UniProt: A0A147K6L1

Database: UniProt
Entry: A0A147K6L1_9BACI

LinkDB:  A0A147K6L1_9BACI 
Original site:  A0A147K6L1_9BACI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (14)   
   Pfam (3)   
   PROSITE (1)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (31)   

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ID   A0A147K6L1_9BACI        Unreviewed;       876 AA.
AC   A0A147K6L1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=Q75_11435 {ECO:0000313|EMBL:KUP05572.1};
OS   Bacillus coahuilensis p1.1.43.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP05572.1, ECO:0000313|Proteomes:UP000074108};
RN   [1] {ECO:0000313|EMBL:KUP05572.1, ECO:0000313|Proteomes:UP000074108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX   PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA   Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA   Olmedo-Alvarez G.;
RT   "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT   Phosphorus Acquisition Strategies and Their Regulation.";
RL   Front. Microbiol. 7:58-58(2016).
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, 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:KUP05572.1}.
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DR   EMBL; LDYG01000034; KUP05572.1; -; Genomic_DNA.
DR   RefSeq; WP_059351430.1; NZ_LDYG01000034.1.
DR   AlphaFoldDB; A0A147K6L1; -.
DR   STRING; 1150625.Q75_11435; -.
DR   PATRIC; fig|1150625.3.peg.2433; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000074108; 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   Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          4..263
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          300..466
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          633..840
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   876 AA;  99322 MW;  E53141F8F392309B CRC64;
     MSKKKLVLID GNSIAYRAFF ALPLLNNDKG IHTNAIYGFT TMLMKIMEEE KPTHVLVAFD
     AGKTTFRHET FTEYKGGRQK TPPELSEQFP FIRELLKAYG ISHYELPNYE ADDIIGTLSK
     KAEQDGFSVK VISGDKDLTQ LASEHTTVMI TKKGITDMEE YTPEHIREKW EIDVSQIIDM
     KGLMGDSSDN IPGVPGVGEK TAIKLLKQFS SIEQLLESID EVSGKKLKEK LEENKEQAVM
     SKKLATIMTD APVEITLEEV FYEGIVDEEL QMLFKELGFQ SLLEKFDFEG GALEELEELS
     FIVAHEITQE MLAHPSALYV EMLEENYMNG KIIGYGLSNQ SGHYFIPTDI ARESEGWQEW
     LRDKSKEKVV YDAKKSIVAL KRQGLELNGV SFDSLLAAYI INPAQNHEDF ASVGKEYGLS
     CVQSDEQVYG KGAKQAVPNL DALSEHVARK ASMLWDLTEK LKTALKENHQ DALFFDLELP
     LAFILGEMEY QGVKVDRTRL TSMGKELGGK LKELEEKIYE LAGETFNINS PKQLGVILFE
     KLELPVIKKT KTGYSTSADV LEKLQSKHEI VKYILHYRQL GKLNSTYIEG LLKVIHEDSD
     KVHTRFNQAL TQTGRLSSTD PNLQNIPIRL EEGRKIRQAF VPSKEGWVIF AADYSQIELR
     VLAHISGDDK LMEAFQQDED VHTKTAMEVF SVSKDDVTSE MRRHAKAVNF GIVYGISDFG
     LSQSLNITRK EAGEFIERYL DTYPAVKEYM EDIVVEARDK GYVSTLLNRR RYIPELTSRN
     FNLRSFGERT AMNTPIQGSA ADIIKQAMID MAKRLEEENI EAKLLLQVHD ELIFEAPQSE
     IEKLKTMVPD VMENAVELNV PLKVDFAFGP TWYDAK
//

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