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Database: UniProt
Entry: Q74N74_NANEQ
LinkDB: Q74N74_NANEQ
Original site: Q74N74_NANEQ 
ID   Q74N74_NANEQ            Unreviewed;       676 AA.
AC   Q74N74;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   OrderedLocusNames=NEQ068 {ECO:0000313|EMBL:AAR38923.1};
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908 {ECO:0000313|EMBL:AAR38923.1, ECO:0000313|Proteomes:UP000000578};
RN   [1] {ECO:0000313|EMBL:AAR38923.1, ECO:0000313|Proteomes:UP000000578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M {ECO:0000313|EMBL:AAR38923.1,
RC   ECO:0000313|Proteomes:UP000000578};
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soll D.,
RA   Stetter K.O., Short J.M., Noordewier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
RN   [2] {ECO:0007829|PDB:5OXW, ECO:0007829|PDB:5OXX}
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 572-676.
RX   PubMed=29754955; DOI=10.1016/j.chembiol.2018.04.008;
RA   Gordo V., Aparicio D., Perez-Luque R., Benito A., Vilanova M., Uson I.,
RA   Fita I., Ribo M.;
RT   "Structural Insights into Subunits Assembly and the Oxyester Splicing
RT   Mechanism of Neq pol Split Intein.";
RL   Cell Chem. Biol. 25:871-879.e2(2018).
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}.
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DR   EMBL; AE017199; AAR38923.1; -; Genomic_DNA.
DR   PDB; 5OXW; X-ray; 2.61 A; A/B/C/D=579-676.
DR   PDB; 5OXX; X-ray; 1.74 A; A=572-676.
DR   PDB; 5OXZ; X-ray; 1.20 A; A=572-676.
DR   PDBsum; 5OXW; -.
DR   PDBsum; 5OXX; -.
DR   PDBsum; 5OXZ; -.
DR   AlphaFoldDB; Q74N74; -.
DR   SMR; Q74N74; -.
DR   STRING; 228908.NEQ068; -.
DR   EnsemblBacteria; AAR38923; AAR38923; NEQ068.
DR   KEGG; neq:NEQ068; -.
DR   PATRIC; fig|228908.8.peg.69; -.
DR   HOGENOM; CLU_000203_6_0_2; -.
DR   BioCyc; NEQU228908:GJB6-75-MONOMER; -.
DR   Proteomes; UP000000578; 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   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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5OXW, ECO:0007829|PDB:5OXX};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000578};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          76..310
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          381..586
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   COILED          491..518
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   676 AA;  79864 MW;  DAC580CEE616863D CRC64;
     MLHQLPTMVV EEKAVKEEEG YSVLKCYWIN IENTPLDEVI LIGKDENNRA CEVIIPYKWY
     FYFEGDIKDL EEFANNKKIK IEYTKEQKKY IEKPKDVYKV YVLHKHYPIL KEFIKEKGYK
     KYETDINVYR KFLIDKGIEP FEWFEVEGKI LLSTSNKVRI KAQSIKRLYE KTKPSVLAFD
     IEVYSEAFPN PEKDKIISIA LYGDNYEGVI SYKGEPTIKV NTEYELIEKF VEIIESLKPD
     IIVTYNGDNF DIDFLVKRAS LYNIRLPIKL VNKKEPTYNF RESAHVDLYK TITTIYKTQL
     STQTYSLNEV AKEILGEEKI YDYENMLYDW AIGNYNKVFE YNLKDAELTY KLFKYYENDL
     LELARLVNQP LFDVSRFSYS NIVEWYLIKK SRKYNEIVPN KPKMEEVERR KLNTYAGAFV
     YEPKPGLYEN LAVLDFASLY PSIILEHNVS PGTIYCEHDD CKQNGVEAII NNEKKYVWFC
     KKVKGFIPTV LEHLYTKRLE LKRKLKELDR DSEEYKIINA KQAVLKIIIN ATYGYMGFPN
     ARWYCIDCAA AVAAWGRKYI NYILKRAEEE GFKVIYGDSI MDTEIEVIEN GIKKKEKLSD
     LFNKYYAGFQ IGEKHYAFPP DLYVYDGERW VKVYSIIKHE TETDLYEING ITLSANHLVL
     SKGNWVKAKE YENKNN
//
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