ID A0A2N3NFN8_9PEZI Unreviewed; 346 AA.
AC A0A2N3NFN8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN ORFNames=jhhlp_003004 {ECO:0000313|EMBL:PKS11243.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS11243.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS11243.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS11243.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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:PKS11243.1}.
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DR EMBL; NLAX01000008; PKS11243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3NFN8; -.
DR STRING; 41688.A0A2N3NFN8; -.
DR VEuPathDB; FungiDB:jhhlp_003004; -.
DR InParanoid; A0A2N3NFN8; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000233524; 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; 1.
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:UP000233524}.
FT DOMAIN 150..301
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
SQ SEQUENCE 346 AA; 37992 MW; 6A051D12E7364937 CRC64;
MSNNILKFYQ HFQAAVASLD TEIVQLSSAS SRQNAIDTIR LGIAHLSNEL ADAAEYLPTY
DQKSYAETIK GLTEKLDREV DKVAPRQRFQ FKARSRNAAQ ESQEDRRHNV GVLASYQDTQ
AGSAAPSKQD ELAANAKDYN QEIKGSSSSA VRRPSFSAAK TVSLSQHKEL HVVLAPSASQ
AATYGDLTDL EACVIDMSAA ARGEVAFSGL ALKNLRKCII VTGSVDGPVH ITGISDSILV
VASRQVRIHE CKNVKFYLHC SSHPIIEDCT QVQFAPIPEC YTPRWSSTHE NKWDQVDDFK
WLKADHSPNW SILPESGRLS GSFWTEWVAG GAEVRVADIL NKGGIS
//
