ID A0A1Y0MI27_9FLAO Unreviewed; 949 AA.
AC A0A1Y0MI27;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BTO05_10125 {ECO:0000313|EMBL:ARV09975.1};
OS Winogradskyella sp. PC-19.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=754417 {ECO:0000313|EMBL:ARV09975.1, ECO:0000313|Proteomes:UP000195547};
RN [1] {ECO:0000313|EMBL:ARV09975.1, ECO:0000313|Proteomes:UP000195547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC-19 {ECO:0000313|EMBL:ARV09975.1,
RC ECO:0000313|Proteomes:UP000195547};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-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}.
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DR EMBL; CP019332; ARV09975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0MI27; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000195547; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000195547};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 5..265
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 356..537
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 706..913
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 296..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 568..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 107104 MW; 92FF0F2BD3C8D3ED CRC64;
MSDQKRLFLV DAYALIFRGY YAFIKNPRIN SKGEDTSAIM GFMNSLLDVI KRERPDHLAV
CFDKGGSVDR VEMFEAYKAN RDETPEGIKT AIPYIHNILK AMHIPIMVKE GFEADDVIGT
LSRQAEKEGY KVYMVTPDKD FAQLVTDNIF MYRPVFGGGY ETWGIPEVQK KFEVTDPMQV
IDYLGMMGDA SDNIPGLPGV GPKTAKKFLA AYGSMEGLLA NTHELKGKMK EKVEANGELG
LLSKKLATIM LDVPVDFDAK DFELDHPDIE KVKEIFQDLE FRRLTDNFLK TFSTEVPTAN
SSSTTTETKT EVKATPKEQK SAGAGQFSLF GGDTSTSDET TSEYTRHTVE TSSHFYQSIA
PGMATKLFVK NLMNQTSVCF DTETTGLNPL TAELVGIAFS WETGKGFYMP FPEDKNKAQN
LIEELRPFFE NENIEKIGQN LKHDIKVLAK YNIDVKGKLF DTMLAHYLIN PDMRHNMDVL
AETYLNYKPI SITELIGKKG KNQLSMRDVP LDKQTEYAVE DADITLQLKE HFEKELGEAN
TQKLFNEIEL PLLRVLADME LEGINLDKDF LNSLSEDLNN DIQTLEKRIY EAAGEEFNIG
SPKQLGIILF EKMKLVDKPK KTKTGQYSTA EDVLSYLAKD HQIIKDVLDY RGLAKLKSTY
VDALPLQVEE STMRVHTDYM QTVAATGRLS SNNPNLQNIP IRTERGRQVR KAFVPRDENY
TLLAADYSQI ELRIIAALSE EETMIEAFKN GEDIHASTAS RVFNAPITEV SREQRSNAKT
VNFGIIYGVS AFGLSNQTDL SRGEAKELID TYYETYPKLK AYMSKQVDFA RDNGYVQTVL
GRRRYLKDIN SRNAVVRGAA ERNAVNAPIQ GSAADIIKIA MINIHNKLKA SDYKSKMLLQ
VHDELVFDIY KPELDAMKTL IKTEMENAYK LSVPLDVDLD IGDNWLEAH
//
