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Database: UniProt
Entry: A0A164NXC2_9AGAM
LinkDB: A0A164NXC2_9AGAM
Original site: A0A164NXC2_9AGAM 
ID   A0A164NXC2_9AGAM        Unreviewed;      1164 AA.
AC   A0A164NXC2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Kinase-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SISNIDRAFT_418676 {ECO:0000313|EMBL:KZS88135.1};
OS   Sistotremastrum niveocremeum HHB9708.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS88135.1, ECO:0000313|Proteomes:UP000076722};
RN   [1] {ECO:0000313|EMBL:KZS88135.1, ECO:0000313|Proteomes:UP000076722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB9708 {ECO:0000313|EMBL:KZS88135.1,
RC   ECO:0000313|Proteomes:UP000076722};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV419440; KZS88135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164NXC2; -.
DR   STRING; 1314777.A0A164NXC2; -.
DR   OrthoDB; 5479089at2759; -.
DR   Proteomes; UP000076722; 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; 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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076722}.
FT   DOMAIN          60..224
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          836..1164
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          338..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1164 AA;  129316 MW;  7DFECE8113F2CE1B CRC64;
     MAAVASPQDT PPIVDGDVLL AAKENIQPLA AGRRVTSLAT VLSTPRKELT TQRDSIRAQF
     RQELSTAFEE DDPLDIYHRF IQWTVENYPQ GQSAESGLLE LLEEATRVFK DDEMYKADLR
     YLKIWIMFAG LVERAEVVYK WLVVNEVGTG YSLLYEEYAL LLEHLGRRPE ADEIYNLGIA
     RKARPLERLQ NRHKAFQTRM MTSTALPPPS RSSTTIITST SRRNVLGTVA SGAAASPLSL
     TAGSRPNGRI QPFVDTDGPH SADGNEWQEL GTRKSRVKEN TRETTKMGET ILKSKLGPTP
     LTPKIIPYRD EDDVMSVKKS TAEEEAIRRD PFRKWDAVDL KPKTNAMPPP QSTSKPALSE
     SAKSSTSSTV SSAGKTRFTF PATDAKGKKH PYAHLLSQTV STKPQKQMCD LSLLLSEDGT
     ESCIAEVRLR GMGILGKVWD EPQASSSTIP ADKSSKKIAP TVTINTKAAL SDVFDMYNSP
     EKTRLLKEAS IKEVSTPAPE KPTLGRKTSE RTPGPMQVFV DDAEAKAAFM PFVDEPEPSK
     SAATKASFVP FVDDDASDAR VSATPAPART PFGRARIQEA ETPMSDHPFE SEEIGEDEED
     EDEHHLRRIP MGGRFGQFNV MTPITERTNE FTTSTRAFST PSGTLSMSDK AFLQMDAVES
     AELLAAELRE EEAREKGLVV DVHAPLLGHS VLVKEGSPPS SSSAESIFTS HNRSSPPFKL
     SDGFTIPPVP VHPPPAPAAE LSKAIDKPEP LNLRESINVT SQFKPPNPCN PFDPEILGTL
     LSLLPNDRAH HDLKHQEAKL LQSLQKFTAK KVRRGSYTVG MGDSDCLEIK LGEQGYRVFE
     KIGEGGFGAV FMAQEVDPNE EDRDLEDDFE EKSFALKVVR PRNVWEFYIL RNILRSLPPP
     LRKSIIQPHG LYTFKDESFL ILELSEQGTL LEVVNGAAGA GVAQHGGSGL EEVLVIFFAV
     ELLRLVEGMH RLGLIHGDLK IDNCLVRLDE VEAPTIWESK YDPAGGNGWS AKGVKMIDFG
     RSVDMRMFPA SQRFVGDWPT DVRDCLEVRE ARPWSYQTDY WGLASIFYCM LYGKYIETVV
     SAGRVKLAQP LKRYWQGEMW TRTFDLLLNS GSAREDGKLP LCEEIGGLRV EMEDWLVQNC
     TLPTRDLKAL LKKVERGILN RVRR
//
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