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Database: UniProt
Entry: A0A0E0K149_ORYPU
LinkDB: A0A0E0K149_ORYPU
Original site: A0A0E0K149_ORYPU 
ID   A0A0E0K149_ORYPU        Unreviewed;       339 AA.
AC   A0A0E0K149;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G18480.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC02G18480.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC02G18480.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A0E0K149; -.
DR   STRING; 4537.A0A0E0K149; -.
DR   EnsemblPlants; OPUNC02G18480.1; OPUNC02G18480.1; OPUNC02G18480.
DR   Gramene; OPUNC02G18480.1; OPUNC02G18480.1; OPUNC02G18480.
DR   eggNOG; KOG2512; Eukaryota.
DR   HOGENOM; CLU_032612_2_0_1; -.
DR   OMA; YFQHEIT; -.
DR   Proteomes; UP000026962; Chromosome 2.
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:UP000026962}.
FT   DOMAIN          146..311
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..162
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   339 AA;  37035 MW;  3C2CF7BD4DBE6CFD CRC64;
     MEPEPEPDHS KPSAAAAAGG HRKHLAMLER LSKRAAAPSQ DSPVAAFLSR FAAAKLAAES
     ALSACRSSSP DDAQPSLSAA AAAIDDLDRI VAEASHSLPP YELRSALAAA SDLRAAHRMA
     ASDLRPKKSF SFRNKSKAPK NPPQDPPTSP PPTPPPEQPN PSVEAILPGF GFRGRRDAKL
     VKDLRVSDEK DGDFTLADLV CCQVYLKGKC RALYVHKLKD CRVFVGAVFG SVLIEDVEHC
     TFVMAAHQIR IHEARATDFY LRVRSRPIIE DCSGVRFAPH ALKYEGIGED LRDAGLEEET
     GNWANVDDFK WLRAVQSPNW CLVPEEERLQ TIDISDVQE
//
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