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Database: UniProt
Entry: A0A1W2DHV5_9SPHI
LinkDB: A0A1W2DHV5_9SPHI
Original site: A0A1W2DHV5_9SPHI 
ID   A0A1W2DHV5_9SPHI        Unreviewed;      1058 AA.
AC   A0A1W2DHV5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=SAMN04488524_3830 {ECO:0000313|EMBL:SMC96984.1};
OS   Pedobacter africanus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=151894 {ECO:0000313|EMBL:SMC96984.1, ECO:0000313|Proteomes:UP000192756};
RN   [1] {ECO:0000313|Proteomes:UP000192756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12126 {ECO:0000313|Proteomes:UP000192756};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC       subfamily. {ECO:0000256|ARBA:ARBA00007391}.
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DR   EMBL; FWXT01000003; SMC96984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2DHV5; -.
DR   STRING; 151894.SAMN04488524_3830; -.
DR   Proteomes; UP000192756; 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-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192756};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          17..84
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1058 AA;  119898 MW;  47439A4353A91361 CRC64;
     MVYTWIFCLE EPLMQYTELQ VTTNFSFLRG GSHPEELVKQ AAALGHKEIA ITDRNTLAGI
     VRAHVAARGK NIRVIPACHL ELLDGPPLLA YPTDRAAYSR LSTLLSEGNL RAEKGQCHLY
     KADVYRYAEG IKFIAIAPIN LNSGFDFDPE FKQALKTYRW ALGTHLYLAA SRSYQANDGK
     RLFRLSQLSD ELRIPLIAVN DVHYHIPQRR ELQDILTCIR EKCTIYNAGF RLHQNAERYL
     KPIAEMHRLF SQYPQALERT QEIAEACQFS LDSLEYVYPE ELTTEGRNPQ QELVHLTWQG
     AKEKFGNKIP PEICETIRYE LDFMERKNYA AYFLTVYDFV RFARSQNILC QGRGSAANSV
     VCYCLGITSV DPSKFKVLFA RFMSDARDEP PDIDVDFEHE RREEVMQYIY SKYGRDRSAI
     VATVTQVHYR GAVRDVAKVM GLSVDTINRL ASSAWEFTDE WHNGRTVSSE GFDASDPHLK
     KVLELTQQYI GFPRQLGQHT GGFVMTRGKI TDLCPILNAR MENRTCLEWN KDDIEALGFL
     KVDVLALGML TCIRKAFDLA KQHYGLNLTL ANVPQDDPEV YEMISHADTL GVFQIESRAQ
     MSMLPRLRPK CFYDLVIEVA IVRPGPIQGD MVHPYLRRRN GEEPIEYPSK ELETILGRTL
     GVPLFQEQAM EIAIVAAGFT PAEADGLRRS MATFKSHGKV SEWRNKLVSG MVAKGYKEEF
     AQRVFKQLEG FGSYGFPESH AASFALLVYI SSWIKCHYPD VFATALLNSM PMGFYQPAQI
     VIDARKHGVE VRPADVNHSS WDNLLETKSG RYHPIRLGFR QIKGLNEEEM QVLLAARQSP
     FTSIHALLNA GVSLAALERL ADADAFRSLG LDRRQALWEV SALSDSPVGM FEGQVQESRH
     EKEVGLPVMS LSEHVVQDYN STTLSLKAHP LSFVREKLNL LKVLPIRELD QHADGDIVKV
     SGLVLVRQRP GTATGVCFIT IEDETGFANL VVFKKWFDKY RKEILRAKLL MVEGKLQREG
     EVTHVVVTCC SDQSAYLNAL TEVENNGSGI FHEGRNFK
//
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