ID A0A1V3R184_9BACT Unreviewed; 945 AA.
AC A0A1V3R184;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=B0E43_18090 {ECO:0000313|EMBL:OOG70515.1};
OS Algoriphagus sp. A40.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1945863 {ECO:0000313|EMBL:OOG70515.1, ECO:0000313|Proteomes:UP000188460};
RN [1] {ECO:0000313|EMBL:OOG70515.1, ECO:0000313|Proteomes:UP000188460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A40 {ECO:0000313|EMBL:OOG70515.1,
RC ECO:0000313|Proteomes:UP000188460};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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 -!- 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:OOG70515.1}.
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DR EMBL; MUNY01000072; OOG70515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3R184; -.
DR STRING; 1945863.B0E43_18090; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000188460; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 7..268
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 352..533
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 702..909
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 945 AA; 106825 MW; 312E3252A4795E8D CRC64;
MSQKQACKLF LLDAMALIYR AHFAFSKNPR INSKGLNTGV MLGFTNTLLE VLEKEKPTHI
GVAFDTKAPT FRHVQYELYK ANRQDQPEDI TTAIPWVKEI VKAFKIPILE LDGFEADDVI
GTLAKKAEKE MFTVYMMTPD KDYGQLVDDH IFLYKPAFMG NGVDVMGPKQ ICEKWDIDHV
DKVRDILGLM GDAVDNIPGI PGIGEKTAVK LLKEFGTVEG LIANVDKLKG KQRENVENFA
QQGILSKELA TIKIDVPVDF VQEELRYDGF EEEKLKSIFT ELEFRTLAAR IFKEPSSKKA
SISAPAQMDL FGAATAPLAT VSLEREEGEP ESTLEVGPPP ILDTIWANVH NYHKIKGKEE
VAELVTYLQM QKEVCFDTET TDLDAMKAEL VGLSFSYVSG EAYYIPVYED QNQTQEILEI
LRPFFENEAI LKIGQNVKYD MLVLKNYGIE VKGTLYDTML AHYLIEPEGK HSMDWLAQQY
LHYKPVSITE LIGKKGKNQG NMRDVDEDEV TAYAAEDADI TLRLKEKFDP TLKANGLEKL
FDEVENPLIR VLTDMEFEGV RIDTASLAEL SILLEKESKE IEKQVYELAG VRFNLASPKQ
LGDVLFEKLK LDPKAKKTKT GQYATGEEIL SKMANEHPIA EAILDFRQMV KLKSTYVDAL
PTMINPKTGR IHTTYNQFVA ATGRLSSINP NLQNIPIRTA RGREIRKAFV PRDENHILLS
ADYSQIELRL MAAFSGDESM LEAFKNGRDI HATTAAKIFK VPLEEVTTDM RRKAKTANFG
IIYGISAFGL SQRLSIPRTE AKEIIDAYFQ EFPAVKEYMD GAIEKARKNE YVETILGRRR
YLRDINSRNM TMRGFAERNA INAPLQGSAA DLIKVAMIHV YEWMKKENLK SKMILQVHDE
LVFDAHIDEV ELLKKNIPEL MSNAIKLAVP IEVEVGVGAD WLQAH
//
