ID I8I5H3_9GAMM Unreviewed; 937 AA.
AC I8I5H3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=WQQ_18330 {ECO:0000313|EMBL:EIT71696.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT71696.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT71696.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT71696.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(2012).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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 ECO:0000256|RuleBase:RU004460};
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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:EIT71696.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKGD01000001; EIT71696.1; -; Genomic_DNA.
DR RefSeq; WP_007184782.1; NZ_AKGD01000001.1.
DR AlphaFoldDB; I8I5H3; -.
DR STRING; 1172194.WQQ_18330; -.
DR PATRIC; fig|1172194.4.peg.1773; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000003704; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00593; pola; 1.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000003704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 8..262
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 329..516
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 685..891
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 937 AA; 103135 MW; 016A98245111DBD8 CRC64;
MAETAAEHPL ILIDGSSWLF RAFHALPPLS NSRGEPTGAV YGIVNMLKRL CREYEPQRIC
VVFDPSGPVF RNELYADYKA NRDETPAELS AQYPDVVAVI KALGFPLLVV DGVEADDVIG
TLTRQGRERG LPVLIVTSDK DMAQLVDEHV HLLDTMKNRR MDRAGVIEKF GVPPERIIDY
LALVGDTVDN IPGVPGVGPK TAAKWLTEFG SLDAIRDRSG EIGGKIGEKL RAALDILPLS
HRLATIICDV ELPVQLDELV PGERDVEQLV ALYRKLEFHR WREELEGGKP AAGPATEAGA
ELESAAPESL AAVGANAADI GTVSKPTDAI CVVDEAELDR MIGCLERAGL ICFDTETDAL
DANQAGLVGL AFSVESGSGW YVPLAHNYLG APEQLPLQHV IARVKPLLED QSKPKLAQHG
KYDINVLARY GIEVRNLRFD TMLESYVLDA AGNRHDMDTL ADKYLGHKTI QFADVAGKGK
NQLTFNQVAL DKATEYSAED ADITLRLHET LYPKLEAEPV LAKVFHEIEM PLVPVLARIE
RRGVKVDAPL LRKISAELAQ RMDELQAQAF VVAEGEFNLG SPKQLQALLY EKFQLPVLAK
TPKGDPSTAE DTLEQLAAQH PLPRLILDWR AMQKLRSTYA EQLPAAINPR TGRIHTSYHQ
AVAATGRLSS QEPNLQNIPI RTAEGRRIRQ AFIAEPGNTL LAVDYSQIEL RLMAHFSGDE
RLREAFRQNL DVHQATAAEV FGLPLEKVGS DERRAAKAIN FGLIYGMSAF GLARQLGIGR
NEAGEYIERF FGRYPGVKQF MDDTRSAARS RGYVETLFGR RLYLPNINAR NQGLRQYAER
TAINAPLQGT AADLIKKAMI DLQAWLDANA PGISMIMQVH DELVFEGPEA LLREKAQTIA
DHMVRIAPLA VPLVADFGLA GNWDEAHQPH GHARSTG
//
