ID A0A7J8E0I7_MOLMO Unreviewed; 1080 AA.
AC A0A7J8E0I7;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=Mitotic checkpoint serine/threonine-protein kinase BUB1 {ECO:0000256|ARBA:ARBA00074401};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=BUB1A {ECO:0000256|ARBA:ARBA00079871};
GN ORFNames=HJG59_001634 {ECO:0000313|EMBL:KAF6428998.1};
OS Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC Molossus.
OX NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6428998.1, ECO:0000313|Proteomes:UP000550707};
RN [1] {ECO:0000313|EMBL:KAF6428998.1, ECO:0000313|Proteomes:UP000550707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6428998.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6428998.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SUBUNIT: Interacts with BUB3 and KNL1. Interacts (when phosphorylated)
CC with PLK1. The BUB1-BUB3 complex interacts with MAD1L1.
CC {ECO:0000256|ARBA:ARBA00062095}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6428998.1}.
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DR EMBL; JACASF010000015; KAF6428998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8E0I7; -.
DR FunCoup; A0A7J8E0I7; 831.
DR InParanoid; A0A7J8E0I7; -.
DR OrthoDB; 248495at2759; -.
DR Proteomes; UP000550707; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:TreeGrafter.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR CDD; cd14028; STKc_Bub1_vert; 1.
DR FunFam; 1.10.510.10:FF:000390; Mitotic checkpoint serine/threonine-protein kinase BUB1; 1.
DR FunFam; 1.25.40.430:FF:000001; Mitotic checkpoint serine/threonine-protein kinase BUB1; 1.
DR Gene3D; 1.25.40.430; -; 1.
DR Gene3D; 6.10.130.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR015661; Bub1/Mad3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR PANTHER; PTHR14030:SF26; MITOTIC CHECKPOINT SERINE_THREONINE-PROTEIN KINASE BUB1; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00777; Mad3_BUB1_I; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51489; BUB1_N; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KAF6428998.1};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000550707};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 11..166
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 781..1080
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 532..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1080 AA; 122318 MW; 0DFAE745210CA720 CRC64;
MEDPENVWQM FEAHMQSYIG NDPLNEWESY MQWIEENFPQ NKEYLTILLE RLMKEFLDKK
RYHNDPRFIN YCLKFAECNS DRHQFFEFLY NHEIGKRSSP LYVAWAGHLE GQGELQHASA
VFRRGIQNQA EPRELLQQQY RLFQTRVTKA HLPAQARTSE PLHNAQILNQ LVTSKSNPIC
VSKNQGSEVS KVTSSACDKE SNMEQRVIMI SKSECSAHPS ETARADVQQV VMYCKEKLIC
GESEFSFEEL RAQKYNQRRK HEQWVNEDRH YMKRKEANAF EEQLLKEKMD ELHKKLHQVK
TSQEHLPALQ ESHEVNPACV GPSVGSQQEL STLSLPAVTQ LTSEYVGEKP RWAPPPDPPE
ASAVAVTLVS PAISQCVAPP VPLTAQPVTD SMFSVARKDA RYVTRTTQEF KPQSQAEMKE
GCETHKVVNP SSFHTTPNTS LGMVQATPSK VQPSPTVHTK EALGFIMNMF QAPTLPDVSD
DKDEWPSLDQ NEDAFEAQFQ KNTRSSGAWG VNKMISSLST AFSVFEDGNK ENYGLPQPKN
KPTGARTFGE RSMSRFSPKP KEVPHADELW DDSTVWGVRC TKTLAPSPKS PGDFTSAAQL
ASTPFHKPLV DSVHALEDKE NVVAAPCTHA TLDLCEEIVV KPSEDRKFSP IQEESPEPAF
PIDASSAPSL HPNQPATGGM LTVEAERSLK ACTLTDTDLA VVGEPSDAGA GLQAEWIQPC
SLGNVDTPNV TVENPWDDQL IFKLLSRLSQ PVRSSPNAFE WHCKLPAIKP KTEFQLGSLL
VYIDHLLGEG AFAQVYEVTH GDVKDTKSKQ KFVLKVQKPA NPWEFYIGTQ LMDRLRPDAR
HMFIKFYSAH FFQDGSVLVG DLYSYGTLLN AVNLYKNTPE KVMPQALVLS FAIRMLYMVE
QIHSCEIIHG DIKPDNFILG SRFLEQDGED DDLSAGLALI DLGQSIDMKL FPKGTAFTAR
CETSGFQCTE MLSNRPWNYQ IDYFGVAATV YCMLFGSYMK VKNEGGVWKP EGLFRRLPHL
DMWNEFFHIM LNIPDCHHLP SLDLLRQKLK KIFQQHYSNK IKTLRNRLIV LLLEHKRSRK
//
