ID A0A1D8BVN1_9PSEU Unreviewed; 901 AA.
AC A0A1D8BVN1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BKA25_003425 {ECO:0000313|EMBL:MBB5909109.1};
OS Actinoalloteichus hymeniacidonis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=340345 {ECO:0000313|EMBL:MBB5909109.1, ECO:0000313|Proteomes:UP000551592};
RN [1] {ECO:0000313|EMBL:MBB5909109.1, ECO:0000313|Proteomes:UP000551592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45092 {ECO:0000313|EMBL:MBB5909109.1,
RC ECO:0000313|Proteomes:UP000551592};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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:MBB5909109.1}.
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DR EMBL; JACHIS010000001; MBB5909109.1; -; Genomic_DNA.
DR RefSeq; WP_069848400.1; NZ_JACHIS010000001.1.
DR AlphaFoldDB; A0A1D8BVN1; -.
DR STRING; 340345.TL08_10220; -.
DR Proteomes; UP000551592; 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; cd06140; DNA_polA_I_Bacillus_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 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 11..271
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 312..490
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 657..864
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 901 AA; 98110 MW; CCF39BD5F66DC5D9 CRC64;
MSLSDGNSAP GRLLLLDGHS LAYRAFHALP AENFRTTTGQ TTNAVYGFTS MVINLLRDET
PTHLAVAFDV SRKTFRSEVY PEYKATRSAT PDEFKGQISL IQDVLAVLGI PVLAKEGFEA
DDIIATLTTQ AAQQGLRVSI CTGDRDALQL VTEAVTVLYP RKGVSDLTRF TPDAVQEKYG
LTPVQYPDYA ALRGDPSDNL PGIPGVGEKT AAKWIREYGS LADLVDRVDE VRGKAGEALR
SRLEAVLLNR RLTELDRAVE LELAPQDLEV RQWDRDAVHR LFDDLEFRVL RDRLFATLGA
AEPEVEEGLD VHGGLLPSGA LAAWLGEHAV AGTRIGLATK GTWARGAGDT EGLALATASG
QGAYIQTVDL TEDDEQALAA WLADPQQPKA AHDAKIVRHV LGARGWRLAG LTSDTALAAY
LVRPGQRSFD LADLVVRYLG RELRLQAEED SGQLSLLADE RADAAAQATD EIVRANAIAL
LADALDGELA GINGSSLLTE LELPVLGVLT ELEEAGIAVD ADRLHGLADH FAAQVKVAAD
AAFGVIGKEI NLGSPKQLQV VLFDELGMPK TKRTKTGYTT DAEALQTLFA STEHPFLAHL
LAHRDATRLK STVDGLIKSI AADGRIHTTF NQTIAATGRL SSTEPNLQNI PIRTEEGRRI
REVFVVGAGH AELMTADYSQ IEMRIMAHLS GDEGLIDAFR QGEDLHTYVA SRAFDVAADQ
VDAELRRRVK AMSYGLAYGL SVYGLAQQLR ISAEESRAQM DAYFARFGAV RDYLHDVVER
ARKDGYTETV LGRRRYLPDL TSDNRQRREM AERMALNAPI QGSAADIIKV AMIEVHKGLV
ESGLRSRMLL QVHDELVLEI AEGERDVVEE LVRRTMGSAY QLDVPLEVSV GVGRSWDSAA
H
//
