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Database: UniProt
Entry: A0A109FKM6_9BASI
LinkDB: A0A109FKM6_9BASI
Original site: A0A109FKM6_9BASI 
ID   A0A109FKM6_9BASI        Unreviewed;       251 AA.
AC   A0A109FKM6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Tubulin-folding cofactor B {ECO:0000313|EMBL:KWU46132.1};
GN   ORFNames=RHOSPDRAFT_15555 {ECO:0000313|EMBL:KWU46132.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46132.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU46132.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU46132.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TBCB family.
CC       {ECO:0000256|ARBA:ARBA00025779}.
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DR   EMBL; KQ954468; KWU46132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FKM6; -.
DR   STRING; 1305733.A0A109FKM6; -.
DR   OrthoDB; 5485090at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF14560; Ubiquitin_2; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          191..225
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          232..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..251
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  27500 MW;  4BD6105FDF3517B0 CRC64;
     MSLISVWVSS PDTHSERRLG TDLTIHQLKL KLEPVTGIPL ASQTLSLRRT APETGHGASS
     SLGQLVANLD DASKTLADYG VQEYMTIRVD SSDPHARSLA GQFTDDSQVE KFELTEEEYA
     KRADTVLAYK KRNQLGRFAP SASPAPHAAP SIPSDLVPGA RCQVSLSDEL QRRGTVRFVG
     PTEFGPQDGS VWVGVEWDEP VGKHDGTVDG KRYFETGPLR ASFVRPDKVT VGDFPELDPF
     ADEDNDEEME M
//
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