PDK1B_XENLA
ID PDK1B_XENLA Reviewed; 339 AA.
AC Q6NU98;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Serine/threonine-protein kinase pdik1l-B;
DE EC=2.7.11.1;
GN Name=pdik1-b;
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=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BC068699; AAH68699.1; -; mRNA.
DR RefSeq; NP_001084589.1; NM_001091120.1.
DR RefSeq; XP_018100452.1; XM_018244963.1.
DR AlphaFoldDB; Q6NU98; -.
DR SMR; Q6NU98; -.
DR DNASU; 414541; -.
DR GeneID; 414541; -.
DR KEGG; xla:414541; -.
DR CTD; 414541; -.
DR Xenbase; XB-GENE-919823; pdik1l.L.
DR OMA; XAFELEL; -.
DR OrthoDB; 813266at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 414541; Expressed in blastula and 19 other tissues.
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:0006468; P:protein phosphorylation; 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 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..339
FT /note="Serine/threonine-protein kinase pdik1l-B"
FT /id="PRO_0000086499"
FT DOMAIN 8..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 339 AA; 38508 MW; 87AC29522E531DFC CRC64;
MVSSQPKYDL IREVGRGSYG LVYEALVRRT GQRVAVKKIR CQAPENVELA LREFWALSSI
QSQHPNVIHL EECVLQRDGM VQRMLHGSSS VLYLPLVETS LKGEIAFDPR STYCLWFVMD
FCDGGDMNEY ILTRRPSRRT NTSFMLQLSS ALAFLHKNQI IHRDLKPDNI LVCKSRDGVD
EPTLKVADFG LSKVCSSSGL NPEEPANVNK SFLSTACGTD FYMAPEVWEG HYTAKADIFA
LGVILWAMLE RITITDTHTK KRLLGGYVQR GAQVVPVGEA LLENPKLELL IPVKKKSMNR
RMKQLLRQML SANPQERPDA FQLELKLIQI AFRDFTWET