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Database: UniProt
Entry: F2PZI1_TRIEC
LinkDB: F2PZI1_TRIEC
Original site: F2PZI1_TRIEC 
ID   F2PZI1_TRIEC            Unreviewed;       271 AA.
AC   F2PZI1;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Tubulin folding cofactor B {ECO:0000313|EMBL:EGE07299.1};
GN   ORFNames=TEQG_06208 {ECO:0000313|EMBL:EGE07299.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the TBCB family.
CC       {ECO:0000256|ARBA:ARBA00025779}.
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DR   EMBL; DS995758; EGE07299.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PZI1; -.
DR   VEuPathDB; FungiDB:TEQG_06208; -.
DR   eggNOG; KOG3206; Eukaryota.
DR   HOGENOM; CLU_067577_2_0_1; -.
DR   Proteomes; UP000009169; 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:SF94; RESTIN HOMOLOG; 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.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701}.
FT   DOMAIN          12..98
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          214..248
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
SQ   SEQUENCE   271 AA;  29919 MW;  5565E1D19B59ECC8 CRC64;
     MDPLVSPADV SVQVSVASDN PVEKPSFATE RRVTPSWTVT QLKIKLETMT GIPPGSQRLM
     LKYPGREHQW MDGEEKTIGQ WGITKGCEIE IHDQRPVAAR PNYSDVSATE KFELSDSTYE
     TLPNSVLAWK KAQKLGRFDP NAASPEDKAR QQVQKDVNEI KAKGIKVSER AIILPSSPPH
     IRRGTIRFVG PVPAIPSPLG KTYSGEIPDD LAPIWVGIEL DEPTGKNDGS VNGERYFTCP
     NNCGVFVKPE KVEVGDYPPL GLDLDEDMEE I
//
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