ID   WEE2C_XENLA             Reviewed;         554 AA.
AC   Q6DFE0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Wee1-like protein kinase 2-C;
DE            EC=2.7.10.2;
GN   Name=wee2-c;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein tyrosine kinase that phosphorylates and inhibits cdk1
CC       and acts as a regulator of meiosis in oocytes. Required to ensure the
CC       meiotic cell cycle in oocytes by phosphorylating cdk1 at 'Tyr-15',
CC       leading to inhibit cdk1 activity and prevent meiosis (By similarity).
CC       {ECO:0000250}.
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=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; BC076799; AAH76799.1; -; mRNA.
DR   AlphaFoldDB; Q6DFE0; -.
DR   SMR; Q6DFE0; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
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   InterPro; IPR017164; Wee1-like_protein_kinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF037281; Wee1-like_protein_kinase; 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   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Kinase; Magnesium; Meiosis; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..554
FT                   /note="Wee1-like protein kinase 2-C"
FT                   /id="PRO_0000409530"
FT   DOMAIN          213..487
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          490..516
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        22..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         219..227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  61412 MW;  EFE3B011E2E66E06 CRC64;
     MRTAMSCGGG LVQRLDFSSS EEEDGLSNGI NEAPQKGSPV SSWRTNNCPF PITPQRNERG
     LSPTQELSPS SDYSPDPSDK GAGGECPGTP LHYSTWKKLK LCDTPYTPKS LLYKTLPSPG
     SRVHCRGQRL LRFVAGTGAE TEDPTLVNVN PFTPQSYRQT HFQPNGKRKE RPEDDCSSDS
     QMKFTDKEHP SVFQSKRFVL RETNMESRYK TEFLEIEKIG AGEFGSVFKC VKRLDGCFYV
     IKRSKKPLAG STDEQLALRE VYAHAVLGHH PHVVRYYSAW AEDDHMIIQN EYCNGGSLQD
     LIMENNKKGQ FVPEQELKEI LLQVSMGLKY IHGSGLVHMD IKPSNIFICR KQTEVGEDES
     DGEDDVSSAS VLYKIGDLGH VTSILNPQVE EGDSRFLANE ILQEDYRQLP KADIFALGLT
     IALAAGAAPL PCNEDGWHHI RKGNLPHIPQ PLTPAFLALL KLLVHPDPAT RPPAASLAKN
     SVLRRCVGKA AELQKQLNVE KFKTAMLERE LQAAKLAQDE CLDLPPVSGF SCRGRKRLVG
     AKNARSLSFT CGGY