NEK3_DICDI
ID NEK3_DICDI Reviewed; 1123 AA.
AC Q86I06; Q554H8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable serine/threonine-protein kinase nek3;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis protein A-related protein kinase 3;
DE AltName: Full=NimA-related protein kinase 3;
GN Name=nek3; ORFNames=DDB_G0275241;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69901.1; -; Genomic_DNA.
DR RefSeq; XP_643733.1; XM_638641.1.
DR AlphaFoldDB; Q86I06; -.
DR SMR; Q86I06; -.
DR STRING; 44689.DDB0220003; -.
DR PaxDb; Q86I06; -.
DR PRIDE; Q86I06; -.
DR EnsemblProtists; EAL69901; EAL69901; DDB_G0275241.
DR GeneID; 8619775; -.
DR KEGG; ddi:DDB_G0275241; -.
DR dictyBase; DDB_G0275241; nek3.
DR eggNOG; KOG0589; Eukaryota.
DR HOGENOM; CLU_280118_0_0_1; -.
DR InParanoid; Q86I06; -.
DR OMA; SMTPVTE; -.
DR PRO; PR:Q86I06; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1123
FT /note="Probable serine/threonine-protein kinase nek3"
FT /id="PRO_0000362028"
FT DOMAIN 4..264
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 283..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1123 AA; 120809 MW; 69DFDE5E2B0A3283 CRC64;
MDKYEEIKTI GKGSFGRAIL VKRKSDGLLL VLKEINVMEM QPKERSDAMN EVNLLSMLDH
ENIIGYYDSF ILNGCLYIIM EYANAGDINL EIKKRTLQNK TFSEFEILSW FSQICKALQY
ISSRNILHRD LKTQNIFLSI VNGDYFIKLG DFGIAKILNS ETSLASTVLG TPYYLSPELI
QNEKGYDHKS DIWSLGCVLY ELTTLKHAFN AANLPALVLK ILKGTYPPIP SHYSNDLRNL
ISSMLQIDPK NRPSVNDILE LPFINQYLGI PLKPFDSNLN ENNNDSLNIS NNSSGSNNSA
SNNISSSTEV KDQKFQNIPL AMARNINNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNKSNV DDVNSSSTTT TSSSIVKSKV NTTVSPPLSP KKPITTTTTK TTSLKTTPSI
KPTLVKTPTI KSSLVKTPLS KTPISGTKNP TTSKITPSIK TPLPKAPISS KTPTRLVSKP
TTPKITTPKS TSTMITPKRT TTTTTTPTPT TATTTPKKSS LSSSSSSSVK PPPPTTTTTT
PSKDRSSVNT INKPMASNLS SQISSSSSSS SSSNSQFRPT TPSKERMSPT STSTKSPTNP
SPTLSSSSSL PKSSLKSDSL CTSPPRFSNT TGSSGGIGVS GNGNSNVNST VLNRSVSSLS
IQHKPTNSGS SSISSSSSGN NSNSNTTTNN NTTSTTPIRP GLKSTKSMLE LSTPTSISTS
NKSTTTTPTS SRSNTPSTGR LSLTTSIPRP PSSNGSNTGS SSSTTTTPTK ISTTSSSSSL
NKLTTPIKSS TTTSTTASTN SQTIKKSITP IKVTSQQVDS TISNIKNNIV IGNSVSTKTN
ISVISHLSPS IKPLPTQSII TQLPTSASTA STASTTNTTL TSGTNTMTTK KRTDFKLDDL
GHRSKLNSVK LSSKSSSPIK TSSSSSSSSS SSSSITDKKS INRVKLNNLK EKNKEIINNI
KISSTIPKPS NINSSSSSAF SDLNSSGSSS LNNSLTSSSS SIITNQNNQN NQNNQNNQNN
QNNLKIINEL ILQNNLNNSI SKENLDDKRL HSRANALRHF CSSIFGEDKF KETYNLLKSQ
SPSTSNNEIV DIASIENQLS QLIGDKIYYL KYLQQLIYCE SQI