ID A0A0C3LIR1_9AGAM Unreviewed; 925 AA.
AC A0A0C3LIR1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=M407DRAFT_17464 {ECO:0000313|EMBL:KIO33863.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO33863.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO33863.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO33863.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN822946; KIO33863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3LIR1; -.
DR STRING; 1051891.A0A0C3LIR1; -.
DR HOGENOM; CLU_000288_7_37_1; -.
DR Proteomes; UP000054248; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10098; RAPSYN-RELATED; 1.
DR PANTHER; PTHR10098:SF106; TETRATRICOPEPTIDE REPEAT PROTEIN 28; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13424; TPR_12; 4.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054248};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 42..352
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 530..563
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 650..683
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 102574 MW; 86432C0535CA248E CRC64;
MTDERRDPSD ARRPGATSPG PSLRNILRGL HHRRVHPDNI LTAKCGPHGW GGKSEVYKAT
LVREPDKYNS WQQSKIQVAV KKLRFDDEVD QDRTSKAFVR ELRVLDGLNH PNVAKLVGFV
EDLERGIAWL VSSWEPNGNV RQFLMSAKCA IPGRISLIRD TLEGLLYLHT REPPICHGDL
KSLNILVTAS YNAVITDFGS ARVIKRQSGN DIHPSLLSLQ TTNDHTSAAN NVPKLAPIIP
ESDLTLTNAE FSFRWAAPEV LLGDRPNLPS DIWAAAWTCW EILTDQLPFS NTNSEGVITM
HIIEGKVPSS IQGEQIQMSQ IQGLFRLMTD CWASNPRDRP SAEECLAEVR RLPSSIPSSP
TRLGSKIRFT SLSCPPAQMR YSTSEFKRMK SIHRNALEVA RSTENGVAAA DTLFALGRAY
QARGKYQLAE EAYIHAQVYY ASGGNPRGRA RAFEELGSVY RAQCLYGDAE GSYLRAKTIY
TCLKDDLGRA STLCGLGDIY RARCRYKQAE EFYQEARGIH ARSGEDRGRA NALLGLGEVY
SAQSRYRKAE ETFLQARDMC SDLGDDLGRA NALSGLGDVY RAQLKYDEAE DAYGAAYTFH
TKAKDIPGIA NALLGRGEVY LARTKYNEAE VMFTQAQAIY EYVGNDIDKV NALLGLGDVY
RAQRKYDEAE KLFNQALNLS ARTDNDLARA NALRGLGDIH LAQTNYDQAE DSFSLARDLY
DRIGNDGGSA DALLGLGHAY RAQTKWDMAE ESFAHAQYIY AHIRNDIGRA NALSGIGDVY
HALREYGDAE RSYRQAYNLY AGLADDSGKA NALLGLGEAC VAQVKYDDAE MAFTRAQKIY
TRIGNGPGRA NVVRALELLR RDRSKSEGGG ETPTAGSKHV RHPSKDEGMT SRRATRCRPR
TAQVLRHPNR CCPFSQPDLT GSRGC
//
