ID A0A166UFZ9_9AGAM Unreviewed; 283 AA.
AC A0A166UFZ9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=Butyrate kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBSPDRAFT_944734 {ECO:0000313|EMBL:KZP31656.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP31656.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP31656.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP31656.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV417488; KZP31656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166UFZ9; -.
DR STRING; 436010.A0A166UFZ9; -.
DR OrthoDB; 21304at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 1.
DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR21060; ACETATE KINASE; 1.
DR PANTHER; PTHR21060:SF19; ACETATE KINASE; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 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:UP000076532};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 283 AA; 30130 MW; 0F322BC38D3F988E CRC64;
MARKGDHILF VNSGSSSLKI NGNMLMDSQT RSYFARWLQL TIMMLDQQPS ESLNLIVLHL
GSGASACAIQ NGRSLDTSMG LTPLNGLPGA TRSGAVDPSL IFHYTNSAGK MSHDPKNARE
PALRVTEAEH ILNTQSGWQS LTGTADFGAI TAKAALASAP SDENAHRLAF DLFADRILNY
VGSYYVKLGG RVDALVFAGG IGEKGGELRA RIGKGVECVG FPEIDRDRNE GAAVGDGGVV
VGIGVDAAGE GKRILVCKTN EQLEMARQCA LEKKFWEEDG SET
//
