UniProt: C5ZZ02

Database: UniProt
Entry: C5ZZ02_9HELI

LinkDB:  C5ZZ02_9HELI 
Original site:  C5ZZ02_9HELI

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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 (23)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (1)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   C5ZZ02_9HELI            Unreviewed;       896 AA.
AC   C5ZZ02;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
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   ECO:0000313|EMBL:EES89260.1};
GN   ORFNames=HCAN_0543 {ECO:0000313|EMBL:EES89260.1};
OS   Helicobacter canadensis MIT 98-5491.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89260.1, ECO:0000313|Proteomes:UP000007032};
RN   [1] {ECO:0000313|EMBL:EES89260.1, ECO:0000313|Proteomes:UP000007032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX   PubMed=19542273; DOI=10.1128/JB.00729-09;
RA   Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA   Weinstock G.M., Wren B.W., Pallen M.J.;
RT   "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL   J. Bacteriol. 191:5566-5567(2009).
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}.
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DR   EMBL; CM000776; EES89260.1; -; Genomic_DNA.
DR   RefSeq; WP_006655239.1; NZ_DS990368.1.
DR   AlphaFoldDB; C5ZZ02; -.
DR   STRING; 537970.HCAN_0543; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_7; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000007032; Chromosome.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007032};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..259
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          311..495
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          662..860
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   896 AA;  103171 MW;  6EE54075A386212E CRC64;
     MATKTLTIID TFGFLFRSYF ALPPLKNHEG FPTGLLTGFA KLIMQLHKDY PKDYLVFALD
     SKGENFRKQI DPLYKANRPE VPQDLKLQLE VAIRWVEDMG FKNISIEGFE ADDVIASINK
     QVNKLDVNVR IISHDKDLYQ LIDKDTFLFN PSKKEEIREE ECKEKYGVYP SQFVDYQSIV
     GDSADNVPGV KGIGAKGAVN LLNNFGSLDS IYQHLDEIPQ KRTRELLSAA KDDAYRSREL
     VKLRDDLLED FDLSECEMPQ DSPLLRILDS LREYDLNSVL KKLHKNPITK KKISQIESQE
     NEQEKKFIYK THLIDNDSKL KEFFSTLPKE SIFSFDTETT SLDVRKAKIV GFSFSVNGVD
     CYYIPIAHNY LGVESQVSLE CARECIEQIF QSQYVIGHNL KYDLEILKTN FDFVLEDFSK
     VRDSMLLAWL LQSDTLCNLD FLMKKYFNHE MIHYKDIVGK NENFSNILIQ HACEYASEDA
     AACYQLYFKL RGLMDESLLE IAQKVEFPFI QSLMNMELSG IKIDLEYFLG LNAETREKLH
     QISEEIFVLA NKRFNLNSPQ QLASILFDDL KLEASKKTKS GYSTSELVLN SLYDSHPIIP
     KILEYRESFK LYSTYIEPLI EHAKSDLEHR IYTSFMQTGT STGRLSSKNP NLQNIPVKTL
     EGRRIRKGFI AKENCLLISL DYSQIELRLL AHFSQDKAMI DAFLQDADIH LETAKKIFGE
     EMAQEKRAVA KSINFGLIYG MGPKKLSETL KINFQEAKTY IQNYFTSFPM IKNFLKEQEE
     FILENGYSKT LLGRMRKFDF EGVQEYQKAA FLREGINAIF QGSAADIIKM AMNKIMHSSL
     ESKLLLQVHD ELIFEAPKEI ASKEAKKIAL IMENIATLRV PLKCSISIGE NWGELK
//

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