ID A0A0X1KR25_9THEM Unreviewed; 892 AA.
AC A0A0X1KR25;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=AJ81_05660 {ECO:0000313|EMBL:AJC73766.1};
OS Pseudothermotoga hypogea DSM 11164 = NBRC 106472.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=1123384 {ECO:0000313|EMBL:AJC73766.1, ECO:0000313|Proteomes:UP000077469};
RN [1] {ECO:0000313|EMBL:AJC73766.1, ECO:0000313|Proteomes:UP000077469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11164 {ECO:0000313|EMBL:AJC73766.1,
RC ECO:0000313|Proteomes:UP000077469};
RA Zhang X., Alvare G., Fristensky B., Chen L., Suen T., Chen Q., Ma K.;
RT "Genome sequencing of Thermotog hypogea.";
RL Submitted (JAN-2014) 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; CP007141; AJC73766.1; -; Genomic_DNA.
DR RefSeq; WP_031505167.1; NZ_JONI01000011.1.
DR AlphaFoldDB; A0A0X1KR25; -.
DR STRING; 1123384.AJ81_05660; -.
DR PaxDb; 1123384-AJ81_05660; -.
DR KEGG; phy:AJ81_05660; -.
DR PATRIC; fig|1123384.7.peg.1121; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000077469; 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; 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.
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:UP000077469};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..262
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 297..484
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 652..859
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 629..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 101310 MW; 5E1600BCD2FBF62B CRC64;
MARLFLFDGT GLAYRAYYAI DQSLSTSDGI PTNATYGLMR MMIKFLKERI REGDYAGFAM
DKKTRTYRHE LLAEYKAQRA PAPDAMLQQL PYIKRGVEAL GVKVLEYEGC EADDVIATLA
KKGESRFEEV HIVSGDKDVL QLVSDKIKVW RPIKGISELE LYDEQKVLEK FQVPPNHIVD
LLALAGDTVD NVPGVQGIGP KTAVELISKY GSLEEIYEKI DKNSRLGKLL LQHREDAFKS
KKLVTLMSDL ELGLNWEDLR YEGFKQEKLI EFLKELEFSS LMKELGLYAQ QPEQTPYRAI
LTEQEFEQLL QRMQSSQYVV IDTETDSLDP LSAHLVGISV ALPDKSSHYV PVGHRRGPNL
PLEKVLKGLK PILEDKTIKI VGQNLKYDYS IFMAHGITPN PPAFDTMIAA YLLNPDEKRF
GLDELALKFL NYKMMSFDEL VKSSSPLFSA VTFADVDVQD ATKYSAEDAD VTRRLYELLN
VKLHEQGLTD VLEKIEMPLI VVLAEMELTG VYMDVSYLKD LSLKYSAKMN ELSRQIFDLA
GEVFNLNSPK QTAYVLFEKL KIKPKGKTPG GELSTRADVL EDLIEEHPIV PLILSYRKYQ
KLKSTYLDVL PRLVHPKTGR IHTSFHQTGT ATGRLSSSDP NLQNLPSKQE EGREIRKAVV
PQQSGWKILS ADYSQIELRV LAHMSKDENL IEAFVKDKDV HTFTAARIFG IREEDVGPEE
RSIGKMVNFS IIYGVSPYGL SQRTGLSYRQ AEAFIKEYFE LYPHVREYLT KTVAFAKTHG
HVRTLFGRKR EVPQLRSSDS SVRQEGERIA VNTPIQGTAA DIMKLAMIAV HRFLKEKGLR
TKMILQVHDE LVFEVPNEEA ELVTKKVKEI METVVKLSVP LKVDVKLSEH WE
//
