ID H8XP38_FLAIG Unreviewed; 948 AA.
AC H8XP38;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 ECO:0000313|EMBL:CCG52305.1};
GN OrderedLocusNames=KQS_01560 {ECO:0000313|EMBL:CCG52305.1};
OS Flavobacterium indicum (strain DSM 17447 / CIP 109464 / GPTSA100-9).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1094466 {ECO:0000313|EMBL:CCG52305.1, ECO:0000313|Proteomes:UP000007599};
RN [1] {ECO:0000313|EMBL:CCG52305.1, ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RX PubMed=22582381; DOI=10.1128/JB.00420-12;
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.F., Touchon M.,
RA Duchaud E.;
RT "Complete Genome Sequence of Flavobacterium indicum GPSTA100-9T, Isolated
RT from Warm Spring Water.";
RL J. Bacteriol. 194:3024-3025(2012).
RN [2] {ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.-F., Touchon M.,
RA Duchaud E.;
RT "Complete genome sequence of Flavobacterium indicum GPTSA100-9T, isolated
RT from warm spring water.";
RL Submitted (MAR-2012) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; HE774682; CCG52305.1; -; Genomic_DNA.
DR RefSeq; WP_014387449.1; NC_017025.1.
DR AlphaFoldDB; H8XP38; -.
DR STRING; 1094466.KQS_01560; -.
DR KEGG; fin:KQS_01560; -.
DR PATRIC; fig|1094466.5.peg.307; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_10; -.
DR OMA; NRPPMPD; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000007599; Chromosome.
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:SF27; DNA POLYMERASE NU; 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|RuleBase:RU004460};
KW DNA repair {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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000007599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..265
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 354..535
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 705..912
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 948 AA; 107728 MW; A0E7DF458FEAF569 CRC64;
MSQKRLFLLD AYALIFRGYY AFIKNPRINS KGMDTSAIMG FMNSLMDVIR REKPDHLAVA
FDKGGSDYRL EMFTEYKANR DETPEAIKIA VPYIQELLRA MHIPIIEEAG YEADDLIGTL
AKQAEKQGYK VFMVTPDKDF GQLVSENIFM YRPARMGNDI EIWGVDEVKA KFEVEHPLQV
IDFLGMMGDA VDNIPGLPGV GEKTAKKLLA EFGSMENLLE NTDKLKGALK EKIEANKEKG
ILSKKLATIL LDCPVTFNET DYELSKPDVE KTDAIFQELE FRQMKAQFDK LFGSGKEYDE
IDTNGTDTNL ITKKAPIKKA PENQMDLFGF SDDESDEPKG HSFYATLETT NHFYQIVQGE
IPTRLLIQNL MTQKSVCFDT ETTGIDALNA ELVGMSFSWE KGKAFYVPFP ENQEEAQQLA
NKFKPFFENE AIEKIGQNMK YDLKVLRNYG LEVKGSLFDT MIAHYLINPD MRHNMDVLAE
TYLKYSPKSI ETLIGKKGKG QKSMRDVALE DIKEYAAEDA DITLQLKENF QPILEKVGTK
KLFDEIEIPL VQVLADMEAE GIRLDVDFLK EMSKEMAIEI QLLEQKIYET AGETFNLASP
KQLGDILFDK LKIGGAKQKK TKTGQYATGE EILSYLANDH EIVRNILEWR QMVKLQSTYI
DALPNQVDAK TQRVHTDYMQ TVAATGRLSS NNPNLQNIPI RTERGRQIRK AFIARDENYT
LVSADYSQIE LRIIAALSGE ENMIKAFQNH EDIHKSTAAK VFNVPLEEVT KEQRSHAKTV
NFGIIYGVSA FGLSNQTNLS RKESAELIEA YYQNYPKLKS FMSHQVDFAR EHGYVETISG
RRRYLKDINS ANAIVRGGAE RNAVNAPIQG SAADIIKIAM INIHKRLKQE NWQSKMLLQV
HDELVFDVHN SELEKIQPMI KHEMENAFIM AVPLEVEIGL GKDWLAAH
//