ID A0A084QRN1_STAC4 Unreviewed; 316 AA.
AC A0A084QRN1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ACT domain-containing protein {ECO:0000259|PROSITE:PS51671};
GN ORFNames=S40285_03024 {ECO:0000313|EMBL:KFA66616.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA66616.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA66616.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA66616.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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}.
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DR EMBL; KL660417; KFA66616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QRN1; -.
DR STRING; 1283841.A0A084QRN1; -.
DR HOGENOM; CLU_055003_0_0_1; -.
DR InParanoid; A0A084QRN1; -.
DR OMA; KHEHLND; -.
DR OrthoDB; 1361624at2759; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000028524; 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:UP000028524}.
FT DOMAIN 85..159
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 316 AA; 34380 MW; B7DE1E26B0A22F44 CRC64;
MASLRPLVAP LRWAASAKTL PAGSLGAVRY SSSSSTSAIA YKALRRRSSP LPVTEAPPAW
SASAAVSNIL YETPTPSMAP PKRHILNCLV QNEPGVLSRL SGILAARGFN IDSLVVCNTE
VEDLSRMTIV LTGQDGVVEQ ARRQLEDLVP VWAVLDYSNA ALVQRELLLA KINILGPEYF
EELLTHHREI TTGDLEAEHE ASEQSLEETA KDFHPSKLAA SEALRHKHEH LKSITYFTHQ
FGGKVLDIST NSCIVEVSAK PSRIDSFLKL VVPFGILESA RTGLMALPRS PLHNPNEEVM
LKDADEVVDA SQLPPG
//
