ID A0A1K1RQK3_9GAMM Unreviewed; 906 AA.
AC A0A1K1RQK3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=SAMN02800691_3384 {ECO:0000313|EMBL:SFW74076.1};
OS Luteibacter sp. UNCMF366Tsu5.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1502758 {ECO:0000313|EMBL:SFW74076.1, ECO:0000313|Proteomes:UP000182005};
RN [1] {ECO:0000313|EMBL:SFW74076.1, ECO:0000313|Proteomes:UP000182005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCMF366Tsu5.1 {ECO:0000313|EMBL:SFW74076.1,
RC ECO:0000313|Proteomes:UP000182005};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; FPIS01000004; SFW74076.1; -; Genomic_DNA.
DR RefSeq; WP_072323774.1; NZ_FPIS01000004.1.
DR AlphaFoldDB; A0A1K1RQK3; -.
DR STRING; 1502758.SAMN02800691_3384; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000182005; 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:UP000182005};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 1..255
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 309..496
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 665..870
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 906 AA; 99142 MW; AEF8BB630ECCF4EB CRC64;
MPTLTLIDGS SYLYRAFHAL PPLTNTFGEP TGALFGIVNM LRTTMKAGSD YVAFVCDAPG
RTFRDDLYPE YKANRAAMPD DLRAQIEPMM KIVGALGFPI ICVPGVEADD VIGTLALQAA
DQGIDTIIST GDKDFAQLVS AHIVLINTMT NTTLDIDGVI EKFGVRPEQI VDYLTLVGDS
IDNVPGVEKC GPKTAAKWLA EYGNLDAIFA NADKIGGKIG ENLRAAMPRL PLSRELVTIR
TDVPLEHGPA DLHMRERDVE ALRELYVRYD FKAALKDLDA AQPAPSSPAV VAAVAEPTAP
LPVALEGEYE MVVTEDRLAA WLEKLETAPL IAFDTETTSI DAMQADIVGI SLAVEAGKAA
YIPLAHDYPG APAQLPKEHV LGALKPILED PTRPKVGQHG KYDINVLSHY GIALRGLAHD
TMLESYVFNA TATRHDMDSL ASRYLGYTTI KYEQVAGKGA KQIPFSQVDC DTACRYAAED
ADITLRLHEA LWPKLEAEPS LRNVYADIEI PLVPVLAKME RTGVLIDANV LRLQSQQLGK
RMVELQKQAY ASAGHDFNMD SPKQLQAVLF DELGLAAKIK TPTGQPSTNE EALEAIADTH
ELPRLILEYR GLAKLRSTYT DKLAGIVNPR TGRVHTSYHQ GAVATGRISS SDPNLQNIPV
RTEEGRRIRQ AFIAPEGWRI VAADYSQIEL RIMAHLSNDE GLVRAFREGG DVHRATAAEV
FGVTPDEVTA NQRRAAKAIN FGLMYGMSAF GLARQLGVDR GEASDYMGRY FSRYPGVRAF
MDATREQAHR DGFVQTLFGR RLYLENLKSR NQAFRAGAER AAINAPMQGT AADIIKRAMI
AVAAWIEPRD DVRLLMQVHD ELVFEVREDA VDAIRAGIEE HMTGAAQLSV PLQVDIGVGA
NWDEAH
//
