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Database: UniProt
Entry: A0A1X1Z4C7_9MYCO
LinkDB: A0A1X1Z4C7_9MYCO
Original site: A0A1X1Z4C7_9MYCO 
ID   A0A1X1Z4C7_9MYCO        Unreviewed;       899 AA.
AC   A0A1X1Z4C7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=AWC17_10975 {ECO:0000313|EMBL:ORW18188.1};
OS   Mycobacterium nebraskense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=244292 {ECO:0000313|EMBL:ORW18188.1, ECO:0000313|Proteomes:UP000193781};
RN   [1] {ECO:0000313|EMBL:ORW18188.1, ECO:0000313|Proteomes:UP000193781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44803 {ECO:0000313|EMBL:ORW18188.1,
RC   ECO:0000313|Proteomes:UP000193781};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) 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:ORW18188.1}.
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DR   EMBL; LQPH01000148; ORW18188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1Z4C7; -.
DR   STRING; 244292.ABW17_20740; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000193781; 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          9..271
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          312..488
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   899 AA;  98514 MW;  204CD4D56E41A9BC CRC64;
     MPVATEEQTK PTLMLLDGNS LAFRAFYALP AENFKTRGGL TTNAVYGFTA MLINLLRDEA
     PTHIAAAFDV SRQTFRSERY PEYKANRSST PDEFHGQIGI TKEVLNALGI TVLAEEGFEA
     DDLIATLATQ AENQGYRVLV VTGDRDSLQL VSDDVTVLYP RKGVSELTRF TPEAVVEKYG
     LTPTQYPDFA ALRGDPSDNL PGIPGVGEKT ASKWIAEYGS LQGLVDNVDS VRGKVGDTLR
     ANLATVIRNR ELTDLVKDVP LAQTPDTLRM QPWDRDHIHR LFDDLEFRVL RDRLFDTLAA
     VEPEVDAGFD VRGGALQAGE LAVWLAEHSS GKRFGLAVVG THLAYDADAT ALAIVSADGE
     GRYIDTSALD PDDEAALASW LADPGPPKAL HEAKLAMHDL AGRGWTLAGV TSDTALAAYL
     VRPGQRSFSL EDLSLRYLRR ELRAETPEQQ QLSLLDDSDG TDDQAVQTLI LRAVAVLDLA
     DALDEELARI NSTSLLGGME LPVQRVLAGM EHTGIAVDLD LLGELQSDFA HQIRDAAEAA
     YAVIGKQINL GSPKQLQTVL FDELDMPKTK RTKTGYTTDA DALQSLFDKT GHPFLQHLLT
     HRDATRLKVT VDGLLNSVAS DGRIHTTFNQ TIAATGRLSS TEPNLQNIPI RTEAGRRIRD
     AFVVGDGYSE LMTADYSQIE MRIMAHLSRD EGLIEAFNTG EDLHSFVASR AFGVPIEEVT
     AELRRRVKAM SYGLAYGLSA YGLSQQLKIS TEEAKEQMDA YFARFGGVRD YLMNIVEQAR
     KDGYTSTVLG RRRYLPELDS SNRQVREAAE RAALNAPIQG SAADIIKVAM IEVDKAIKEA
     GLKSRMLLQV HDELLFEIAP GERDRVEALV REKMGGAYPL DVPLEVSVGY GRSWDAAAH
//
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