ID A0A182PJM0_9DIPT Unreviewed; 1620 AA.
AC A0A182PJM0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=BUB1 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI007134-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI007134-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI007134-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR STRING; 199890.A0A182PJM0; -.
DR EnsemblMetazoa; AEPI007134-RA; AEPI007134-PA; AEPI007134.
DR VEuPathDB; VectorBase:AEPI007134; -.
DR OrthoDB; 5479089at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR CDD; cd13981; STKc_Bub1_BubR1; 1.
DR Gene3D; 1.25.40.430; -; 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:SF4; BUB1 KINASE, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR14030; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 39..205
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 1336..1620
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 576..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1620 AA; 181277 MW; 1623FB9F54871AC7 CRC64;
MDLEDKKENI QPLRGGRNAN LLEYAFVSAE QWEEERKEHE KEIDRYDGDD PLAPWYEYFF
WMEQTNVSNF KPSIQEQALR RCVQLYENDP RYLQDHRFIK LCIKYIDAQP SPVELYNELY
MRGVGTLCAE LYIAWAYYYD AVDNFSKTEE VFQKGLRAGA EPKADLEQAH KQFGFSMSQR
LLHKDEGSML KFQTSLNERR NALTSLRASR KKHVGSIRTG LAVKSYHPGI VNQENVPKNS
GMSSNAPAST IVFTDDATSA EPCSSIVRPF SSVHSEPENI IEAARLAKTK SNSSHKKPLF
GTHQALSFDI PVDQEEFIPI PVLVDNGSKG VTLFAQFCRR NKPQTPFEVG ICVGDPKERA
VPMYDKIRLY CRAKEHPRDG SERTEYSPEE LRAYGYFMRR GIENALTREC AKVWGRGHEV
GIRLHPLHVP ESKSKERGDV GFQNPKLAEC DMNIQSKIAQ MYANPSEEKS IEELLVERWL
KGKINKCIDR RYQDDIDPVD MDETHVESKR ISMGPARFSM APSALSHDGN THPPIGQRKS
IFPTGMVAAS IQEETEEQLL NKSVVPAGKL TTQLEHSVHA TNVPSRKRLS NDVLEQEVSK
KEDSTPTPLK APIANDRVEK QQSVDRNCQE ESPQAIASPP EPAAVASKKI EIFVDDSDEN
DEREDERANF KVPNELQPQQ QPQQSYYPND TCSTQMFNLF VKNISTPVAP IRKTSPENAI
TATKRTVVFA DDDEEEERVT GTNGAVQKEP YPVAAPVPIP DVVINDENAV PLVDHLTPPS
VSSGCNSTQS HKQLSTIMER TETSTVSSVG VTKSSVDTQP TKKSVFTLPG DGKGFCIHVD
STETMANIPL KRIPVEAAVI QSDDKENELI TRAAGGGARP GIFQLSEEPT FSGYGFLPPA
AGAKNVSQMV QRELEANSIV SFRLGTERTN TVPIQLVKPQ YAIPEIVTLP APSSSTSGES
ITTSNASTIL SATASQSTVV AGEENKTEPK IKKKNNSLLD LLDTTFSPKP TGNSGRGGAI
EVAASKEEEK RKECSFNLSD LIKSPQPKRK PANELPQSCL RELEPLAPLP ASCNDLSLLP
IAQIKTEKSL NIDASTAPLP SFRATEAPLP EPMIAKTVAP VGRIVLDDFP SPARPTGSGG
RASLEDINTM AFSLNINNAV NSTIIQDGFK TPAKQRPSQK EQTKFRIVDV QGGVSKSNGF
LMPPPPPQVA KHDPLGRISP AHDYDGDNQD VSIYHPRPVI SQDAERWEEI DEQFDDMQSN
EYQHKPIDMD GTIQQINTHM LMDEIDPFER QLLDAFLDRV EFPAYIAEHP TCLLVNKVHP
LRKDALVEMK EQGVAFKVQQ KIGKGTYGTI FCATEQSTGR KVALKQERPA NLWEYYICLE
LRSRIENPDI LPGFMPIDYA IIGNNASIFI CPYSRYGNIL DVCNLINNAT NRNIDEFIAM
ILSAQILSII DHLHSCQIIH ADIKPDNFLL MGPIAMNTKV PCIQLIDFGV SIDMKLFPED
AKFKKVITTE GFTCIEMMEN RHWTYQPDLY GVAATSHVML FGKYMQVQKN VVNWSIKTAM
PRYFKKVVWE NYFTTLLNIR DCEHLPNLQK LRTAFLEEIT MHEKYIQSKV SEFNNVLATV
//
