UniProt: Q05XN5

Database: UniProt
Entry: Q05XN5_9SYNE

LinkDB:  Q05XN5_9SYNE 
Original site:  Q05XN5_9SYNE

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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 (21)   
   InterPro (13)   
   Pfam (4)   
   SMART (4)   
All databases (29)   

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ID   Q05XN5_9SYNE            Unreviewed;      1007 AA.
AC   Q05XN5;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=RS9916_31797 {ECO:0000313|EMBL:EAU74185.1};
OS   Synechococcus sp. RS9916.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU74185.1, ECO:0000313|Proteomes:UP000004972};
RN   [1] {ECO:0000313|EMBL:EAU74185.1, ECO:0000313|Proteomes:UP000004972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS9916 {ECO:0000313|EMBL:EAU74185.1,
RC   ECO:0000313|Proteomes:UP000004972};
RA   Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-2006) 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   -!- 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:EAU74185.1}.
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DR   EMBL; AAUA01000001; EAU74185.1; -; Genomic_DNA.
DR   RefSeq; WP_007098291.1; NZ_DS022299.1.
DR   AlphaFoldDB; Q05XN5; -.
DR   STRING; 221359.RS9916_31797; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_3; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000004972; 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; 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.
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:UP000004972};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          6..289
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          375..578
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          749..971
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          333..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1007 AA;  108986 MW;  2C01D76C04B53FE7 CRC64;
     MSPSQDKPLL LLVDGHSLAF RSFYAFSKGG EGGLATKDGV PTSVTYGFLK ALLDNCKSLT
     PQGVAIAFDT AEPTFRHKAD PNYKAHRDTA PEVFFQDLNQ LQEILRQQLQ LPLCMAPGFE
     ADDVLGTLAN RAANAGWRVR ILSGDRDLFQ LVDDSRDIAV MYMGGGPYAR SSGPMLINEE
     GVVAKLGVVP TSVVDLKALT GDSSDNIPGV KGVGPKTAIN LLKENGDLDA VYRVLAEVEA
     EGPKASRGAI KGALKGKLSN DRDNAYLSRQ LAEILVDIPL PEEPALELGP VDGEGLQQQL
     EMLELNSLVR QVPAFVATFS TGGLAANRHL VESAKTSSSK TKASASSSTS DPDQAAANDP
     STSPESSASL PDLQPELITT PAQLTGLVER LMACRDPLAP VAVDTETSDL NPFKAQLVGV
     GVCWGADLKD LAYIPVGHMA PAAPDGEDAA GEPEQLALDA VLQALAPWLA SSDHPKALQN
     AKYDRLILLR HGLTLGGVVM DTLLADYLRD AAAKHGLDLM AQRDYGITPT LFTDLVGKAK
     DGKASSFAAV PVDQAALYCA MDVHLTRRLA LDLRQQLTSM GEQLPALLEQ VELPLEPVLA
     LMEATGIRID VPYLQELSAE LGATLERLET EAQDVVGTSF NLASPKQLGE LLFDTLGLNR
     KKSRRTKTGW STDATVLEKL EGDHPVVPLL LEHRVLSKLK STYVEALPQL VEAETGRVHT
     DFNQAVTATG RLSSSNPNLQ NIPVRTEFSR RIRKAFLPQE GWQLLSADYS QIELRILTHL
     SGEEVLQQAY RDGDDVHALT ARLLLEKDEV SADERRLGKT INFGVIYGMG AQRFARETGV
     SQVVAKDFLA KYKQRYPKVF AFLELQERLA LSRGYVETIL GRRRPFHFDR NGLGRLLGKD
     PLEIDLDVAR RGGMEAQQLR AAANAPIQGS SADIIKLAMV QLQTALQQQG LPAQLLLQVH
     DELVLEVEPA ALDTVRQLVV QTMENAMTLS VPLVVETGSG ANWMEAK
//

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