMLSALK YAFRYMQEVR GEDLGLHSLP QEDPAVYDLL CAADTVGVFQ VESRAQMATL
PRLRPRRFYD IVIEVALIRP GPIQGGSVHP YINRARGREE VTYLHPLLER SLGKTLGVPL
FQEQLMQMAM DAAGFDGALA DQLRRAMGSK RSPERMEALR ARFMVGANER GITAEVAHQI
FDKLKAFSDF GFPESHSFSF AYLVYASSWL KVNRPAAFYA GLLAAQPMGF YSPQSLAADA
RRHGQAILRP CVVRSEALAR VEKLEAPFPT PEEVREDMAR LVHVDPLLGV RMGLGAVRGL
GDDAAAAIVA AREERPFADL HDMARRVRIR PKGVSGQAGL APEKGLTTAQ WEALATAGAL
ERLGVTRREG LWASGVLSRE GPDTLPGTVP GAQAPMLPGM SVVEEAVADV WASGVSVEGY
PTRFVREGLD KAGVLRVAEV LTHEAERRVT VAGVVTHRQR PGTARGVTFI SLEDETGFLN
VICSVGVWKR FQAVARRSPA LIIRGRIERA DGATNLVAEH LSPLSLKVPS KSRDFR
//
