ID A0A1N6JMG3_9BACT Unreviewed; 938 AA.
AC A0A1N6JMG3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=SAMN04488055_4175 {ECO:0000313|EMBL:SIO45480.1};
OS Chitinophaga niabensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=536979 {ECO:0000313|EMBL:SIO45480.1, ECO:0000313|Proteomes:UP000185003};
RN [1] {ECO:0000313|EMBL:SIO45480.1, ECO:0000313|Proteomes:UP000185003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24787 {ECO:0000313|EMBL:SIO45480.1,
RC ECO:0000313|Proteomes:UP000185003};
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 -!- 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; FSRA01000002; SIO45480.1; -; Genomic_DNA.
DR RefSeq; WP_074241545.1; NZ_FSRA01000002.1.
DR AlphaFoldDB; A0A1N6JMG3; -.
DR STRING; 536979.SAMN04488055_4175; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000185003; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000185003};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..264
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 345..526
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 695..902
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 938 AA; 104513 MW; 62FD0DEAE90C604C CRC64;
MSKKLFLLDA MALIYRAYYA LIRSPRLTSK GRNTNAQFGF TSTLLDLLNK EKPTHIAVAF
DTHAPTERHT DFADYKANRE EAPEDIISSI PDIKRIIEGF NIPVLELDGY EADDIIGTVA
WQAAAQGYEV YMVTPDKDYG QLVKDNIFIW KPPALGNKEE ILGPKEVCER WQIKDVSQVI
DILGLMGDAV DNIPGIPGVG EKTAMKLLAE WGSLENILAN ADKIPGKMGE KIKAGTESAI
LSKKLATIIT NVPVDFHEEN FCCTEVNKEA LTEIFAELEF KTLGKRILGD GFNAIGGEAK
PVQQDLFGNA TASPAESLAA SAEAIESVAV GLVADKNIDN TPHTYHLADT PEKHAELIAV
LMKEPEISFD TETTGTDANA VEIVGMSFAV KPGEAWYVPL PPDQFVVKEV LEKFRQVFER
EDALFIGQNT KYDMIVLKWY GIEVKGKLFD TMLAHYLIEP EGRRSMDLLS AQYLQYAPVS
IETLIGKKGK GQGTMRDVEI EKIKEYAAED ADITLQLKSK FKPLVTEKEV EKVFYEVENP
LVKVLTDMEY EGIAIDMKAL ADYSKELETD IRKSEESVYQ QAGVRFNLAS PKQLGEVLFD
KLQLDPKAKK TRTGQYATGE DVLTKLASKH PIVDSILAFR ELSKLKSTYV DALPLMLNPR
TNRVHTSFNQ AVAVTGRLSS NNPNLQNIPI RTERGREVRK AFVPKSEEYT LLSADYSQIE
LRIIAAISED ANMMEAFRSG LDIHTATAAK VYGVDIADVS SDMRRNAKSV NFGIIYGVSA
FGLSENLGIA RGEAKMLIDN YFAQYPNIKK YMEDQVKFAQ KTGYVQTLLG RKRWLKDINS
SNAVVRGFAE RNAINMPIQG TAADMIKLAM ISLHKTFRDH NFKSKMILQV HDELVFDAHL
DEVEIIKPLI IEGMRNAMPL AVPVEAEIGT GKNWLEAH
//
