ID A0A1Y6F371_9SPHN Unreviewed; 948 AA.
AC A0A1Y6F371;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-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=SAMN06297468_1539 {ECO:0000313|EMBL:SMQ69338.1};
OS Altererythrobacter xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ69338.1, ECO:0000313|Proteomes:UP000194420};
RN [1] {ECO:0000313|Proteomes:UP000194420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Varghese N., Submissions S.;
RL Submitted (APR-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 -!- 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}.
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DR EMBL; FXWG01000002; SMQ69338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6F371; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000194420; 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: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:UP000194420};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 5..272
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 340..536
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 705..908
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 294..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 104457 MW; 6815B6F46B4D189F CRC64;
MPDQQHLYLV DGSSYIFRAY HRLPPLTDPE GTPVGAVYGY TTMLWKLAED LDKADGPTHL
AVILDKDSQS FRNEIYPEYK ANRPDPPEDL VPQFPLIRDA TRAFSLPCIE EQGLEADDLI
ATYARAAQRE GWNVTIVSSD KDLMQLVGEV DGPNGPARID MLDTMKSQRI YIEEVEDKFG
VKPELVGDVL ALMGDSVDNI PGIYGIGPKT ASKLIAEHGS LTAALDAAEY MKKSKLKERL
LENRADAEMS RVLVTLKEDC DLPEPLDDFK LDGVPPEPLA AFLEKHGFTS LLRRLDAGSG
SPDRPNNLNP EKAQTKGDAG TEEGNSQPLP EMPAVDRSAY ETVQTMDRLL SWIERAEAAH
EVAVDTETSS LDAMRAELVG VSLALGPNEA CYIPLGHGGS DMFAERPEQV DREAALAALK
PLLESDAVTK IFQNGKYDLN VLARYGIEVS PIEDTMIVSF ALDAGRGQDG IGGGHGMDEL
SERHLGHTPI AFKEVCGTGK KQIPFGEVPL DKATEYAAED ADVTWRLYQH LKPRLSVEGG
TRIYERVDRP LIPVVAGMER EGIKVDRARL AKLSEEFAQE TARLEDEIHE AAGQEFTVGS
PKQLGDILFE KLGYKGGKKG KSGQYSTDQS VLERLAGEGA DIAKLVLEWR QLTKLKSTYT
DALQQAINPD TGRVHTSYSL VGAQTGRLSS TDPNLQNIPI RTAIGRQIRE AFVPESGNVL
LAADYSQIEL RLAAHMADVE TLKEAFANGE DIHARTATEM FGEVTRDTRA RAKTINFAIL
YGISRWGLAG RLEVEPDEAQ EMIDTYFKRF PGIQRYIMET LETVRERGYS QTLFGRKTWF
PRINSKNQAE RQGSERAAIN APIQGTSADI IKRAMVRMLP ALREEGLDNV RMLLQVHDEL
VFELPEGDVE KASPIIERVM AEAARPAVEL AVPLGVEIGT GASWDAAH
//