YPK1_CRYNH
ID YPK1_CRYNH Reviewed; 575 AA.
AC J9W0G9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Serine/threonine-protein kinase YPK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9P7J8};
GN Name=YPK1 {ECO:0000303|PubMed:22339665};
GN ORFNames=CNAG_04678 {ECO:0000312|EMBL:AFR97540.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-274; ASP-386;
RP THR-402; SER-543 AND SER-562.
RX PubMed=22339665; DOI=10.1111/j.1365-2958.2012.08016.x;
RA Lee H., Khanal Lamichhane A., Garraffo H.M., Kwon-Chung K.J., Chang Y.C.;
RT "Involvement of PDK1, PKC and TOR signalling pathways in basal fluconazole
RT tolerance in Cryptococcus neoformans.";
RL Mol. Microbiol. 84:130-146(2012).
CC -!- FUNCTION: Probable serine/threonine-protein kinase which may act in the
CC sphingolipid-mediated signaling pathway (PubMed:22339665). May act
CC downstream of TORC2 (TOR complex 2) and PDK1 to regulate sphingolipid
CC metabolism (PubMed:22339665). {ECO:0000269|PubMed:22339665}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9P7J8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9P7J8};
CC -!- DISRUPTION PHENOTYPE: Decreases virulence in a mouse systemic infection
CC model (PubMed:22339665). Sensitive to: high temperature; sirolimus;
CC fluconazole; myriocin (phytosphingosine biosynthesis inhibitor);
CC aureobasidin A (inositol-containing sphingolipid biosynthesis
CC inhibitor); phytosphingosine (PubMed:22339665). Abnormal sphingolipid
CC metabolism (PubMed:22339665). {ECO:0000269|PubMed:22339665}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000305}.
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DR EMBL; CP003829; AFR97540.1; -; Genomic_DNA.
DR RefSeq; XP_012052138.1; XM_012196748.1.
DR AlphaFoldDB; J9W0G9; -.
DR SMR; J9W0G9; -.
DR EnsemblFungi; AFR97540; AFR97540; CNAG_04678.
DR GeneID; 23888064; -.
DR VEuPathDB; FungiDB:CNAG_04678; -.
DR HOGENOM; CLU_000288_120_1_1; -.
DR Proteomes; UP000010091; Chromosome 10.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
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 Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..575
FT /note="Serine/threonine-protein kinase YPK1"
FT /id="PRO_0000451208"
FT DOMAIN 245..500
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 502..573
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 251..259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MUTAGEN 274
FT /note="K->A: Sensitive to fluconazole (cell wall stress
FT inducer)."
FT /evidence="ECO:0000269|PubMed:22339665"
FT MUTAGEN 386
FT /note="D->A: Sensitive to fluconazole (cell wall stress
FT inducer)."
FT /evidence="ECO:0000269|PubMed:22339665"
FT MUTAGEN 402
FT /note="T->A: Decreases YPK1 protein level, sensitive to
FT fluconazole (cell wall stress inducer)."
FT /evidence="ECO:0000269|PubMed:22339665"
FT MUTAGEN 543
FT /note="S->A: Sensitive to fluconazole (cell wall stress
FT inducer)."
FT /evidence="ECO:0000269|PubMed:22339665"
FT MUTAGEN 562
FT /note="S->A: Decreases YPK1 protein level."
FT /evidence="ECO:0000269|PubMed:22339665"
SQ SEQUENCE 575 AA; 63923 MW; 48BE1BC42D474330 CRC64;
MMSWKFGKKF KEGGFLSGKH HSSNNNSPSD TSRSTTPTPG NPHPEDAVKP PVPRSGMLKI
RVTAAKGLSL PQGVSVPAPV QEALTTHPTL ASRIATSPPT AIVKAAGANR DSLQRRQVWW
LPYLVLEFDK NEVLVDALGG DLASPVWMYS ATFDVSRISE ISATVYLRTR EPHAEGREKS
NGEGEGEDMG NSDLCLGSIR FTPNLDSLRV TDDWVTVQGG GGSGSINVQV SFKPASGQIL
TIDSFELLKV IGKGSFGKVM QVRKRDTLRI YALKTIRKAH IVSRSEVTHT LAERTVLAQV
NCPFIVPLKF SFQSKEKLYL VLAFINGGEL FHHLQREGKF NETRSRFYSA QLLLALEHLH
SFNVIYRDLK PENILLDYAG NIALCDFGLC KLNMSNSDTT NTFCGTPEYL APELLSGHGY
TKCVDWWTLG VLLYEMLTGL PPFYDENTNE MYRKILTEPL RFPDGVRSEA RSLLTGLLNR
DPRQRLGVNG AQDIKNHPFF AKHINFTKLW NKQIQPPFKP AVASAIDTSN FDEEFTNEVP
LDSVVDDSHL SQTVQQQFEG FSWSVSPLGE SVGRY
