ID A0A1F7ZV21_9EURO Unreviewed; 485 AA.
AC A0A1F7ZV21;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=MAPKKK cascade protein kinase regulator Ste50 {ECO:0000313|EMBL:OGM43302.1};
GN ORFNames=ABOM_008674 {ECO:0000313|EMBL:OGM43302.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM43302.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM43302.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM43302.1}.
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DR EMBL; LYCR01000073; OGM43302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZV21; -.
DR STRING; 109264.A0A1F7ZV21; -.
DR OrthoDB; 1423392at2759; -.
DR Proteomes; UP000179179; 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:OGM43302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transferase {ECO:0000313|EMBL:OGM43302.1}.
FT DOMAIN 67..130
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 379..452
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 54008 MW; 3FC9935639FC35C9 CRC64;
MSLHTSYHAD SDADDEYERS VITSPHLATD SEASPSESDF PSSEQTPTTF ANADEHPKSP
RTIITEWTAE ECAHFLAALG LRQYCQSFLE NEIVGEALIA LKHDELKEMG IASVGHRLTI
LKSVYETKVK QDIPLDADHY IPLSADQSMN ETASQEDVAR LIQSIRLRDE RIVTVESELR
RMAEDYRRLR EELLPVFKMA KDRSQPLPPP TSMASSGPDG YHDSQQTLVS PSGITLLERS
ATLSRQISKR LHTGGTTPKN NSPTHIPPSI HEGRMYHDNG VLDPSSALYT NGKSQLSPGI
PSPTSPGVHY TAAQTLGSRS YQPTPNTSRS PYDHHDDASA TQTRERLNPT PTQPNRPDIP
TRSDSRAGNG NDPPSVEIFK SFRVSMEDPC YKVLPAALKK YNINADWKQY ALYIVYGDQE
RCLGLDEKPL ILFKQLEKEG RKPMFMLRKQ LQHPVENSYP PVNPVPTSAG FESRQAQINL
PGGVL
//