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Database: UniProt
Entry: A0A316VY33_9BASI
LinkDB: A0A316VY33_9BASI
Original site: A0A316VY33_9BASI 
ID   A0A316VY33_9BASI        Unreviewed;      1448 AA.
AC   A0A316VY33;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IE81DRAFT_141055 {ECO:0000313|EMBL:PWN42234.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN42234.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN42234.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN42234.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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DR   EMBL; KZ819382; PWN42234.1; -; Genomic_DNA.
DR   STRING; 1522189.A0A316VY33; -.
DR   InParanoid; A0A316VY33; -.
DR   OrthoDB; 5479089at2759; -.
DR   Proteomes; UP000245783; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245783}.
FT   DOMAIN          89..252
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          1077..1418
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..692
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..823
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..934
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1448 AA;  156708 MW;  6DBB2A9EAF68C26C CRC64;
     MSARGGPSAA VATPMRGQGS HAGLRTPART PGGSEQTSAT PVIDFARLEA AKENITRSAQ
     GRSASALNTT LSLKPGARSR ALAERAEIFE KECKAASAPD SDHDDPIEPW SRYAMWAFDA
     YPSHGPHLVH MLERATREFK GRERYAQDPR YLKLWVLYAR ACEKPQHVYQ FLLAQEIGTN
     LATLYEELAI VYEGRGVYDQ ADATYKLGAA RFAEPVDRLK KRYREFQARL TGRSQLAATA
     AAAGKPEPTF REVLAAAMAS ANRATLGERA PDSRGAGASS RSGNVARAFG SNTAVPLKAI
     AAPNNARQMD VFKDDDEGRG PDSKAPWDTL PTNAERNQES GLGGSKLWHG EKLLQKPPTR
     PLASATPSKG APLAVFRDSD DEDDEPKPKG GKAVSPAADP EAQVWDAANK LREDPLAHYD
     KTTKRALSVE EVQEARRKAN QNQANKERRA ARNKATHSHS VAGASASSSK PNAQPKATAA
     SKGGEQYALP LTVLYQGIDP KAPPDSGVDL SERSVPEVLA AQKGVQSSSG DPDPWSYLDS
     RIGLWLPTRQ SESHVSKKAR SSTGSTLTKS STSESLSRNK SASSAPAQKQ PAEQQSKLKP
     PRDQQHGQGT ELLALKEKPP RDAFDPDDSA ANAAALGFSA PRRRMGNVRA DQPTVTMATA
     SALKEVNAFF NEAEEEDTDS DSESESDEDE DDLPPMSARR PPAMMAPSSR VVDETPTPAT
     RSLCSGAAQA ANSLKSRPAL GAVSENLNKE TQPFEIAKSA VTVPSTPAKS ALGGTVGETK
     KSVAVAPQLN PQPASRAQRI DISTLAEEED EDDEEEDEEQ NDGMEPDAAH PLDEHEYHHL
     TRVTEVTELT RFTMFSRTPG RSNSGGTSDA VSSCSRSRPG AVLAQHGPSD PAARAHPVAI
     DRAIVDQQGL PRLDNADADR SWNSNPSTEG DDPRNLSGSF DWARQRRGAD VSPGHTIEQR
     AEDALERFGR PALADTLVIS DEEALEATRG VAIPVQSQQR IPNPCSPTDV EVVAELLAAL
     VLPIESSPDF VDLSSRSAEG RLAALRKRAK LQNRKSISSG PNTPGKEWKL DIDGNPFLVR
     GLLGEGGFGS VFLAEDVEEC APAPRKAIGG IAGDSSFEGS AAARMGEEDE EEDEEEAERR
     RLVAVKVESP ANRLEFYILG QLRARLERKS LNSIVSARKC FVYQDESFLL LEYAERGTLL
     DMVNNAQAAG VAGSNVGGGG AGSGVDETLA MFFTIELLRL VEALHTARFV HGDVKIDNCL
     LRLDEPPRGV TWANTYSSAG QDGWSAKGIT LIDFGRAIDL HLYPQGQTFL ADWDTDDKDC
     PQMREGRPWT FEADYYGVAS VSHCLLFGKY IETAKAQDDS DAGHGRYKIT QTLRRYWQTD
     IWQEFFDAML NVRLDDPSDP SAALEKLRIL RGRMESWLES NACRGGRNLR GALKKVALYA
     LKKSLARA
//
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