ID A0A2T4CH09_TRILO Unreviewed; 1148 AA.
AC A0A2T4CH09;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Kinase-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M440DRAFT_1322717 {ECO:0000313|EMBL:PTB80849.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB80849.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB80849.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB80849.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ679126; PTB80849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4CH09; -.
DR STRING; 983965.A0A2T4CH09; -.
DR Proteomes; UP000240760; 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:UP000240760}.
FT DOMAIN 62..228
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 804..1148
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 228..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..538
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 128658 MW; D01DAED0BB0FB3E1 CRC64;
MAGSGDITDF EVIENQKENI QALPGGRSAR KLAGLFSSPL HNLSTPTPTD TRNINEAIRA
EFEAEIDNIS ESDDPLDVFD RYVRWAIDAY PSAQATAESQ LHTILERATK AFISSSQYKN
DPRYLKLWMY YIQLFSDTPR ETFLFLSRHG IGESLALYYE EYAAWLEGAD RWAQAEEVYK
LGIEREARPV QRLLRKFKEF GERLAQHPDA LAEPSSPALP TVRPALASKT DPFASSSHPV
DPQAPRQTSG VGGSSSRPAK PKMAIFSDAD AQQPAMSSRD AASKGWDSIG SLSDRKKENT
MEPKPWVGET LKAGGRKPGA GGTKLAVFRD PSLAQIQTIV VVPSKHQVTV HPQTGKREYI
FVDLAAVYPT PEEPGTELSF EEIIAAHRGW LDRLWDTDME SENGTANRMV PLRDMEHLSD
QMVIEQDCDP MDLDENGVAQ EKPREPRGGR RKKMMEVNET QIIKAKLDSP SGPKFRKKKA
AEPTMTIHTK AATDDIYEIF NAPLKPAPVE GEETGDDYDD DDDEDEDDDD DDDGDEDEIV
TDADFASDAE STGTTRQIQQ GEQERRTWLK ILTTLDIDVT SHSLARDVDE VFSEDEEMEP
PRTRTIFIPL PPEDYEPPTR PYRDAATMAN NRLPFMTPIT ERTEYSMDVD MDRAYQFKTP
SKRDGRATPI EEASDSEPSG SPLRDFFPEE SPFAKGREPL GSKAAKALSK TGPNRGVPVK
GPIVKEAQCS PIDDDIRRTI LTNIQPPLAA YPGFHDHRNQ RYERGGEIRR FAKAVSRLGK
GNQDRPGLGL APVVIRFADC HSRYTVKREL GAGAFAPVYL VENSHPDQED GRVMMGKGAF
AVSQRAAVEA LKMESPPTPW EFYIMRTAHA RLGPRHRATA SISVAHEMHL YHDEAFLFLP
YHPHGTLLDV INLFRAEPSG VMDEQLAMFF TIEIFRTVEA LHSKGVLHGD LKPDNCLLRL
DAKSAFSSSD HGLSSKWHAD GSGGWDSRGV VLIDFGRGID MKAFGKDVEF VADWKTTAQD
CPEMREGRPW TWQIDYYGLA GVVHCLLFGK YLETVRADQG GLGRGGRKYR IRESLKRYWQ
TDIWADCFEV LLNPASFAAH EEGGRMPVLR SMRSIRERME AWLEDHCERG AGLKAMMGRV
EAFVKSRR
//