ID   DNAE2_SACD2             Reviewed;        1029 AA.
AC   Q21LY9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Error-prone DNA polymerase {ECO:0000255|HAMAP-Rule:MF_01902};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01902};
GN   Name=dnaE2 {ECO:0000255|HAMAP-Rule:MF_01902}; OrderedLocusNames=Sde_1028;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
CC   -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC       translesion synthesis (TLS). It is not the major replicative DNA
CC       polymerase. {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01902};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01902}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01902}.
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DR   EMBL; CP000282; ABD80290.1; -; Genomic_DNA.
DR   RefSeq; WP_011467510.1; NC_007912.1.
DR   AlphaFoldDB; Q21LY9; -.
DR   SMR; Q21LY9; -.
DR   STRING; 203122.Sde_1028; -.
DR   EnsemblBacteria; ABD80290; ABD80290; Sde_1028.
DR   KEGG; sde:Sde_1028; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_6; -.
DR   OMA; NSWPMGF; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000001947; Chromosome.
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   HAMAP; MF_01902; DNApol_error_prone; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR023073; DNA_pol_error_prone.
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   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 1.
DR   PANTHER; PTHR32294:SF4; PTHR32294:SF4; 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; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1029
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_1000073691"
SQ   SEQUENCE   1029 AA;  115435 MW;  32D7E9BDFC895488 CRC64;
     MQYTQLQTLT NYSFLKSASH PQELVEEAKI LGYHALAITD ECSLAGIVKA HVAAKELNLK
     LLVGSYFELT NGFKIIAIAP NRQAYAELSG FISLARRRAS KGEYEAHLSD LRFRLQQCLI
     IWLPYFNNHI SDVDVTTLAT AFKQRLWIGV SHTLIAAEQR LFSHLNKLAN ALHVPLVASG
     LTYMHNKNCK PLLDILTAIR ENTPIQQLGT RLHSNAEVNL KPLHELNQLY PEALIQQTQV
     IAQLCNFSLD ELRYQYPKEL VPSNTTPIAH LKKLVKEGEA KRWPQGTPEH AQKIIAMELG
     LIEEMQYEYY FLTVHDIVHF ARSKNILCQG RGSAANSVVC YCLFITEIAP GQINVLFERF
     ISKERNEPPD IDVDFEHQRR EEVIQYIYQK YGRERAALAA TVITYRSRSA IRDVGKAMGL
     EAGLVGQLAK SLAWWDRTGD LIKRMESFGL NPETQKTMQH FFALVQQILG FPRHLSQHVG
     GFIITQDKVS DLVPLENASM PDRTIIQWDK YDIEAMGLLK VDVLALGMLT ALRKSLETVS
     QYDAAVYSLA TIPREDPATY AMLSKGDSIG VFQVESRAQM SMLPRLRPKC FYDLVIEIAI
     VRPGPIQGDM VHPYLRRRDG IEEVHYQNDK IKSVLEPTLG IPIFQEQAIR LAMVAADFSG
     GEADQLRRAM ASWGKNGSLL KFEDKFIQGM LNNGYPLDFA HRLFEQIKGF GGYGFPESHS
     ASFALLCYAS SWLKCHHPAA FYCALLNSQP MGFYSASQLI QDARRHKVVV LPVEVNASGY
     ESHVVLTNHN TSAPPNIIQL GLHMIKGLSI LTAERIVLAK GDKPFTTLKE LSLRAQLSSA
     DLQLLASADA LHKLTGNRHN SRWQAAALMP HSPLLDGAEL EEDALNTPAP SIEKNIQTDF
     NSTGLSLRLH PMALLRAQQP FNRCKKQSEL ASIHNGGFAQ VAGLVTGRQR PGTAKGTLFL
     TLEDETGNIN IVVWTSTQER CRQALLTAKL LLVKGRLETK DNVTHIIAGQ MFDYSHMLSE
     FDIKSRDFH