ID F7CNQ2_ORNAN Unreviewed; 973 AA.
AC F7CNQ2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=NEK9 {ECO:0000313|Ensembl:ENSOANP00000012344.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000012344.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000012344.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000012344.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000012344.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000012344.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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 AlphaFoldDB; F7CNQ2; -.
DR STRING; 9258.ENSOANP00000012344; -.
DR Ensembl; ENSOANT00000012346.3; ENSOANP00000012344.3; ENSOANG00000007750.3.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000156145; -.
DR HOGENOM; CLU_676074_0_0_1; -.
DR InParanoid; F7CNQ2; -.
DR OMA; TKRMSCD; -.
DR OrthoDB; 198307at2759; -.
DR Proteomes; UP000002279; Chromosome 1.
DR Bgee; ENSOANG00000007750; Expressed in fibroblast and 7 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
DR CDD; cd08221; STKc_Nek9; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR44535; PROTEIN CBG16200; 1.
DR PANTHER; PTHR44535:SF1; SERINE_THREONINE-PROTEIN KINASE NEK9; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 3.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50012; RCC1_3; 6.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 49..305
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 385..441
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 442..495
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 496..547
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 548..612
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 613..665
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 666..723
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 106990 MW; 4410067E25921D8E CRC64;
MSVLGQYERH CDSINSDFGS GSGPDPDPHP RPGSGPRPGP GAEQEELHYI PIRVLGRGAF
GEATLYRRTE DDSLVVWKEV DLTRLLEKER RDALNEIVIL ALLQHDNIIA YYNHFMDNST
LLIELEYCNG GNLYDKILRQ KDKLFEEEMV LWYLFQIVSA VSCIHRAGIL HRDIKTLNIF
LTKANLIKLG DYGLAKKLNS EYSMAETLVG TPYYMSPELC QGVKYNFKSD IWAVGCVIFE
LLTLKRTFDA TNPLNLCVKI VQGIRAMEVD SSLYSLELIQ MVHTCLDQDP EKRPTADELL
NRPLLRKHRR EMEEKVALLN GPTKRPRSST ANETPIAVVT SRTSEVYVWG GGKSTPQKLD
VIKSGCSARQ VCAGNTHFAV VTVEKELYTW VNMQGGTKLH GQLGHGDRAS YRQPKHVEKL
QGKAIHQVSC GDDFTVCITD EGQLYAFGSD YYGCMGMDKV AGSEVLEPMQ LNFFLNNPVE
QVSCGDNHVV VLTRNKEVYS WGCGEYGRLG LDSEEDFYTP QKVDVPKALV IVSVQCSCDG
SFLLTQSGKV LACGLNEFNK LGLNQCMSGI INHEAYHEVP YTTSLTLAKQ LSFYKIRTIA
PGKTHTAAID ERGRLLTFGS NKCGQLGVGD YKKRLGINLL GGPLGGKQVI RVSCGDEFTI
AATDDNHIFA WGNGGNGRLA MTPTEKPHGS DICTSWPRPI FGSLHHVPDL SCRGWHTILI
VEKVLNSKTI RSNSSGLSIG TGAQSSTQGG NGSGEEEETQ RVSETPDPSG GFRGTMEADR
GIGGLLSPPE AMGVSSVGSS SCPGWLRKEL ENAEFIPMPD SPSPLSAAFS EPEKETLPYE
ELQGLKVASE APAECNKPTT EAWPPRLTPA PGCVGKGVPP AAACVCSSLQ VEVERLRGLV
LKCLAEQQLL QEENLRICSQ LQRLQKGMEG TQQLETHSRR TQTAKEEMET DTKPDLDSDS
WCLLGTDSLR SGL
//
