ID A0A3A9ZRN3_9ACTN Unreviewed; 1127 AA.
AC A0A3A9ZRN3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D7223_03375 {ECO:0000313|EMBL:RKN50803.1};
OS Micromonospora endolithica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN50803.1, ECO:0000313|Proteomes:UP000281726};
RN [1] {ECO:0000313|EMBL:RKN50803.1, ECO:0000313|Proteomes:UP000281726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN50803.1,
RC ECO:0000313|Proteomes:UP000281726};
RX PubMed=15046305; DOI=10.1078/072320204322881781;
RA Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT Micromonospora endolithica sp. nov. and two isolates related to
RT Micromonospora coerulea Jensen 1932.";
RL Syst. Appl. Microbiol. 27:166-174(2004).
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:RKN50803.1}.
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DR EMBL; RBAK01000001; RKN50803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9ZRN3; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000281726; 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 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:UP000281726};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 78..145
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 122674 MW; 9A2ACA4A57F19D77 CRC64;
MSFHNPKQPW SELERVLSGR GSGGGRSGGT SRDERHLHVV DPLAVDADGG DAPAWTRKRQ
PYEAPELPRP DDGAVPYAEL HAHTNFSFLD GASHPEELAE EAARLGLTAL AVTDHDGFYG
VVRFAEAARE LHLPTIFGAE LSLGLPGPQN GEPDPLGAHL LVLAHGHEGY ARLASVISRA
QLRGGEKGRP VYGELEEVAA ELRDHVLVLT GCRKGHVPGA LLTEGVDAAA RELDRLTALF
GAETVAVELT DHGHPVDADR NDALAELAAT AGLPTVATNN VHYATPGRRR LATTVAAVRA
RRSLDEIDGW LPAAATAHLR GGAEMAVRFA AYPGAVARAA EFGAELAFDL QLVAPTLPAY
PVPPGHTEMS WLRHLTEQGA RERYGPREAH PRAYAQLDHE LRMIDELGFP GYFLVVYDIV
AFCRAQDIYC QGRGSAANSA VCYALRITNV DAVRHRLLFE RFLAPERDGP PDIDVDIESD
RREEVIQHVY ARYGREHTAQ VANVISYRPR SAVRDVAKAF GFSPGQQDAW SKQIDRWGSV
AAVDVEDIPE QVVAYANELQ TFPRHLGIHS GGMVICDRPV IEVCPVEWGR MPGRSVLQWD
KDDCAAVGLV KFDLLGLGML SALHYGYDMI GASLDLGDMT LDDPEVYDML CRADSVGVFQ
VESRAQMATL PRLKPREFYD LVVEVALIRP GPIQGGSVHP FIRRKNGQEP VEYAHPLMRN
ALEKTLGVPL FQEQLMQLAI DLAGFDAAEA DQLRRAMGAK RSAERMARIA ERLYAGMAER
GITGELADDV YRKLSAFASY GFPESHAMSF AYLVYASSWL KRYHPGPFLA ALLNAQPMGF
YAPQTLVDDA RRHGVEVRRP DVNASGARAV LESTPRTRWG SVPGEPPHAW GLGGPAVRLG
LSSVRTLGDD VAERIEAERT AHGAYRDMPD LARRVGLTAA QLEALSTADA FACFGLSRRQ
ALWAAGAAAQ DRPGRLPGTV TGTTAPPLPG LEAVDRLMAD VWATGLSPES HPARFLRPRL
DALGAVPIAR LPRVEPGRRI RVGGIVTHRQ RPATAGGVTF LNLEDETGML NVTCSPGLWE
RYRRVARTSA ALVVRGLLQR HEGVINLTAD RLDAIEPPVS PASRDFR
//
