UniProt: A0A1B0ZRD1

Database: UniProt
Entry: A0A1B0ZRD1_9RHOB

LinkDB:  A0A1B0ZRD1_9RHOB 
Original site:  A0A1B0ZRD1_9RHOB

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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)   
All databases (31)   

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ID   A0A1B0ZRD1_9RHOB        Unreviewed;       945 AA.
AC   A0A1B0ZRD1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=JL2886_01818 {ECO:0000313|EMBL:ANP36726.1};
OS   Phaeobacter gallaeciensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=60890 {ECO:0000313|EMBL:ANP36726.1, ECO:0000313|Proteomes:UP000092565};
RN   [1] {ECO:0000313|EMBL:ANP36726.1, ECO:0000313|Proteomes:UP000092565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL2886 {ECO:0000313|EMBL:ANP36726.1,
RC   ECO:0000313|Proteomes:UP000092565};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) 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}.
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; CP015124; ANP36726.1; -; Genomic_DNA.
DR   RefSeq; WP_065271659.1; NZ_JARCJU010000010.1.
DR   AlphaFoldDB; A0A1B0ZRD1; -.
DR   PATRIC; fig|60890.4.peg.1775; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000092565; 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};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092565};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          7..270
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          330..534
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          702..905
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   945 AA;  103721 MW;  6302A2E58693E29E CRC64;
     MSGTQFGKGC HLHLIDGSAF IFRAYHALPP LTRKSDGLPI GAVAGFCNML VKYIETNTGP
     DAPTHVAVIF DHSGKTFRND LYDLYKANRP PAPEDLRPQF PLTRDATRAF NIACKEIEGF
     EADDIIATLA HQARDAGGRC TIISSDKDLM QLVGGGVEML DAMKNKRIDS DGVMEKFGVG
     PDRVVDVQAL AGDSVDNVPG APGIGIKTAA LLINEFGSLD ELLDRAEEIK QPKRRQTLIE
     KRDQIELSKK LVQLDCDMVL DFSLDDLELR EPDPDTVLNF LTEMEFRTLS ARMAKQMGRE
     APVIPEPTAT PAAAAEDDPA EAVPFDAEKY ECVRDAEALQ VWIDRIRGRG WVAFDTETTG
     LNEMTADLVG VSLCVEPGEA CYIPLTHKAE AGSDDLFGSD ALAEGQMDFD TALSMLKPVL
     EDPAILKIGQ NMKYDAKIMA RQRGAGFADG ITVAPYDDTM LLSYSLHGGE HGHGMDTLSE
     RYLDHTPIPI KPLLGTGKSA ITFDRVPIAD AVPYAAEDAD ITLRLWKTFK PQLHREKVTT
     VYETLERPLS PVLARMERHG IKVDRDTLSR MSNAFAQKMA ALEDEIHTLA GESFNVGSPK
     QLGEILFDKM GIEGGKKGKT GAYATGADIL EELATEHELP ARVLDWRQLS KLKSTYTDAL
     QDHINPETGR VHTSYVQTGA NTGRLASADP NLQNIPVRSE EGRRIREAFV AETGNKLLSL
     DYSQIELRIL AHVADIGTLK QAFADGLDIH AMTASEVFDV PLDEMTPDIR RKAKAINFGV
     IYGISGFGLA RNLRIPRAEA QGFIDRYFER FPGIRKYMDS TVEFAKEHGH VQTLFGRKIH
     TPEINAKGPR AGFAKRAAIN APIQGTAADV IRRAMVRMPD AIAHLPAKML LQVHDELIFE
     VPEAAVEETT ETARRVMESA ADPAVHLDVK LTVDAGTGDN WAEAH
//

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