UniProt: A0A142YJA5

Database: UniProt
Entry: A0A142YJA5_9PLAN

LinkDB:  A0A142YJA5_9PLAN 
Original site:  A0A142YJA5_9PLAN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (1)   
   SMART (4)   
All databases (32)   

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ID   A0A142YJA5_9PLAN        Unreviewed;       902 AA.
AC   A0A142YJA5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
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_1 {ECO:0000313|EMBL:AMV39315.1};
GN   Synonyms=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=VT85_17900 {ECO:0000313|EMBL:AMV39315.1};
OS   Planctomyces sp. SH-PL62.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV39315.1, ECO:0000313|Proteomes:UP000076365};
RN   [1] {ECO:0000313|EMBL:AMV39315.1, ECO:0000313|Proteomes:UP000076365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV39315.1,
RC   ECO:0000313|Proteomes:UP000076365};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) 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; CP011273; AMV39315.1; -; Genomic_DNA.
DR   RefSeq; WP_068418197.1; NZ_CP011273.1.
DR   AlphaFoldDB; A0A142YJA5; -.
DR   STRING; 1636152.VT85_17900; -.
DR   KEGG; plh:VT85_17900; -.
DR   PATRIC; fig|1636152.3.peg.4059; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000076365; 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   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:UP000076365};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..260
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          302..487
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          655..862
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   902 AA;  100466 MW;  C727359FEDC98D62 CRC64;
     MADRPTFYIL DAYSLIFQVF HAIPEMTSPT GGPTNAAFGI FRDVLNLFRD RKPDYIAAAF
     DGGGPVFRSE IFADYKSNRP DMPINLVPQI DVIRRIFEGF NVPVLVEPGM EADDVIATLA
     RRGEERGLDV FICTSDKDAR QLISDHVKIL NIRKNTLMDE AALEKEWGIR PGQVVDFLAL
     TGDAVDNVPG VPGIGPILAS GYLKQFGDLE TLLANPDKVK GPKKQQALRD NAEVARRARS
     LVALRDDLEL ALDWNALQAS PPNAPVLREI CVESGFHRFA ADLSDSKETV PDAPKAEWVA
     RYSTIDTPES FQTFVQELRK QPRFCIDAET TSINPLLSSL VGIAVSWNAG EGFYIPLRAP
     IGFKILDPEM VLDALRPILA DPEVEKVGQN LKYDMLAFRR AGVSIEGPIT DTMILSYLLE
     SGERNHSLDQ LSDRLLGHKM IPISDLIGKG KKQLRMDQID VPRIAEYAGE DADATWRVYE
     ILAPRVREEG LWDLYADLER PLVSILMRME EIGVMVDVHR LKELSDDFAV RLAATEEEIH
     KLAGRPFNIN SVPQLRQILF EELKLPKLQK TPGGELSTAT EVLEELASKH PLPALLVRHR
     QLTKLKGTYL DALPLLAHPD DGRIHASFNQ GVAATGRLSS SDPNLQNIPV RTEEGRQIRQ
     AFVAEGDDQR LLTADYSQIE LRVLAHFSQD PALCKAFEAD HDIHRAVAAR IYGVAEDQVD
     DTMRRVAKTV NFGVIYGLSP FGLAGRLGIK QSEAAAFIDA YFQEYQGVDQ FITRTLESAQ
     ASGRVETILG RRRPIAGIKA TTGRNRNLAE RTAVNTVIQG SAADLIKRAM ILVDRRLREE
     RLEARMILQI HDELVFESPV SELPRLAALV REEMTRALSL AVPLKVDLAV GRNWLDVETP
     DY
//

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