ID A0A4Z0A523_9AGAM Unreviewed; 992 AA.
AC A0A4Z0A523;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 19.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=EWM64_g1903 {ECO:0000313|EMBL:TFY82112.1};
OS Hericium alpestre.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Hericium.
OX NCBI_TaxID=135208 {ECO:0000313|EMBL:TFY82112.1, ECO:0000313|Proteomes:UP000298061};
RN [1] {ECO:0000313|EMBL:TFY82112.1, ECO:0000313|Proteomes:UP000298061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108284 {ECO:0000313|EMBL:TFY82112.1,
RC ECO:0000313|Proteomes:UP000298061};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Hericium alpestre (H.
RT flagellum).";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}.
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:TFY82112.1}.
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DR EMBL; SFCI01000141; TFY82112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z0A523; -.
DR STRING; 135208.A0A4Z0A523; -.
DR OrthoDB; 248495at2759; -.
DR Proteomes; UP000298061; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:TreeGrafter.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00777; Mad3_BUB1_I; 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 Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Reference proteome {ECO:0000313|Proteomes:UP000298061}.
FT DOMAIN 26..187
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 835..992
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 164..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..608
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..732
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 992
FT /evidence="ECO:0000313|EMBL:TFY82112.1"
SQ SEQUENCE 992 AA; 109448 MW; 16418774EF8A21C4 CRC64;
MASSTASSSI VSPSALETLT RHTAKLRSQI KAEIDEVDDP LALYDQFVKW TCESYPQEYL
AHSGLLEVLE EATRKYKTDE SYKCDLRYLK MWTLYANLVD KPIVVFKHIM TKGIGIVYAQ
LYEEYALMLE REGRHSDADQ VYRAGIQRKA RPPERLRKRY ELFKQRTSSK PPVPPPAPTV
RLPRSKGTAE ADSLRRNPLK YHNDVKAPSS RRPHPSSQIP STSASASSST SPPPPSKPHD
PYAAMLAPPP PGKRPEKMQF NMSLLFTEDR AEYSMPEARA RSMGLLGKKW GPPPVSELSR
NAPIRVNFND DSKSARPFSA MARKSLLVGE PTVTINTKEA LADVFGMYNS PEKSMRFGPM
PGSKHAPVRK IEPVTPMNLV PPMRSNANEN ANMNAKTPTA FKPFVDENAG RKENATPGLA
KFKPFVDPEA PKTPAFTPES GRRALSAKDP ASMPGSKLRP KGDENTLGSV FTKPAIPAKP
ERESPVDVFV DEPQAPPSQQ EVPVFRSIPE ARNQETAAKP TTFVPFTDSQ APFKVFSRPP
DENVQSVPAK TGGFRPFVES ENPAPPRSAL NNRTPLRSFV PTRVHELRDD TVEEEEGEDE
DDDYDEDGEH VQVARVAFQE DDTDNGRTPR TAPLGGRFGQ FDVMTPITER TFEYTSTSTR
LSAMGQDGSS VFDKGFVQSD AVEAAERLAA ELRDEENTGS RLAVFTPREP IQTPEVVEEA
SFDSLGEAED EDPRSPSDVI EEKTGTLSLS DAIAVASAFA PPNPCNPFDP PIVSTLLSLL
PEDAGHHNLV HQESKMLDGL QKFARSRERR ASGNTSSRSL DSTGSFPVTL GDHRFAVYEK
LGEGGFGAVF AAKDVTSKVA ADDSDDSDDD DDEAGRVALK VVKPRNLWEF HVLRKLHGSL
PAKLRSSIIK PHALYTFRDE SFLILDLCTQ GTLLDIINRS AKAGISQQGA CLDELLVVFF
TIELLRLLEG MHAAGFIHGD LKIDNCLVRL ED
//
