ID A0A0W8CMB5_PHYNI Unreviewed; 450 AA.
AC A0A0W8CMB5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tubulin-specific chaperone C {ECO:0000313|EMBL:KUF84866.1};
GN ORFNames=AM587_10008559 {ECO:0000313|EMBL:KUF84866.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF84866.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF84866.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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 -!- 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:KUF84866.1}.
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DR EMBL; LNFO01002720; KUF84866.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8CMB5; -.
DR EnsemblProtists; KUF84866; KUF84866; AM587_10008559.
DR OMA; CEFFVAC; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
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; 2.30.30.190; CAP Gly-rich-like domain; 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; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR016098; CAP/MinC_C.
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; PF01302; CAP_GLY; 1.
DR Pfam; PF07986; TBCC; 1.
DR Pfam; PF16752; TBCC_N; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT DOMAIN 43..76
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 252..418
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 50634 MW; 0C6517BF346F07A5 CRC64;
MEEPGTRCEL LSSGPSGSLR ASIKRYGEIA YIGAIEGLPG DGWLGVRLDK PLGKGDGTFQ
GRRYFDCKPL HGAIVRPERV NTIGEFPILT THEESLAHAL EERRKEKQGA RSAATVNNTH
DASKLNRELT TDELATAFWE KFTQQEEHIR KQVGLFCEQK KQPLPCDPAN EVKLDALVLE
VNSMRDAAAT ASSLYLSPYD TRHTQLIXSK LLKLIETTRT MFAPRKKFTF RARAANRAKA
KEAEKQDQPE SPALTGNQQA SSTSQRAIEF DELVHANKQN EVIIIDSSSF TDADYSKRRD
LNFSHLTDCV VLVCVETSAI RGDALKNCVF YTGAIFGSLW LENCNGCEFF VACRQLRVHL
STATTFHLRI PSHPIIEDCQ QMQFGPYRIQ FDGLEAQLER LGLSKDSGLW AKVNDFKWHK
AQQSPNWNIR DPKQPLPKIP VKLENLVSYD
//
