ID A0A0J6Y8K9_COCIT Unreviewed; 894 AA.
AC A0A0J6Y8K9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Kinase byr2 {ECO:0000313|EMBL:KMP03083.1};
GN ORFNames=CIRG_02775 {ECO:0000313|EMBL:KMP03083.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP03083.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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}.
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DR EMBL; DS028094; KMP03083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6Y8K9; -.
DR STRING; 404692.A0A0J6Y8K9; -.
DR Proteomes; UP000054565; 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; IPR000159; RA_dom.
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; PS50200; RA; 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:KMP03083.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:KMP03083.1}.
FT DOMAIN 64..127
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 250..340
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 617..889
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 126..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 894 AA; 98751 MW; 6AC2EC05FCAA4F0D CRC64;
MMLGTQNPYT AVLPSIPSAI SSTYMTLPGK GQAGSMLNRE GVFSSPTESE FSEGCDGFDS
VRLWDEKKVA DWLHSIRCGQ YEAIFKANHF NGDNLLDCDQ KILQEMGIKK VGDRVRISVA
VKQLRTKSVS SRKKKNRDSF VALDSSRFTP PSAESPRPST ARQQPSNSRQ WPRHENGKGS
PRAASPLTEH DRGLRPYRYA GASPVESARR EQGGSYFSRP SDPSQSSRAA AHMRQAPSID
GLTMGALPPN SPVIRVIYTG GQTKVLNVKH CKTAEEVMLA VLRKLLLPES HFRNYCFYVL
DGLDPDPANC RRISDSELLQ ICDGSGRSER GRLILRKLHA GEPEAEELQR AAQLAMDENQ
VAHMNALSTT NVRNQIKLQK LTGESWHNIR QPRSPLTATD RHRDDYPKIA TAKAGDRQQS
TKLRSFFGAR PPSEMIIHEL TSYFPSHQKE DIEKTMRLSV RRSQRLSRAA SRLSVVSNIS
LASSLKDAPP IPSIADTWLT GAGQQPTRGS RPLSVSRFNL PQASFRDSIA SSNLQPLQEE
SPVEPNRKSY VSFDSASEIA GGESRQGFLD ESICLNAPDT GGSLNERLSI IVAEDGEEDD
DGLADFLAGN NFSNKNWMKG SLIGEGSFGS VFLALHAITG ELMAVKQVEL PSATKGTEFD
NKKTTMVNAL KHEISLLQGL QHPNIVQYLG TSTDDQYLNI FLEYVPGGSI ATMLKQYNTF
QEPLIRNFVR QILTGLSYLH SRDIIHRDIK GANVLVDNKG QIKISDFGIS KRVEASNMLS
AGGSARHLHR PSLQGSVYWM APEVVRQTAH TKKADIWSLG CLVVEMFIGA HPFPDCSQLQ
AIFAIGNNKA RPPPPENASK EATAFLDMTF EIDHEKRPSA DDLLNDPFLE TMIG
//
