NEK9_XENLA
ID NEK9_XENLA Reviewed; 944 AA.
AC Q7ZZC8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Serine/threonine-protein kinase Nek9;
DE Short=xNek9;
DE EC=2.7.11.1;
DE AltName: Full=Nercc1 kinase;
DE AltName: Full=Never in mitosis A-related kinase 9;
DE Short=NimA-related protein kinase 9;
GN Name=nek9;
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 [MRNA].
RA Roig J., Avruch J.;
RL Submitted (APR-2003) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Dimerizes through its coiled-coil domain. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AY271412; AAP31900.1; -; mRNA.
DR AlphaFoldDB; Q7ZZC8; -.
DR SMR; Q7ZZC8; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd08221; STKc_Nek9; 1.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042767; Nek9_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 3.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 6.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..944
FT /note="Serine/threonine-protein kinase Nek9"
FT /id="PRO_0000086437"
FT DOMAIN 34..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 370..426
FT /note="RCC1 1"
FT REPEAT 427..480
FT /note="RCC1 2"
FT REPEAT 481..532
FT /note="RCC1 3"
FT REPEAT 533..597
FT /note="RCC1 4"
FT REPEAT 598..650
FT /note="RCC1 5"
FT REPEAT 651..708
FT /note="RCC1 6"
FT REGION 726..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 835..890
FT /evidence="ECO:0000255"
FT COMPBIAS 765..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 192
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 944 AA; 104540 MW; E0B36623378E15F2 CRC64;
MSALGRYDRH CDSINSDFGD SVRSCGPEQE ELHYIPIRVL GHGAYGEATL YRRTEDDSLV
VWKEVGLARL SEKERRDALN EIVILSLLQH DNIIAYYNHF LDSNTLLIEL EYCNGGNLFD
KIVHQKAQLF QEETVLWYLF QIVSAVSCIH KAGILHRDIK TLNIFLTKAN LIKLGDYGLA
KQLSSEYSMA ETCVGTLYYM SPEICQGVKY SFKSDIWAVG CVLYELLTLT RTFDATNPLN
LCVKIVQGNW AVGLDNTVYT QELIEVVHAC LEQDPEKRPT ADEILERPIL SWRRRDMEEK
VSMLNRSNKK PRTGTVTEAP IAVVTSRSSE VYVWGGGKTT PQKLDVFKGG WRARQVCAGD
AHFAVVTVEK ELYTWVNMQG GSKLHGQLGH GDRASYRQPK HVEKLQGKSV QKVSCGSDFT
VCITDEGQLY SFGSDYYGCL GVNQSAGSEV LEPLLVDFFL NEPVDQVSCG DSHIMALTRS
KSVYSWGCGE YGRLGLDSED DVYSPQKVEV QRGLCIVNVC CGSDGSFLLT LTGKVLACGL
NEHNKLGLNQ YTAGIINHEA FQEVPYTTSL TLAKQLSFYK IRSISPGRTH TAAIDERGRL
LTFGSNKCGQ LGVGDYRKHL GINLLGGPLG GKQVIRVSCG DEFTTAATAD NHIFAWGNGG
NGRLAMTPNE RPQGSDICTS WPRPIFGSLH HVTDLSCRGW HTILIVEKVL NSKTIRSNSS
GLSIGTLAQS CSSGGSGSRE EDSDRESLTS DPSRGFRGTI EAEPETGPFN TTENMESSSC
PSWLRQELEE AEFIPMPDTP NFVSAESSQN GTTSMQDVRE TPPDALEKPS FQACTCSTLQ
EEVRKLQDLV STYRHEQELL CRENSRLALE VQELNGKLQS AMQMNQVVNK HGEAIHQIQK
QLSLHWKSSP PSSGNPEMSR EDSDAESWCF LGTEACRSSS GTPM
