ID A0A094F4B4_9PEZI Unreviewed; 378 AA.
AC A0A094F4B4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN ORFNames=V497_07862 {ECO:0000313|EMBL:KFY54237.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY54237.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY54237.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY54237.1}.
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DR EMBL; JPJZ01001213; KFY54237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094F4B4; -.
DR STRING; 1420910.A0A094F4B4; -.
DR HOGENOM; CLU_032612_1_0_1; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000029268; 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; 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; 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 PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029268}.
FT DOMAIN 206..332
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 137..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 41292 MW; 3CF7A99F2342F217 CRC64;
MEQAAGSTGI LPRQPFNDAS KSHADLKDNF YRYFQQEVAD LQDQIDKLER TALVGGERQD
AIDYCLASIS RLTTEVHDAL DFIPAYDQRA YTASINSLTD KFREARAKFA PKSRFAFKIK
KNESALSLQD VAAAAATNGR RADSENHASG LSSGEPSRPA ASSIQPPSRD YNAEISENSA
RIRAPSFRQA KSVAISDHEG LHIILPSSAS HATSSGSLTD LTKCIVDMSI STANGKPFAG
LALKNITNSL IVAGQVAGAT HITNVRDTVV VVSSRQVRMH DCVNVDVYLS SMSRPIIEDC
KNIRFAPIPK SYEVPSDEPT ENHWDQVDDF KWLKAEKSPN WSVLEESDRL PEGIWTTVVP
GKPGMAAEDI LKQVGTSK
//
