BUB1_DICDI
ID BUB1_DICDI Reviewed; 1306 AA.
AC Q54CV5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable inactive serine/threonine-protein kinase bub1;
GN Name=bub1; ORFNames=DDB_G0292676;
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=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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. BUB1 subfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to other species, in which it plays an essential
CC role as component of the mitotic checkpoint, bub1 is predicted to be
CC inactive in D.discoideum. Its function is therefore highly unsure.
CC {ECO:0000305}.
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DR EMBL; AAFI02000194; EAL61141.1; -; Genomic_DNA.
DR RefSeq; XP_629565.1; XM_629563.1.
DR AlphaFoldDB; Q54CV5; -.
DR SMR; Q54CV5; -.
DR STRING; 44689.DDB0231500; -.
DR PaxDb; Q54CV5; -.
DR EnsemblProtists; EAL61141; EAL61141; DDB_G0292676.
DR GeneID; 8628825; -.
DR KEGG; ddi:DDB_G0292676; -.
DR dictyBase; DDB_G0292676; bub1.
DR eggNOG; KOG1166; Eukaryota.
DR HOGENOM; CLU_261109_0_0_1; -.
DR InParanoid; Q54CV5; -.
DR OMA; RSWSYET; -.
DR Reactome; R-DDI-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-DDI-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DDI-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-DDI-179409; APC-Cdc20 mediated degradation of Nek2A.
DR PRO; PR:Q54CV5; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:dictyBase.
DR InterPro; IPR015661; Bub1/Mad3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR PANTHER; PTHR14030; PTHR14030; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 1.
DR SMART; SM00777; Mad3_BUB1_I; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51489; BUB1_N; 1.
PE 3: Inferred from homology;
KW Coiled coil; Reference proteome.
FT CHAIN 1..1306
FT /note="Probable inactive serine/threonine-protein kinase
FT bub1"
FT /id="PRO_0000362008"
FT DOMAIN 47..211
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
FT DOMAIN 953..1298
FT /note="Protein kinase"
FT REGION 229..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..218
FT /evidence="ECO:0000255"
FT COILED 467..544
FT /evidence="ECO:0000255"
FT COILED 843..881
FT /evidence="ECO:0000255"
FT COMPBIAS 229..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1306 AA; 149359 MW; 9F1265931DF0E7EC CRC64;
MSSLSDWENT KENIVPLKTG RDPTKLALFA KQTNQSDEEL EKEKQKFEII INEYQGEDPI
DNWLKYIKWV QQSYPGGNMK EQLIVLLERC TRLFLSTEKY KNDPRYLRIW ITYADMCRDP
IEVFSFLEVQ RIGFYLSLLY EARAIVYENK GNYEQADKSF KQGIERKAQP IERLQQKHLD
FERRLIARLK HQQQHQQLQQ QQQQQNDQLE QQQLDENGNT KLTRSALGTI SSSSVHSERK
SQQTKGLPLG NSTIDKKRKV GNDQKNNLGF QIFDDEKGGS TTNEVLTDSK FFGSSRKAAA
LMAAGQTQQT SQMKWDELEP ELNKHKENTQ LSQKWSDVKL LQKKQKITTA GFQIYCDQDS
LSNNNNGSNN NNNNNNNENI PLSPDKLRVH SSKQQSKLEQ IQNNPLANFP KVSTSNSSSS
SSSSTNKSTS TTTVTTTKNE RVGYNKPLFT KENEKHEISF EEYRASLFKK KLIEKQEQQN
KKIEKEKEEL DIKLKQEQKE QKEKEQKEKE QKEKEELEIK LKQEQQEKEL QYQQHQQKQY
QQKQQQQQSY NPPSPTMTIH TKQAFHDVMA MFSEPLEFEK NNKSTSSSSS LQLNNVPSSP
NPFTESTLMK STIDNNKNDN NNNNNNNNNN NNNKNTDVSF DEKSIEDQEN IDPNQGGGGG
NNDGNPLLSS KITNRDVLMK QLFSKDEDEG NQFDQERDMV KTIERIDLLV KGKDTPKFEI
FEDSTLASSQ LHSKSVSLAD KVASKNKQLN PLEQSQNPLK KSILGSSGIN GINGNNGGFT
IFQDQPNQEK KQPLQQSQLQ NPLKNSILGI SDANGNGGGG GSGSGSGGFT IFQDQAAEEK
KPFNEKEQQQ QEEKEKENKI EEEEEEEEKD KEKEINYQNI TGNITSTIDP TTVIICSLTP
DDGIVNPYLI DHQYLLEQHV SATVQSIQSF FNVGDDLAPL PEQLDQCEPN QLFEDNSIIV
QWPFSDITVN FTKCVCKSTM DGSMTFKVER IDDLAMTTSE DSWLSCKVQD PPSIWEFYIG
NQIHQRLQER SLTISNSKFP TIHSLYYYTD KSIMLMDHTI DQGTLDDVVS STNGVPMEEP
LAMFHCIELL KMIEDLHLVG IIHGNICANN LHFLFGQTSD WPDWTAGECK GAWKSKGFTL
TDFSRSIDTT IYSQDARYQS PIELLPIGTP LEWLKINQSS TTNVGWSYNL DYLGICKVMF
HILTCGKEEL KLSLSQQTGK LEIINQSIIQ KDSFSELDTL WLPFLTTLLN HNGENGNQQT
TTTTYILKQQ RNLFENYLQS NPVKSKIKSL LRIQNIKLFE SMKSKQ
