ID A0A317VBG2_ASPEC Unreviewed; 489 AA.
AC A0A317VBG2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE SubName: Full=MAPKKK cascade protein kinase regulator Ste50 {ECO:0000313|EMBL:PWY70719.1};
GN ORFNames=BO83DRAFT_315391 {ECO:0000313|EMBL:PWY70719.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY70719.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY70719.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY70719.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY70719.1}.
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DR EMBL; MSFU01000016; PWY70719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VBG2; -.
DR VEuPathDB; FungiDB:BO83DRAFT_315391; -.
DR OrthoDB; 1423392at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01786; RA_STE50; 1.
DR CDD; cd09533; SAM_Ste50-like_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24135:SF28; LD13733P; 1.
DR PANTHER; PTHR24135; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PWY70719.1};
KW Transferase {ECO:0000313|EMBL:PWY70719.1}.
FT DOMAIN 67..130
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 382..455
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53817 MW; F8C74842B2C037D5 CRC64;
MSLHTSYHAD SDADDEYERS VITSPHLATD SEASPSESEF PSAEHTPTTL ANVDENPRSP
RTIITEWTAE ECANFVAALG LRQYCAAFLE NEIVGEALIA LKHDELKEMG IASVGHRLTI
LKSVYETKVK QDIPIDADHY IPLSADQSMN ETATQDDISR LIRSIRVRDD RIMSMESEMR
RIAEEYRRLR EELLPVFKMA KDKSQPLPPP SSVPASGSEG YHDGPTLTSS SGITLLDRSG
SILSRTFSKR NHTGGTTPKT NSPTHIPPSI HEGRMYSDGL DPSAANSSHL TMLNGKSQLS
PGIPSPTSPG NQYAPQTLAS RAYTQPSSSS INHVSHNHHD DTAASQSRPD RLNPTPTQST
RPDIPTRSDS RATQDPPSVE IFKSFRVSMD DPCHKVLPAA LKKYNINADW KQYALYIVYG
DQERCLGLEE RPLILFKQLE KEGRKPMFML RKQAHPIDSS MYSGGGSAPN SAGFEGGRQA
QINLPGGVL
//
