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Database: UniProt
Entry: A0A1Y1UIC2_9TREE
LinkDB: A0A1Y1UIC2_9TREE
Original site: A0A1Y1UIC2_9TREE 
ID   A0A1Y1UIC2_9TREE        Unreviewed;       382 AA.
AC   A0A1Y1UIC2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Small subunit of acetolactate synthase-domain-containing protein {ECO:0000313|EMBL:ORX37234.1};
GN   ORFNames=BD324DRAFT_625368 {ECO:0000313|EMBL:ORX37234.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX37234.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX37234.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX37234.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC   -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC       {ECO:0000256|ARBA:ARBA00006341}.
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:ORX37234.1}.
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DR   EMBL; NBSH01000006; ORX37234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1UIC2; -.
DR   STRING; 4999.A0A1Y1UIC2; -.
DR   InParanoid; A0A1Y1UIC2; -.
DR   OrthoDB; 1361624at2759; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000193218; Unassembled WGS sequence.
DR   GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04878; ACT_AHAS; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.70.1150; ACT-like. Chain A, domain 2; 1.
DR   InterPro; IPR004789; Acetalactate_synth_ssu.
DR   InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR   InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR039557; AHAS_ACT.
DR   NCBIfam; TIGR00119; acolac_sm; 1.
DR   PANTHER; PTHR31242; ACETOLACTATE SYNTHASE SMALL SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR31242:SF2; ACETOLACTATE SYNTHASE SMALL SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF10369; ALS_ss_C; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193218}.
FT   DOMAIN          106..183
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  40377 MW;  012B4DFEA73C88FC CRC64;
     MSLRRALTGI TPLKRGSSPL LSTSTRCASS TSSSSSANAT GSSNPPKAPK SIDDSTSALD
     YKMHRPIRRM PHVTTPPPRA PSVEEAVTNI LYNTPPPSTE PYKRHLLNCL VQNEPGVLSR
     VSGIIAARGF NIDSLVVCAT EIRDLSRMCI VLKGQDGVVE QARRQLEDLV PVWAVLDYTQ
     TPKIERELLL AKVSILGPEF AAAQLGSSPT GSDSQSFDAA IDHQDSAHPP SFVGQSSSGS
     ESTSGGSGGA GGAGDKYERE QALARSFESS GSSPSLYPAR QSGLSVSEAL IAKNLHLGAI
     KTLTDQFGGK VVDVADSSCI VELTAKSSRV EAFLNLIRPF GLLEAARSGV MVLPRTPLAR
     WGEEEEVAIE RGEVDASMLP PG
//
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