ID A0A2V1DE94_9PLEO Unreviewed; 1241 AA.
AC A0A2V1DE94;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Checkpoint protein kinase-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DM02DRAFT_674861 {ECO:0000313|EMBL:PVH96378.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVH96378.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVH96378.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVH96378.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ805466; PVH96378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1DE94; -.
DR STRING; 97972.A0A2V1DE94; -.
DR Proteomes; UP000244855; 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; 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:UP000244855}.
FT DOMAIN 63..222
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 902..1238
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 139479 MW; 8DB8C2FDF870700C CRC64;
MGSDDLIDFE IIENQKENIQ ALPSGRSAKA LAQLYTPPLS CKPGQTPSPS QLQDAHNETR
QKFEKELLAI DDSDDPLDIY DRYVKWTLEA YPSAQNTPQS QLCPLLERAT KAFQSSTHYK
DDPRYLKLWL HYIRFFSDAP REAFAYLARH NIGDRLALFY EEFAAWLETA GRWTQAEEVY
SMGIDKEARP VERLVRKYGE FQHRFESRAQ NVPEPTSPAL PTVRPALAAK VDPFSHAAAG
PADPQAQSRA RAGGATAQKS SKPKLAIFSD ADEAPKPGSS GSTQGWDSIG SLGERKKENT
TEARSWVGET LKVGKKNTGV QKMMIFKDEN ESNLDTEPTK SHPLREHQQA LNPRTGRLEV
VFVDLQKVYP NYEDHLSVEY SFEELRAKHR GWLDKDWAAI RREEEKQSRK LIDIPATKPA
KPKTSPLAPK EQHKESLRPQ TIPLKGSIDD ENHVNDENTP PSQLETERAK TAKKQRKDDR
ANRTRKIKVM DVKEIRGETQ TIQTNLDSPT GRKIRRKKGS KEKTVTIHTK EAMDEIYDIF
SQPLQEAKDL VAEVESEDES SEESSDNDDD EDDYTSAGES TGTGRLSCAN SEFGDETTAA
DFTLGTTIGD NDGSGSEADE TDAKSVSAEW SEFTEIKQDP EEHERQPSDA EDESDGDSFS
EIHHEQHEDH SQGIVTPTSP AASSNSLPTR FVPIPPEDYE IPTRPYRDPA VAANNRLPFM
TPIVEKTESS LGIATVQAQK ENISAKTPSR SKGGPVILED DNELWSSPFQ EVMSKPLEGT
GKLPKLALRE AKTASEPKPA VAEKKDDSLK ESLKPKGPII KDMQCNPVDE DVRQTILREI
QPPLSSYDGY FADTERNYGK GAEIRKYTKA VNKANNRNGN EKTTTSLSIP PTLVFKGSDR
MYTVKKELGK GAFAPVYLAE SAETEEQDEN APAVMGKGEF GLQRRSLEAI KMEEPPSPWE
FYMMRQAKRR LGVSRPVESI VHAYEMHMFK DECYLIEEFR DQGTLLDLVN ISRAENGGMD
ENLAMFFTVE LFRTVEALHA KGLIHGDLKS DNVLVRFDAL PKDGVWDTQY RSDGTAGWAS
KGVALIDFGR GIDMKAFIPN VQFIADWPTT EADCAEMREL RPWTYQIDYH GLAGILHNLL
FGKYIATQAE RAANLGAGAT KTYRLKETLK RYWQTDIWQE AFHLLLNPLM HLNGEEGTKM
PVLKGMKEVR EKMETHLESN CEKGVGLKAL IRRMEDAVKK R
//
