UniProt: A0A177ZKH5

Database: UniProt
Entry: A0A177ZKH5_9BACI

LinkDB:  A0A177ZKH5_9BACI 
Original site:  A0A177ZKH5_9BACI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (14)   
   Pfam (3)   
   PROSITE (1)   
   SMART (4)   
All databases (29)   

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ID   A0A177ZKH5_9BACI        Unreviewed;       871 AA.
AC   A0A177ZKH5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-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=ABB05_16855 {ECO:0000313|EMBL:OAK68294.1};
OS   Lederbergia galactosidilytica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lederbergia.
OX   NCBI_TaxID=217031 {ECO:0000313|EMBL:OAK68294.1, ECO:0000313|Proteomes:UP000077881};
RN   [1] {ECO:0000313|EMBL:OAK68294.1, ECO:0000313|Proteomes:UP000077881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-74 {ECO:0000313|EMBL:OAK68294.1,
RC   ECO:0000313|Proteomes:UP000077881};
RA   Zheng Z., Sun M.;
RT   "Comparison of genome.";
RL   Submitted (MAY-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   -!- 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:OAK68294.1}.
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DR   EMBL; LDJR01000057; OAK68294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177ZKH5; -.
DR   STRING; 217031.ABB05_16855; -.
DR   PATRIC; fig|217031.6.peg.3646; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000077881; 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:UP000077881};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          1..257
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          296..461
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          628..835
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   871 AA;  98838 MW;  94D35C9AC824E5F3 CRC64;
     MLIDGNSIAY RAFFALPLLN NDKGVHTNAI YGFTTMLMKV LAEQKPTHVL VAFDAGKTTF
     RHSTFTEYKG GRQKTPPELS EQFPFLRNLL DAYGIKRYEL ENYEADDIIG TLATKAEKED
     FEVLVVSGDK DLTQLSTDKT TVAITRKGIT EIESYTPEHI KEKYGLQPKQ IVDMKGLMGD
     QSDNIPGVPG VGEKTAIKLL KEFHTMENLL EHIDQVGGKK LKEKLTEHKD LAIMSKELAT
     IMKEAPIDVS IDELLYEGYE PEALISLFKE LGFHSLLDKV EGAEAIEEEE IKEISYEIVD
     TITDEIFADE SSLYIEILED NYHTGEIIGF GLTNQNGHYF IPTELALQSE AFKKWASDES
     KKKRVYDGKR SIVSLKWHGV DLNGIDFDLL LVSYLLNPSE SSDDFAGVAR RHHYTDVQTD
     EAVYGKGAKR KIPNEQILAE HLARKAIAID ALYAQCLKEL EENEQTDLFY DLELPLSIIL
     AEMEYTGVKV DTARIQEMQI ELAERLKEIE RRIYTLAGDE FNINSPKQLG VVLFEKLGLP
     VLKKTKTGYS TSADVLEKLA ESHEIIPEIL HYRQLGKLQS TYIEGLLKVV HKDTNKVHTR
     FNQALTSTGR LSSTDPNLQN IPIRLEEGRK IRQAFIPSEK DWVIFAADYS QIELRVLAEI
     AQDKGLQEAF QHDMDIHTKT AMDVFHVTAD EVDGNMRRQA KAVNFGIVYG ISDYGLSQSL
     GITRKEAGKF IDRYLESFSG VKHYMEDIVQ EARENGFVST LLHRRRYIPE ITSRNFNIRS
     FGERTAMNTP IQGSAADIIK KAMIEMAARL KKEQLQTRLL LQVHDELIFE APKDEINKLK
     EIVPEVMEQA LTLSIPLKVD YAYGPTWFDA K
//

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