GenomeNet

Database: UniProt
Entry: D3TAJ5_ACIB4
LinkDB: D3TAJ5_ACIB4
Original site: D3TAJ5_ACIB4 
ID   D3TAJ5_ACIB4            Unreviewed;       784 AA.
AC   D3TAJ5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   OrderedLocusNames=Aboo_1316 {ECO:0000313|EMBL:ADD09124.1};
OS   Aciduliprofundum boonei (strain DSM 19572 / T469).
OC   Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX   NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD09124.1, ECO:0000313|Proteomes:UP000001400};
RN   [1] {ECO:0000313|Proteomes:UP000001400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT   "Complete sequence of Aciduliprofundum boonei T469.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001941; ADD09124.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3TAJ5; -.
DR   KEGG; abi:Aboo_1316; -.
DR   HOGENOM; CLU_000203_6_0_2; -.
DR   Proteomes; UP000001400; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   CDD; cd00145; POLBc; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000313|EMBL:ADD09124.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ADD09124.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001400};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADD09124.1}.
FT   DOMAIN          81..242
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          351..750
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   784 AA;  91295 MW;  64ED63CC6E0DFF69 CRC64;
     MRCLYVYWDV RLLTASYSRE EDGVVVELYG KTREGKSIVV RYKGFKPYFY LVEPPSTILE
     KFSQDPEIYK MEEVELWHKG KVRKCVKVTL HSPWKTPRYR REALEFCDVL AADIPFHQRF
     IYDFDLGSCV RVYGKEEEKG KYTTELVVNA EKFENIGDFK PPLKILSFDI ENSMKNGRIF
     TIGIAIWENG EIRKESIEGD EKDILWKFLE MIWKEDPDII TGYNIDGYDL ELLSERYKKY
     GMDFLIGRDK SKPQRIVGQF WRLHGRVIED AWWAVKKELR LKQETLQAVA MHLFGEGKLD
     VDRTNIDEEW EKDKEKVIEY CKKDAELALR ILLQIGIINK YLDLATVTKF PLEDVIHSGT
     STWVDSLLIR EADRHNIGVP LQGQERKSRK IEGGYVHTIE PGLYHWVCVL DFKSMYPSII
     IKYNICFTTL SKDGDIVSPT GVRFLSKEKR EGLIPKLLAE LMKKRDELKR KMKEDPDNRD
     YYNGLQKAVK ILMNTFYGVL ASSFYRFTNP DIGASITAFA RDTIKRIIAE LESEGIKVVY
     GDTDSVFFQS PYEDLENTIE FGMRKAEEIS RREKLILEFE KILEPFFSHG AKKRYVGRII
     WPDEEKGNMV VRGYEIRRTD SFDLQSEAQR AVFEKILDGD IQGAIELARE IVSKVRAGKV
     PIESLVISRT VKDFKFYKNP DSMPNVQAAR KLIKMGQEFI PGMKVAWIVV NARGSKQDVE
     PYIPGMEFNR KPDYRYYARR VAETLARITD VFGVDEENLL TGSRQISLGA FGKEKKKKTL
     FDFE
//
DBGET integrated database retrieval system