YAK1_ENCCU
ID YAK1_ENCCU Reviewed; 405 AA.
AC Q8SQZ4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable dual specificity protein kinase YAK1 homolog;
DE EC=2.7.12.1;
GN Name=YAK1; OrderedLocusNames=ECU11_0180;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP PREDICTION OF FUNCTION.
RX PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA Barton G.J.;
RT "The complement of protein kinases of the microsporidium Encephalitozoon
RT cuniculi in relation to those of Saccharomyces cerevisiae and
RT Schizosaccharomyces pombe.";
RL BMC Genomics 8:309-309(2007).
CC -!- FUNCTION: Negative regulator of the cell cycle acting downstream of the
CC cAMP-dependent protein kinase. Part of a glucose-sensing system
CC involved in growth control in response to glucose availability (By
CC similarity). {ECO:0000250}.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between both compartments in response to glucose.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR EMBL; AL590450; CAD25928.1; -; Genomic_DNA.
DR RefSeq; NP_586324.1; NM_001042157.1.
DR AlphaFoldDB; Q8SQZ4; -.
DR SMR; Q8SQZ4; -.
DR STRING; 284813.Q8SQZ4; -.
DR GeneID; 859975; -.
DR KEGG; ecu:ECU11_0180; -.
DR VEuPathDB; MicrosporidiaDB:ECU11_0180; -.
DR HOGENOM; CLU_000288_5_15_1; -.
DR InParanoid; Q8SQZ4; -.
DR OMA; FEWENNI; -.
DR OrthoDB; 689446at2759; -.
DR Proteomes; UP000000819; Chromosome XI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..405
FT /note="Probable dual specificity protein kinase YAK1
FT homolog"
FT /id="PRO_0000384422"
FT DOMAIN 40..335
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 405 AA; 46339 MW; F3CFB2CAEB9FB706 CRC64;
MKKKVLTFPS EKIGFSSDNE EFDLVMARGD YLAKNKSQKY MIIDMLGTGT FGQVVRCVGS
DGEEVAIKVV KNQPKYYNYE MNEVRILHKL LYNNLNDRFV TIKDVFMYKQ HLCIVEELLG
RNLYTFLKMT RFKGLDHPTL RTILHQILEG MVQLSLLGII HCDLKPENIL IADYDTFKIK
IIDFGSAVTS PQGSHFYVQS RYYRAPEVIL GIPYGSSCDI WSLGCIGYEL YVGHPLFPGK
DNMDQIGRIH GLFGSLPMFM LEHGKNSSTF FEKENGYRFM GPPSNFTLED MKKMIRSKGN
SKEDDNMLIK FLLRALQPSH LIRPDAKSLA SHSYLKVRDT SAEADKACND RSGVQQNIFP
ANKNMRHMST TGVILPSKKQ KPTDDRRKIS VYGISYENNL NRDSE
