ID CDK9B_XENLA Reviewed; 376 AA. AC Q7ZX42; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Cyclin-dependent kinase 9-B; DE EC=2.7.11.22; DE EC=2.7.11.23; DE AltName: Full=Cell division protein kinase 9-B; GN Name=cdk9-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=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) CC complex, also called positive transcription elongation factor B (P- CC TEFb), which is proposed to facilitate the transition from abortive to CC production elongation by phosphorylating the CTD (C-terminal domain) of CC the large subunit of RNA polymerase II (RNAP II) and SUPT5H. CC {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=2.7.11.22; 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=2.7.11.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho- CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA- CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, CC ChEBI:CHEBI:456216; EC=2.7.11.23; CC -!- SUBUNIT: Associates with cyclin-T to form P-TEFb. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. 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; BC045247; AAH45247.1; -; mRNA. DR RefSeq; NP_001080537.1; NM_001087068.1. DR AlphaFoldDB; Q7ZX42; -. DR SMR; Q7ZX42; -. DR IntAct; Q7ZX42; 1. DR DNASU; 380229; -. DR GeneID; 380229; -. DR KEGG; xla:380229; -. DR AGR; Xenbase:XB-GENE-6256565; -. DR CTD; 380229; -. DR Xenbase; XB-GENE-6256565; cdk9.L. DR OrthoDB; 244018at2759; -. DR Proteomes; UP000186698; Chromosome 8L. DR Bgee; 380229; Expressed in gastrula and 19 other cell types or tissues. DR GO; GO:0070691; C:P-TEFb complex; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0120187; P:positive regulation of protein localization to chromatin; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; ISS:UniProtKB. DR CDD; cd07865; STKc_CDK9; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF546; CYCLIN-DEPENDENT KINASE 9; 1. DR Pfam; PF12330; Haspin_kinase; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Transcription; Transcription regulation; KW Transferase. FT CHAIN 1..376 FT /note="Cyclin-dependent kinase 9-B" FT /id="PRO_0000085805" FT DOMAIN 19..319 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 345..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..370 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 153 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 25..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 376 AA; 43249 MW; 7D35719EF2B0E22E CRC64; MVKNYDSVEF PYCDEVSKYE RLAKIGQGTF GEVFKAKHRQ TGKKVALKKV LMENEKEGFP ITALREIKIL QLLKHENVVH LIEICRNKIS PTANQYNRCK GTIFLVFDFC EHDLAGLLSN AHVKFTVAEI KKVMQMLLNG LYYIHRNKIL HRDMKAANVL ITRDGVLKLA DFGLARAFSL AKNSQPNKYT NRVVTLWYRP PELLLGERDY GPPIDLWGAG CIMAEMWTRS PIMQGNTEQH QLTLISQLCG SITPEVWPNV DKYELYQKLE LPKGQKRKVK ERLKAYVKDV CALDLIDKLL ILDPAQRTDS DEALNHDFFW SDPMPSDLKN MLSTHNQSMF EYLAPPRRRG GHMPQQPANQ ARNPAATNQS EFDRVF //