ID A0A2H3HSE3_FUSOX Unreviewed; 1229 AA.
AC A0A2H3HSE3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=BUB protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU210_000584 {ECO:0000313|EMBL:PCD45141.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD45141.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD45141.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD45141.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD45141.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD45141.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD45141.1}.
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DR EMBL; MABQ02000001; PCD45141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HSE3; -.
DR STRING; 327505.A0A2H3HSE3; -.
DR OrthoDB; 5479089at2759; -.
DR Proteomes; UP000219602; Chromosome 1.
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; 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:UP000219602}.
FT DOMAIN 63..226
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 882..1229
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 237..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..564
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 136375 MW; 6148A90C9CC3AF96 CRC64;
MSASGDLIDF DLIEGQKENI QSLPGGRSAK KLAELYSPSP LHKLSTPTPS DTRNVNDCIR
AEFEQEVENI AESDDPLDVF ERYVRWTLDA YPSAQATPQS QLHTLLERAT KTFIGSGQYK
NDPRYLKLWV HYIHFFSDTP RETYMFLSRH GIGESLALFY EEYAAWLEGA NRWAQAEEVY
KLGIDREARP VQRLIRKFKE FEQRVAQQPD VMNEPSSPAL PTMRPALAAK VDPFAAARAA
DPQAPRPSSG GAGKPSKSKL AIFSDADAQP SAMSSMSAGS KGWDSIGSLA DRRKENAVEA
KPWAGETLPA GGKKSTAPKM SVFRDPSLSQ IQNIVVVPSK HQISVHPQTG KKERVFVDLA
AIYPTPEEIG TELSFEEIMA ADRGWLDHCW EDETFDENLV PEPVMPLEIE EISKGAGERL
MIHQDPVDRL PIHQDPVGKL AIHKDTVEKL VIHQDSSTTL AVHKDTVQYD ENGKAVEQHR
GPRGGKKKKM IEVNETQIIK AKLDSPSRPK LKKKNTSEPT MTLHTKAATD DIYDIFNAPL
KPAGQEEEDE ESADDDDYES DDNYTTDAES TGTTRHIEPS EAGDDENDET SDVKSVSEWS
DFSTRRHIPH IDGEDDGDEG TERNETQVSD SIDTGAPGPG QESSEAFDST DQQMGTGEEQ
NDDAEELETP VSEDFPPTAR TTFVPIPPED YEPPTRPFRD PAEVANNRLP FMTPITERTE
VSLDVTMERR GYKTPSKKDN SPTIDEEDEG SSDSEPLSSP LREMANDPIP PPKMSAPLAP
KSIGPLGKAI PPKPLAPKGP IIKDAQCNPV DESVRSEIIS RMLPPLSSYS GFYDHRHEKY
ERGAEIRKFA KALAKANKSG DNKTGPVAAP VLIELPGTPS TYTIKKELGA GAFAPVYLVE
NSAPEADEND ENAIPTMGKG AFAVSHRSEI EALKMENPPT PWEFHMMRLA HTRLGPQHRT
SASLSYAHEM HLFQDEAFLF LPYHPHGTLL DVVNFFRAEP SAVMDEQLAM FFTIELLRTV
EALHSKSILH GDLKADNCLL RLDALSDDES LTAQWKADGS GGWSSRGVVL IDFGRGIDMR
AFVPEVEFIA DWKTSAQDCA EMREGRPWTW QIDYHGLAGT IHTLLFGKYI ETVRCDQGGL
GKSGRRYKIR ESLKRYWQTD LWSDCFELLL NPGAAAAAGG EDGGKMPVLK SMKNVRERME
TWLGANCERG VGLKSVMGRL EATFGKNRK
//
