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Database: UniProt
Entry: A0A0D2AF15_9PEZI
LinkDB: A0A0D2AF15_9PEZI
Original site: A0A0D2AF15_9PEZI 
ID   A0A0D2AF15_9PEZI        Unreviewed;      1230 AA.
AC   A0A0D2AF15;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV09_03422 {ECO:0000313|EMBL:KIW05543.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW05543.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW05543.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW05543.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847537; KIW05543.1; -; Genomic_DNA.
DR   RefSeq; XP_016215412.1; XM_016356619.1.
DR   AlphaFoldDB; A0A0D2AF15; -.
DR   STRING; 253628.A0A0D2AF15; -.
DR   GeneID; 27311395; -.
DR   VEuPathDB; FungiDB:PV09_03422; -.
DR   HOGENOM; CLU_002115_1_0_1; -.
DR   InParanoid; A0A0D2AF15; -.
DR   OrthoDB; 5479089at2759; -.
DR   Proteomes; UP000053259; 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; 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   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:UP000053259}.
FT   DOMAIN          61..227
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          887..1204
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          197..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..591
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  138060 MW;  E548687255EE22A1 CRC64;
     MADKGDLIDF SVIETCKENI QSIPGGRSAK QLSTVLSPLA AKKSPPLSEI QGSKETKRQE
     FEQELLTIAE ADDPLDVYDR YVKWTMDAYT SAQGTNESNL LPLLERATKA FLTSSLYKND
     PRYLKLWLLY IRLFSDSPRE TYAFLAKHNI GQGLALFYEE FAAWLENAGR WAQAEEVYLK
     GIDCEARPQE RLIRKFGEFQ HRRESKGSAQ DGPTSPAMPK VRPALAAKLD PFAAAAEEAD
     PQARDRAASS TSRTSKPGRS KMSIFADGDE PSKPGSSDSN SGWDSIGSLK ERRKENTREA
     KPWVGETLQG GRRAVSGPKM MVFRDQSLGA NKNTNNEHSQ SELQCSINPK TGRKEYVFAN
     LELVYPSGDA ESGYEFCFEE LRAMKRGLID PTGRVIKPKK QTATKTDIEQ RPVTPPNTAV
     SPKNTKVSSS RKLDIFQDTQ TSKIPVKIPV FDDSVAQDQP VSTTKVSKKI PVFDENGQPQ
     VETDAAARAV KKKMRKEERA NRTRKIEIME VKAEPQTIQT NLNSPAGPKI KRKKSGEATM
     TLHTKEAMNE VYDLFNQTLT KVSEEPVEDN QSQVDSSDDD DDDEDDDDYT SAGESTTTGR
     FSAVTSEAGD ETQADFTMAT QSNVSVGENT NNSDWSEFSE VKELPEQHGS NVGLEIDDEN
     DVGTQEEVLT PTSPQRLSED QYEEDPQDIP SLEAQDEPGM ARRGFSYRSR QLPFMTPIVE
     KTESSLGAMT VYAEKEYFNT KTPSRQNNVK NAQAKDCDVW SSPFQANTEE NKENIKVPQP
     EFVKPVKADQ QKAQPLAPKD LGKEKPKGPI IKELQCNPIE ESIRATILSQ VQPPLGTYAG
     FFDRRGQIAA QGVDIRKYTK AVKNKNDKTL SATTPPVLTL SGSSRRYQVR RELGKGAFAP
     VYLVDSQPLP ASLEQNESTA AARMGEGEFG LRRNEQEAVK MEEPPSAWEF YIIRQAKRRL
     GVSRPSESIV EAYEMHLYED ECFLIEEYRN QGTLLDLVNA YRAEGGVMDE QLVMFFTIEL
     LRTVEALHAK GLIHGDLKAD NILVRLDSSD TEWSSQYHRS GTNGWSDKGI KIIDFGRGID
     MKAFKPEVQF IADWKTSEAD CAEMREMRPW TYQVDYHGLA GIVHSMLFGK YLETVAERGG
     TLGAGATKTY RIRESLKRYW QTEIWSDVFS LLLNPLMHLD GEDGRRLPVL QGVKRLRERM
     EMYLETNCEK GSGLKAGLRR VENMIREKRK
//
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