ID A0A0C9YXN4_9AGAM Unreviewed; 900 AA.
AC A0A0C9YXN4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=TPR-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PISMIDRAFT_179826 {ECO:0000313|EMBL:KIK18659.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK18659.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK18659.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK18659.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN833800; KIK18659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YXN4; -.
DR STRING; 765257.A0A0C9YXN4; -.
DR HOGENOM; CLU_006762_1_1_1; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000054018; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017:SF1; LD02225P; 1.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF81901; HCP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054018};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 91..124
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 125..158
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 159..192
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 196..229
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 233..266
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 270..303
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 342..375
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 376..409
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 31..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 99816 MW; 5AFF0693E3D85A29 CRC64;
MSHRRQPDRD VVHPHPHGLV TLPAAASASA VAPPHLNGNA TVPPSTPGSI SNGSNQASAQ
LVSPTVVPTA TAPAPNGVPT STIHKLALAN EQTWLLIGRV AEQMGDLEHA ITAYENALRH
NPLSLSGLTQ VAGIARIKEN YPKAIDYFQR VLQLQEDNGE VWSALGHCYL MQDDLQKAYS
AYQQALYLLP NPKEDPKLWY GIGILYDRYG SLDHAEEAFA SVLKMDKDFD KANEILFRLG
IIYKQQGKYD ESLGCFDRIL RNPPSPLAHA DIWFQIGHVY EQQNDYTRAK GAYERVVDDN
PTHAKVLQQL GWLYHQEGSS FQNQELAIQF LTKSLEADPS DAQSWYLLGR AYMAGQKYNK
AYEAYQQAVY RDGRNPTFWC SIGVLYFQIN QFRDALDAYS RAIRINPYIS EVWFDLGSLY
ESCNNQISDA IDAYARAAEL DPGNHVISQR LQLLKNAQAT GSQLPAAPGP QDVHPNAYAN
PSAPPPGLSG PPLLLQSTST RSLHRSESRG PGNNDNIHLP LPSVPVSRSS PGPPFRGPPP
PVSIDESRHP PSHTPLAPMD VDRHHHRDFP GPVRESVGRG PAGHQCLLLH HPVPQQQLPT
EELRSSANHD LPQHSEYFNR PLRVSSGSSS PAPHPTRPRS PGSSFSAYAP PGRQPIGPGQ
PSIPASQRSP PLYPREPARP TDRDMAWDRR GPPPEHHRDW EDRDRRGRSE YPGQSSQQPY
YASRSPGPRR APSPMETSPR STHHPRPLWD SKPPSGPPHP PLAPSNPPES GHWRYDPARF
DARERPMERD VESRRQSGSM ANSPEAAPRI PLHTSMRMSM SPEPSSAESK SRRKQPQLLK
DKDSDTQSVS GSIPSDVPKK ERKKRQRRGK DEQSARLESN GLPANMPASF KVASFSAKDD
//
