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Database: UniProt
Entry: A0A2T5BE54_MYCDI
LinkDB: A0A2T5BE54_MYCDI
Original site: A0A2T5BE54_MYCDI 
ID   A0A2T5BE54_MYCDI        Unreviewed;       992 AA.
AC   A0A2T5BE54;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=C7449_102107 {ECO:0000313|EMBL:PTM97238.1};
OS   Mycoplana dimorpha.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Mycoplana.
OX   NCBI_TaxID=28320 {ECO:0000313|EMBL:PTM97238.1, ECO:0000313|Proteomes:UP000241247};
RN   [1] {ECO:0000313|EMBL:PTM97238.1, ECO:0000313|Proteomes:UP000241247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7138 {ECO:0000313|EMBL:PTM97238.1,
RC   ECO:0000313|Proteomes:UP000241247};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-2018) 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}.
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:PTM97238.1}.
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DR   EMBL; PZZZ01000002; PTM97238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T5BE54; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000241247; 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};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241247};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          374..577
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          746..952
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   992 AA;  108215 MW;  B09041262930D53B CRC64;
     MKNGDHLFLV DGSGFIFRAF HAIPPLNRKS DGLPVNAVSG FCNMLWKLLK DARSTDVGVT
     PTHFAVIFDY SSKTFRNELY DQYKANRTAP PDDLIPQFGL IRHATRAFNL PCIEKEGYEA
     DDLIATYARL AEEAGADVTI ISSDKDLMQL VTSKVSMYDS MKDKQIAIPE VVEKWGVTPD
     KMIDLQAMTG DSTDNIPGIP GIGPKTAAQL LQEFGDLDTL LARADEIKQQ KRRENIIANR
     EQALLSRQLV TLKTDTPLDT PLDELQLEPQ DGPRLIAFLK AMEFNALTRR VAEACNCDAS
     AIEPAFVPVE WGTDAHGPDL DIVAGRPLTD DALSAAQAAG TLLPDASPDA PTPAALAKAR
     AAFFSGRPFD RSAYVTIRDL ATLDLWLAAA RETGLVGFAA ATTTADAMQA ELCGFSLAIA
     DNAKDPAGAS IRAAYVPMQH RTGDGDLLGG GLAEGQIPIG ESLARLRQLV EDPSILKVAQ
     NLKFDYLVLK RHGMAIQSFD DAMLISYALD AGAAAHGIDS LSERWLAHKP IALKDVAGSG
     KGAQSFDLVD IDRATAFVAE DADITLRLWH VLKPRLAAEG LTTVYERLER PLVPVLARME
     ERGITIDRQV LSRLSGELGQ GAAALEDEIY QLAGERFTIG SPKQLGDILF GKMGLPGGAK
     TKTGQWSTSA QVLEDLAAEG VPLPRKIVDW RQLTKLKSTY TDALPGYVHP QTRRVHTCYS
     LASTTTGRLS STEPNLQNIP IRTGEGRKIR AAFIASPGHK LVSADYSQIE LRVLAHVADI
     PQLRQAFAEG IDIHAMTASE MFGVPVEGMP AEVRRRAKAI NFGIIYGISA FGLANQLSIE
     RSEAGDYIKR YFERFPGIRD YMESTKAFAR ENGYVETIFG RRAHYPEIRS SNPSVRAFNE
     RAAINAPIQG SAADIIRRAM IKMEPALEAG KLSARMLLQV HDELVFEVEE TEVERTLPVI
     VEVMENAAMP ALAMKVPLKV DARAADNWDE AH
//
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