UniProt: R4Z7P7

Database: UniProt
Entry: R4Z7P7_9ACTN

LinkDB:  R4Z7P7_9ACTN 
Original site:  R4Z7P7_9ACTN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (13)   
   Pfam (3)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (30)   

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ID   R4Z7P7_9ACTN            Unreviewed;       898 AA.
AC   R4Z7P7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=BN381_80407 {ECO:0000313|EMBL:CCM65877.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM65877.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM65877.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM65877.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
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:CCM65877.1}.
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DR   EMBL; CANL01000078; CCM65877.1; -; Genomic_DNA.
DR   RefSeq; WP_012231032.1; NZ_HG422565.1.
DR   AlphaFoldDB; R4Z7P7; -.
DR   STRING; 1229780.BN381_80407; -.
DR   GeneID; 78312567; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_11; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000018291; 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; 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.
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:UP000018291};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          1..262
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          310..489
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          655..861
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   898 AA;  96452 MW;  157542307A806E97 CRC64;
     MPTVMLVDGN SLTYRAYFAL PTDLATASGQ VTNAVFGFTS MLVNLVRDHR PDRIVVTFDL
     PEPTFRHKAV TTYKANRDAT PDLLVQQMEL VRRVVDTLAL PVVEAPGFEA DDVIATLAER
     AKVAGEDVII VTGDRDSYQL VENPHVRVLY NRRGVSDYAL YDEEGILERT GVKPSDYVFY
     AALRGDPSDN LPGVPGVGEK TAAKLVNKYG TIDELFAHAA EQTPKLAQSL EANEGQVRMN
     AQMMALIRDV DLAEEVTSLR VGSIDADEVA ELFGFLEFSS LQARFSEAFG AYLSAPLAAG
     DARVLEAEVT VPGTAVEAAK ALEAAIASGV DGPVGVAADW LGDPGRSPLA GLAVVTDAAA
     GEVAWFPDPA TGVLTGCDDQ VVALLGGDVP LVAHDAKPLL RSLLGLEVEV SGLALDTKLA
     AYLLDPADAR YDLAELLARY AGAEMAGAEP TPSDQLDLGD GPSDQPHQVI ARRALAVEAL
     AGPMREALEV RGLAALNDDV EVPLVRVLAR MEDLGVGVDR DALQGLADRL VAEVAEERAA
     IVATAGHEFN VNSTPQLRQV LFEELGLTPH KKTKTGYSTD AATLEKLRGE HPIVEHLLRY
     REVEKLRSTY GEGLLSEIAP DGRIHATFNQ TVARTGRLSS DQPNLHNIPV RSEEGRLFRR
     AFVPAPGYRL CVADYNQIEL RCIAHLSQDP GLVGAFTAGD DIHAQTAARI FEVDADEVTV
     AQRSTAKMVS YGLAYGMEAY GLGQRLSIPT GEAQVILDAY FEGFPNVRAY MEGAVADARE
     KGYTETLFGR RRQIPELASR VRAVRQAGER QAMNAGIQGL AADIFKLALV RLDRGLEDRG
     GTSRLILQVH DEVVLEVPPA DEAEITAVVL DAMSGAFDLA VPLEVNLAFG DTWADAKA
//

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