ID A0A1E5VH82_9POAL Unreviewed; 361 AA.
AC A0A1E5VH82;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Tubulin-folding cofactor C {ECO:0000313|EMBL:OEL24498.1};
GN ORFNames=BAE44_0014482 {ECO:0000313|EMBL:OEL24498.1};
OS Dichanthelium oligosanthes.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL24498.1, ECO:0000313|Proteomes:UP000095767};
RN [1] {ECO:0000313|EMBL:OEL24498.1, ECO:0000313|Proteomes:UP000095767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC TISSUE=Leaf {ECO:0000313|EMBL:OEL24498.1};
RA Studer A.J., Schnable J.C., Brutnell T.P.;
RT "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT species.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state.
CC {ECO:0000256|ARBA:ARBA00026055}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TBCC family.
CC {ECO:0000256|ARBA:ARBA00008848}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEL24498.1}.
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DR EMBL; LWDX02039584; OEL24498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5VH82; -.
DR STRING; 888268.A0A1E5VH82; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000095767; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR Gene3D; 2.160.20.70; -; 1.
DR Gene3D; 1.20.58.1250; Tubulin Binding Cofactor C, N-terminal domain; 1.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR006599; CARP_motif.
DR InterPro; IPR027684; TBCC.
DR InterPro; IPR031925; TBCC_N.
DR InterPro; IPR038397; TBCC_N_sf.
DR InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1.
DR PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1.
DR Pfam; PF07986; TBCC; 1.
DR Pfam; PF16752; TBCC_N; 1.
DR SMART; SM00673; CARP; 2.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000095767}.
FT DOMAIN 167..328
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 38950 MW; CAC4EA2E294B3F75 CRC64;
MPSGGAAGME PEPDQPKAVA GGGRRKHLAM LERLSKHSSS STTSTASALP DSTSASPVVA
FLTRFAAAKL AAESALSACR ASSSPEDEAT ASLAAAAAAI DDLDRLVAES SHALPPYELR
SALAAAADLR AAHRAAASEI RPKKSFSFRN KSRAPKNPPQ DPATVPPPQP PPPEQPKPSI
DVILPGFGFR ARNGATLVKD LRVSNDKDGD FTLADLVSCE VFLKGKCRAL YVHKLRDCRV
FVGAVIGSVL IEDVEGCTFV MAAHQIRIHE ARATDFYLRV RSRPIIEDCS GVRFAPHALK
YDGIDEDLKE SGLEEETGNW ANVDDFKWLR AVQSPNWCLV PEEERLQTVD ISEIHEREHD
S
//
