ID A0A1L9V1D1_ASPBC Unreviewed; 1218 AA.
AC A0A1L9V1D1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPBRDRAFT_25251 {ECO:0000313|EMBL:OJJ77599.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ77599.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR EMBL; KV878679; OJJ77599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9V1D1; -.
DR STRING; 767769.A0A1L9V1D1; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_25251; -.
DR OMA; NCEKGVG; -.
DR OrthoDB; 5479089at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 6.10.20.170; -; 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; IPR012572; Mad3/Bub1_II.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PF08171; Mad3_BUB1_II; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000184499}.
FT DOMAIN 64..225
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 831..1218
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 234..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 137604 MW; EC9C99F5527B0F6B CRC64;
MAANEDHVNF DIIEGQKENI QSLPGGRSAR ELARIFSPRE STDILATPSP NDTRTVNDAT
RQEYETELQA IGESDDPLDI YDRYVKWTLN AYPTAQATQE SGLLPLLERA VKSFLNSPHY
RNDPRYLRLW LHYIRLFSDS PRETFAFLAR HRIGEGLALY YEEFAAWLES AGRWTQADEV
YRLGIDKEAR PAERLVRKYS EFQHRYENHT QDNGPSSPAL PAVRPALAAK VDPFASAASP
ADADPQAQQP APARSAAPKT KSGKPKMAIF SDADSPSQPA VSAPAQGWDS IGSMHERRKE
NKVEAKPWAG ETLKAGKKPA PAQKMTIFRD ESNSNLQAKE ALQSKHVPEH RVREAINPRT
GRRERVFVNL EAVYPDYKNP NHEVSFEELR AISRGWTDKN WRAHKEPLKQ ISGNAASVEI
PSENPLEHGL ENDLPQQFKQ KLTVKDAETH EPERGNPIQE SKTNKARKLK LREVKGETQT
IKMKFDSPTG GKIRRKSTAE PTMTIHTRAA TDEIYSIFNQ PLKAETENAA ESSDFDDDDY
TSAGESTVTG RMSAASSDFG DDDTTFHKSF VEGDEDGFED NTRAESVADG EWTQFSACDV
PDLGAAHSPA MPDDSTYHGR EDNTEQFHDA DENGERQRFV PQMPEDYNPP YGPYRDPAVM
AQNRLPFMTP IVEQTEHSLS MTAARNSLYN AKTPSKPPMG NLLLSSPLLP ATPHHDDNFP
DIPEDVALSP TMEKFRTSFK LSPLKEITRT GAVINDEQCN PTARGIRNTI LRSLQPPLAS
YPGYHGHPDM DTHYGPEIQR YLKTSPKRSR SGDEASFDVP ILELPGAERS YIIRRELGAG
AYAPVYFAES IDSLPSDDET DSNSRDSHNP SPIRYDTPRY GFEAIKLEVG PPNEWEFYMI
RTANERLSRL PEYSRATESI IRAHELHVYK GESILVEDYR GQGTLLDLVN LIRNEPISPN
TNGEGGIDEA LAMFFTVELF RTVEALHSCG ILHGDIKADN CLIRLDDKPV PPPSLIDLGD
EITADPREIH YSPRGLHGWR NKGLSLIDFG RGIDMQAFQP SVQFVADWET GKHECNEIRE
KRPWTHQIDL YGLAGTIHVM LFGKYLESIP SGNSPETKTY RIRESLKRYW ERDIWNDVFD
LLLNPGEERW ARMEREGHNP AAMTSENKPI LPVTNSMRHL RERMETWLFA NAEKKGLGLQ
IRKLEAIYAE RRKRLEKC
//
