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Database: UniProt
Entry: A0A1B6ZCR1_9SPHN
LinkDB: A0A1B6ZCR1_9SPHN
Original site: A0A1B6ZCR1_9SPHN 
ID   A0A1B6ZCR1_9SPHN        Unreviewed;       932 AA.
AC   A0A1B6ZCR1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=A8B75_09520 {ECO:0000313|EMBL:OAO04260.1};
OS   Sphingomonadales bacterium EhC05.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1849171 {ECO:0000313|EMBL:OAO04260.1, ECO:0000313|Proteomes:UP000078455};
RN   [1] {ECO:0000313|Proteomes:UP000078455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC05 {ECO:0000313|Proteomes:UP000078455};
RA   Rosana A., Orata F., Boucher Y., Case R.;
RL   Submitted (MAY-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   -!- 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:OAO04260.1}.
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DR   EMBL; LXYP01000006; OAO04260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6ZCR1; -.
DR   STRING; 1849171.A8B75_09520; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000078455; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000078455};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          10..273
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          330..520
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          689..892
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   COILED          551..578
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   932 AA;  102057 MW;  EB6F50F522ABCCE2 CRC64;
     MTDISTDTQN HLYLVDGSAY IFRAYHRLPP LTNIHGEPVG AVYGYTTMLW KLADELNKAE
     GPTHMAVVLD KSGTSFRNDL YDQYKANRPE APEDLRPQFP MIRDATRAFS LPLIEEENVE
     ADDMIASYSK AAVAQGWKVT IVSSDKDLMQ LIEPSDDSLV DMLDTMKNVR MNRATVEEKF
     GVGPEKLGDV LGLMGDSSDN IPGVPGIGPK TASKLINEFG DIESVLAAAP DMKKSKMKEN
     LIEFAEQARL SRVLVTLKED CPLPDTLDSF LIQDIPENPL REFLSHHGFH SLLKKLGGNG
     MATPQDPDVG ENAEAPAAAP HAPVIDRSKY ECVQDMAALE TWIARATAKG VCAVDLETDS
     LESVTARVVG VCLATGPNEA CYVPLGHGSG DMFGETPQQI GLEEALAALK PLLEDDAVLK
     VGQNLKYDMG VLAQHDMKIT PMDDTLVMSF NLDAGLHGHG MDELSKLHLG HECISFKSLT
     GTGKKAIGFA EVPLEKATEY GAEDADVTLR LWEILRLRMA PERATRVYQM VDRPLVPVIA
     KMEATGVLVD REELSRLSKT FAEEMESLEK QIHDLAGEPF SIGSPKQLGE ILFGKLGLKG
     GKKGKSGQYS TDVTVLERLA GDGEPIAQKV VSWRQLAKLK STYTDALQEQ INARTGRVHT
     SYSLSGAQTG RLSSTEPNLQ NIPIRTAIGR QIRQAFVAAP GNVILAADYS QIELRLAAHI
     ADVETLKQAF AAGEDIHNRT ARELFGSEDR DARARAKTIN FAILYGISRW GLAKRLEVDP
     DEAQDMINVY FERFPGINQY ISTTLQAARE NGYTETLFGR KTWFERLKSQ NQAERQGSER
     AAINAPIQGT SADIIKRVMA RMLPALDQAG LHDVQMLMQV HDELVFELPE GDVEAASAVI
     RSVMSGAAEP AVKLSVPLDV DIGTGKSWDE AH
//
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