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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
 
 
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