ID A0A395I9I3_ASPHC Unreviewed; 490 AA.
AC A0A395I9I3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=MAPKKK cascade protein kinase regulator Ste50 {ECO:0000313|EMBL:RAL14804.1};
GN ORFNames=BO97DRAFT_432506 {ECO:0000313|EMBL:RAL14804.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL14804.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL14804.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL14804.1,
RC ECO:0000313|Proteomes:UP000248961};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824273; RAL14804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I9I3; -.
DR STRING; 1450537.A0A395I9I3; -.
DR VEuPathDB; FungiDB:BO97DRAFT_432506; -.
DR OrthoDB; 1423392at2759; -.
DR Proteomes; UP000248961; 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:RAL14804.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Transferase {ECO:0000313|EMBL:RAL14804.1}.
FT DOMAIN 67..130
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 383..456
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 53829 MW; D20C835C4BD4395E CRC64;
MSLHTSYHAD SDADDEYERS VITSPHLATD SEASPSESDF PSAEHTPTTL ANVEDNPRSP
KTIITEWTAD ECAHFVAALG LRQYCAAFLE NEIVGEALIA LKHDELKEMG IVSVGHRLTI
LKSVYETKVK QDIPLDADHY IPLSADQSMN DGATQDDVAR LIQSIRLRDE RIVTVEQELR
RMAEDYRRLR EELLPVFKMA KDRSQPLPPP SAVPGSGNEA HHEPPNLTSP SGITILDRSG
SILSRTFSKR VHTGGTTPKT SSPTYIPPSI HEGRMYSDGG GLDPSTANSS HMAMMNGKAQ
LSPGIPSPTS PGILHTQTLA SRAYSQPSSA SINHASYNHH DDTPPTQSRS DRLNPTPTQA
TRPDIPTRSD SRATGDPPSV EIFKSFRVSM DDPCHKVLPA ALKKYNINAD WKQYALYIVY
GDQERCLGLE ERPLILFKQL EKEGRKPMFM LRKQVHPLEN NVYAAGSGSA PNSAGFEGRQ
AQINLPGGVL
//
