GenomeNet

Database: UniProt
Entry: W9ZDJ2_9EURO
LinkDB: W9ZDJ2_9EURO
Original site: W9ZDJ2_9EURO 
ID   W9ZDJ2_9EURO            Unreviewed;      1414 AA.
AC   W9ZDJ2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=BUB protein kinase {ECO:0000313|EMBL:EXJ92584.1};
GN   ORFNames=A1O3_01136 {ECO:0000313|EMBL:EXJ92584.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ92584.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ92584.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ92584.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., 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 Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ92584.1}.
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DR   EMBL; AMGY01000001; EXJ92584.1; -; Genomic_DNA.
DR   RefSeq; XP_007729474.1; XM_007731284.1.
DR   STRING; 1182542.W9ZDJ2; -.
DR   GeneID; 19165274; -.
DR   eggNOG; KOG1166; Eukaryota.
DR   HOGENOM; CLU_002115_1_0_1; -.
DR   OrthoDB; 5479089at2759; -.
DR   Proteomes; UP000019478; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   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   Kinase {ECO:0000313|EMBL:EXJ92584.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW   Transferase {ECO:0000313|EMBL:EXJ92584.1}.
FT   DOMAIN          74..233
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          1058..1414
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          244..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..773
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..873
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..921
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1414 AA;  156046 MW;  172E1ADC74F8E231 CRC64;
     MAVPAADNDL INFDIIETHK ENIQSLPGGR SAKQLASILA PLPTSKAAGV DADADALPTL
     SETKTLNDAI RQEYEIELQS IADSDDPLDI YDRYVRWTLN AYPSAQATPQ SQLLPLLERA
     TKAFLTSPHY KNDPRYLKLW LHYIRLFSDS PRETFTFLSR HGIGEGLGLF YEEFAAWLES
     AGRWIQADEV YKLGIEREAR PTERLVRKYG QFQQRFEARP QSDNEPSSPA LPTVRPALAA
     KIDPFASAPP NDDPQGARQQ SAGRGGSGAP SRTGKPKMAI FSDADSAAPA PTKASANITN
     GWDNIGSMRE RKKENTIEAR PWAGEKLKAG GRVGTVPKME IFKDPSQELL QPSRASRQRS
     EVVNPRTGRA ERAFVNFEAI YPREGNEEFS FEELRAMSRG WMQKDWRAGK PPARSSASPL
     KCTSGNIMAA ASPRPKSKPS RSEEAEDVEN LSHSFRQKLE LTSDIPNPSV HDLSTQSMVG
     MPESNLPPQP QNANKREKKL KVREVKQETV TVMTRLESPT GKKLKRKNSA TTEPTMTFHS
     KAATNDIYDM FNQPLRRPEM ARDDTQSGDD ADFTEGDVDE GYSTTGDGES TGTGRVSGPG
     SDFGDDTSSS LPPDATSTQS QADSVSPWSE FTTSKHVPRL ASVSGSSGKI KGSGSSSKGP
     GKSKLKHAHK RVLSDDMTEN MASSSQNPTQ TSGLGGFDTQ AIAAIAGGNF DDMDTKAIAM
     LAGDFDDDGD EADTIQNQDP GQDQDLDEQG AGAGVNELPE RDGSRHSEHE NNDNTSLNHN
     NNNVTTPVDD VFTEITHKPR FIPLPPEDYE PTPIRPYRDP ALVAHNKLPF MTPIVERTES
     SLAPSTVFND PDYFNSKTPS RSAKEEDESP SKLKMEALLM SSPQQPATPS SAAKRKLDEA
     DDREEEDTAV TPQRKKSLHH TNENSPVPSP AGAKNTKPLK VEDTVFKTPA VPTQSPARRI
     LQPAKIHKGP IVADLQCNPC DDAVRQQILA AVHPPLSSYT GYHDHSDHVY NHYQPLKSYA
     EKLGKSKVKA SPRKSQSEKT CSKAVPPILK FQGTARVYAV KRQLGEGAFA PVYLVDSYDP
     TETETAIGEE SDNKENVSPR GLRTKSSRQD LEALKTEAPP GTLVWEFHIL RLIRQRLGHA
     ARAVQSIVDA HECHLYRDEA YIVLSYSPQG TLLDLVNLAR SENVKAGKLA EGLDETLAMW
     FGVELLRTLE DLHRIGILHG DLKGDNCLVR FDSSVDLSGP FDPSGNHGWS AKGLKMIDFG
     RGIDVRMFQP SAQFIADWPS SAQDCAEIRE CRPWKWQIDY HGAAGVIHSL LFGKYIETVP
     LTAASGGLAL GPRQKKEWKL KENLKRYWEK ELWQEVFSVL LNPGSVSDQE AMPIEGNLKR
     VRMKMEKWLV DEGERGGRDL RASLRKMERL VAMK
//
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