ID A0A1Y2H7D9_9FUNG Unreviewed; 394 AA.
AC A0A1Y2H7D9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Tubulin binding cofactor C-domain-containing protein {ECO:0000313|EMBL:ORZ28952.1};
GN ORFNames=BCR41DRAFT_382849 {ECO:0000313|EMBL:ORZ28952.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ28952.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ28952.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ28952.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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:ORZ28952.1}.
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DR EMBL; MCFF01000001; ORZ28952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2H7D9; -.
DR STRING; 64571.A0A1Y2H7D9; -.
DR InParanoid; A0A1Y2H7D9; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000193648; 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:UP000193648}.
FT DOMAIN 165..337
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
SQ SEQUENCE 394 AA; 44072 MW; 1008044D2F88DB57 CRC64;
MADVSKDFRA TFDPEKQSIE NELANLDKVP VGERQQKIDS LVQRIHALEK SITANIGVIS
PFDARVCLEA VSSLSTTLSQ LRVQLIPKPK FTFKSRKAIS PSTLAVSESV SAKDSSKSQT
SHVDESMFMK FENRTNEHLY IGTLLQQQQQ QQSNSMEEVY LGGLPVTTEN KALNADSSAA
ETTEEQKPKD VALTNLTDCT INLLHDNTPL GAIHIRNLKR CTLVIPPVSG SILLHDCEGC
VLIGACHQSR MHTSTDMDIY LHVTSEPIIE DCTNMRFAPY PYHDLFPTSV APVHDIGATA
ATTFSPESGD PRLNRLFELA KLNPQVNYFD RVKDFNWLRQ QKSPNWRVVD SSEIKEGVAP
LVLIKDELAE HQLQQQLRQQ QQGLRLKRFP VVAV
//
