ID A0A1J9R5V6_9PEZI Unreviewed; 425 AA.
AC A0A1J9R5V6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tubulin-specific chaperone c {ECO:0000313|EMBL:OJD35594.1};
GN ORFNames=BKCO1_16000118 {ECO:0000313|EMBL:OJD35594.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD35594.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD35594.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD35594.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-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 -!- 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:OJD35594.1}.
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DR EMBL; MNUE01000016; OJD35594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9R5V6; -.
DR STRING; 236234.A0A1J9R5V6; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000183809; 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:UP000183809}.
FT DOMAIN 223..377
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 142..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 45311 MW; 6FB12415CE9F16E6 CRC64;
MALPLQQPAD SGLKERFFRY FQHEVTELQE EINTLANKAV TGGERADGVE HCLAGIARLS
REVKDASSYI PAYDQRTYSE AIKALNDKLN QTRASFAPRS KFSFKSTRQS SATTAVSHHK
NSSAISLADV AELASQQRLK LPGAHQHAGA NDPTASSGDT STAESSAFAS PAAPGTPANE
SAEDGSSGQN GAGGLDDRSG GAAAGQDGFV NRHLSSAQQQ GSPMRKPSFS GTSSVAIAGH
TGLHIILPPT ASHATSAGTI ANVRRCIVDM SQPTAEASGG APFAGLTVKN VRDSLLVCGR
VAGAIHVTAV EGSVLVVRAR QFRMHECKNV DVYLRCDSRP IIEDCAGIRF APLPETYTHE
DSSAQPNLWD QVDDFKWLKA EHSPNWSVLP PDTRISEHVW KDLVPGSPDM GLEEIFQAVK
IQPKH
//
