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Database: UniProt
Entry: A0A0J1GDU2_9FIRM
LinkDB: A0A0J1GDU2_9FIRM
Original site: A0A0J1GDU2_9FIRM 
ID   A0A0J1GDU2_9FIRM        Unreviewed;       590 AA.
AC   A0A0J1GDU2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DhaK domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RHS_0446 {ECO:0000313|EMBL:KLU73590.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU73590.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU73590.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU73590.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
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:KLU73590.1}.
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DR   EMBL; JNGB01000003; KLU73590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1GDU2; -.
DR   PATRIC; fig|1504536.3.peg.3749; -.
DR   Proteomes; UP000036477; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.340; -; 1.
DR   InterPro; IPR012736; DhaK_1.
DR   InterPro; IPR004006; DhaK_dom.
DR   InterPro; IPR004007; DhaL_dom.
DR   InterPro; IPR036117; DhaL_dom_sf.
DR   NCBIfam; TIGR02363; dhaK1; 1.
DR   PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR   PANTHER; PTHR28629:SF4; TRIOKINASE_FMN CYCLASE; 1.
DR   Pfam; PF02733; Dak1; 1.
DR   Pfam; PF02734; Dak2; 1.
DR   SMART; SM01120; Dak2; 1.
DR   SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR   SUPFAM; SSF101473; DhaL-like; 1.
DR   PROSITE; PS51481; DHAK; 1.
DR   PROSITE; PS51480; DHAL; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..327
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          372..581
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
SQ   SEQUENCE   590 AA;  63218 MW;  9547DA20E85C2AE8 CRC64;
     MKKIINNPQN VVMEMCNGIV LAHPDLELIP KYKIIKKRDV NKEKVILISG GGSGHEPAHA
     GFVGDGLLDA AVCGDVFASP SQIQVYQAIR ETAGDKGTLL IIKNYSGDIM NFKNAAYLAK
     EDGISVDYIK VDDDIAVKDS LYTVGRRGVA GTVFVHKIAG AAAERGMDLA QVKRLAEKTV
     ANVKSIGFAF TSCTVPAKGT PTFVLGDDEM EYGVGIHGEP GIKREKLITA DELAMKMVDA
     LLEELKPDTD QEIALLVNGF GATPAQELYL LNNSVNKELA KHPVIVSRTL VGSYMTSIDM
     AGASLSILKL DEELKGLLSA PCSAPVFTIQ DWKQSIPYTP AGNMSGTGVK ASYEIETSPD
     YAIIHHNCIS LQNMVYMIDC MSASVIRNEV PFCELDSHAG DGDFGMSIAK GFRRLKMEWN
     EIITHHTDTI GNFLDACSLV IMEHCGGASG PIWGSAFRAA GKYAQAKTEL TISEFAQMLQ
     ASVKGIQATG ERSFGRGAEI GDKTLIDAFL PCANTWSLCA KAGEDISTTL IRAAKAAEDG
     AKATEKIVAR MGRAGTVGER SLGYPDAGAY GLGVIFRDIA EAMKVHGIDY
//
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