ID A0A227SJ92_CRYNV Unreviewed; 365 AA. AC A0A227SJ92; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 22-NOV-2017, entry version 2. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00652812}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00652812}; GN ORFNames=C355_05662 {ECO:0000313|EMBL:OXG45994.1}; OS Cryptococcus neoformans var. grubii Th84. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=1230067 {ECO:0000313|EMBL:OXG45994.1}; RN [1] {ECO:0000313|EMBL:OXG45994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Th84 {ECO:0000313|EMBL:OXG45994.1}; RA Cuomo C., Litvintseva A., Chen Y., Young S., Zeng Q., Chapman S., RA Gujja S., Saif S., Birren B.; RT "Global population genomics of the pathogenic fungus Cryptococcus RT neoformans var. grubii."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00652814}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361165, CC ECO:0000256|SAAS:SAAS00610829}; CC -!- ENZYME REGULATION: Activated by threonine and tyrosine CC phosphorylation. {ECO:0000256|RuleBase:RU361165}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. MAP kinase subfamily. CC {ECO:0000256|RuleBase:RU361165}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OXG45994.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AMKY01000070; OXG45994.1; -; Genomic_DNA. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008352; MAPK_p38. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00652810}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00652820, KW ECO:0000313|EMBL:OXG45994.1}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00652804}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00652809}; KW Transferase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00652816}. FT DOMAIN 20 299 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. SQ SEQUENCE 365 AA; 41213 MW; F28E2E95B6DAD6B5 CRC64; MADFVKLSIF GTVFEVTTRY VDLQPVGMGA FGLVCSAKDQ LSGTSVAIKK IMKPFSTPVL SKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY FLYQILRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR APEIMLTWQK YDVAVDIWST GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVIQT IASENTLRFV QSLPKREKVP FSTKFPNADP VSLDLLEKML VFDPRTRISA AEGLAHEYLA PYHDPTDEPV AAEVFDWSFN DADLPVDTWK VMMYSEILDF HNLGDISQNE AEGPVTGEVP AAPAS //