ID A0A2B7XAE1_9EURO Unreviewed; 921 AA.
AC A0A2B7XAE1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=STE/STE11 protein kinase {ECO:0000313|EMBL:PGH08614.1};
GN ORFNames=GX51_01134 {ECO:0000313|EMBL:PGH08614.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH08614.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH08614.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH08614.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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:PGH08614.1}.
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DR EMBL; PDNC01000008; PGH08614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XAE1; -.
DR STRING; 2060905.A0A2B7XAE1; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000224080; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0000165; P:MAPK cascade; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09534; SAM_Ste11_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:PGH08614.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW Transferase {ECO:0000313|EMBL:PGH08614.1}.
FT DOMAIN 68..131
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 640..916
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 669
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 921 AA; 101890 MW; 5915348255691E70 CRC64;
MLSSQPQYSA GLPLHTPSQL SSSLSTPYMS LPSHKSGLPT ATRDGPFSSP TESEFSDGYD
GLDSVRSWDE KKVILWLHSI RCGQYEALFK ANHFNGDNLL DCDQKILQEM GIKKIGDRVR
IFVAIKQLRN RNVSNRKKRN RDSLAALDSA QFTPSSSESP RAANSRQQGA GNRRRSRHAD
PPSLTGYNTS YTASGRASSR PSSPPADSDR GLRSYRYPGA SPMEGSRRDQ GSNYFNYYSD
SASSNSGTPA EVPQTARTVM HIRQNPSMDG ITMGSLPPNS PVIRVIHSGG QTKVLNIKHC
KTPEDIIICV LRKLLLPESH YKNYCFYVLD GLDPNPDNCR RLSDSELLKI CDGFHRSERG
RLILRKIHAG EPEPEELHRA SQIALDESQT AHLNALSGTN VRNQIKLQKL TGESWHNIRQ
PLSPLSATDR NREEFQRQTP SERHQSAKLR SFFGARPPSE MIIHELTSYF PSHQKEDIEK
TMRLSVRRSQ RMSRAASRLS VVSNLSYASS LKDAPPIPSI ADTWLTGTNG STRTARPLSV
SKFNLPQMSF RDSIASSLQP LQEESPIEPN RKSYVSFDSG SDHTPGETDR QTFLDETISL
STPDGGINER LSMIVAEDGE EADDGLAAFL AGDNFGNKNW MKGSLIGEGS FGSVFLALHS
ITGELMAVKQ VELPSATKGT EFDQRKNSMV TALKHEIDLL QGLQHPNIVQ YLGTSTDEHH
LNIFLEYVPG GSIAMMLKQY NTFQEPLIKN FVRQILAGLS YLHSRDIIHR DIKGANVLVD
NKGGIKISDF GISKRVEAST VLGSNANLGG GAGHLHRPSL QGSVYWMAPE VVRQTAHTKK
ADIWSLGCLV VEMFIGAHPF PDCSQLQAIF AIGSNQARPP PPENASKEAM AFLDMTFEIN
HEKRPSADEL LSSPFLSQQM P
//
