ID G2X033_VERDV Unreviewed; 1213 AA.
AC G2X033;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Checkpoint serine/threonine-protein kinase BUB1 {ECO:0000313|EMBL:EGY21616.1};
GN ORFNames=VDAG_03056 {ECO:0000313|EMBL:EGY21616.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21616.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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DR EMBL; DS572699; EGY21616.1; -; Genomic_DNA.
DR RefSeq; XP_009655216.1; XM_009656921.1.
DR AlphaFoldDB; G2X033; -.
DR STRING; 498257.G2X033; -.
DR EnsemblFungi; EGY21616; EGY21616; VDAG_03056.
DR GeneID; 20704519; -.
DR KEGG; vda:VDAG_03056; -.
DR eggNOG; KOG1166; Eukaryota.
DR HOGENOM; CLU_002115_1_0_1; -.
DR InParanoid; G2X033; -.
DR OMA; NCEKGVG; -.
DR OrthoDB; 5479089at2759; -.
DR Proteomes; UP000001611; Chromosome 6.
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 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; 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:EGY21616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001611};
KW Transferase {ECO:0000313|EMBL:EGY21616.1}.
FT DOMAIN 63..224
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 865..1213
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..548
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 135041 MW; E40AB8709754C90B CRC64;
MAASGDLINF DIIEAQKENI QALPSGRSAK KLAEAFSPSP LHKLSTPTPT GSKNVTDCIR
AEYEAEIANI SESDDPLDVY DRFVRWTFDA YPSAQATPQS QLHTLLERAT KAFITSAQYK
NDPRYLKLWI LFIQFFADAP RETFLFISRH NIGESLALFY EEYAAWLESA GRWAQAEEVY
KLGIERGARP EQRLMRKFNE FEQRRAAQGP EATAAPSSPA LPAMRPALAA KVDPYAAAAA
AAAAAENPQA PRPGQGVGGP TAKPGKAKMA IFSDASAEPS ALSARPASSE GWDTIDSLAN
RKKENVTQAK PWVGETMKAG GKKSSAPKMQ IFKDTSKPKV AETHTLVPST EQVVVNPVSG
KRERVFVDLE AVYPAPELPG SELSFEEVWA MNRGWLDHSW EEHVMMDPLP EDEVENLGHM
VKEKLTVYTE TVTLDENGNI QKKGKSKKTR TMEFNETQIS RCDPWNKPLQ ATNTRASVKA
NLDSPSKPTK LKKRNATAEP TMTLHTKAAT DDIYEIFNQP LKPTQPLEDE EEEEDESDED
DYETDGDGDY TSGAESTMTT TRQVDTSEAG EDDDDEPSDV KSVSEWSDFS TRRHVPGINE
GNEVDESNDT QVSNLIDINE DENSLPSSRD PTGSREEDEQ EPSDLYEEDD DVDDDLQTPI
DEDYPPRTQT VFVPIPPEDY EPRTRPYRDP VEAANNRLPF MTPITERTES SLGVLTARRP
QMSPTKKDDN DESDDDDGAR ADQLFSSPLR EIYNDAQPAR VPQPILEKPK PKPLGVKTIP
PKGPVITDPQ CNPVDDVVRN EILAKMHPPL SSYAGFFDHQ AEKHGKGSEI RKVAKLMAKA
RSSGERTSNA FSVVEVEFPD TPTTYTIRKE LGAGAFAPVY LVENSTADQE DEDQENNGVA
VMGRGAFAVR QRSTLEALKM EQPPSAWEFH MIRLAHSRVG PQHRAAASLT YAHEMHLYQD
EGFLLLPLHP HGSLLDVVNL FRAEPSAVMD EQLGMFFTIE LMRTIEALHA RGVLHGDLKP
DNCLLRLDNG DAANAAPLAT QYRADGTGGW AARGVVLIDF GRGIDMRNFG PDTQFVADWK
TGAHDCAEMR EGRPWTWQID YHGLAGVIYC LLFGRYIETV RCDQGGIGAG GRRYRIKESL
KRYWQTEIWG ECFDLLLNPG SFVDVEEGQK MPILRGLKQV RERMEAWLEE NCERGVGLKS
LVGKVEAHAR ARR
//
