ID D4D8K5_TRIVH Unreviewed; 402 AA.
AC D4D8K5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=GPI-anchor transamidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRV_03442 {ECO:0000313|EMBL:EFE41821.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE41821.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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:EFE41821.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACYE01000179; EFE41821.1; -; Genomic_DNA.
DR RefSeq; XP_003022439.1; XM_003022393.1.
DR AlphaFoldDB; D4D8K5; -.
DR MEROPS; C13.005; -.
DR GeneID; 9580986; -.
DR KEGG; tve:TRV_03442; -.
DR HOGENOM; CLU_044656_2_2_1; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:InterPro.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:InterPro.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; GPI-ANCHOR TRANSAMIDASE; 1.
DR PANTHER; PTHR48067:SF1; GPI-ANCHOR TRANSAMIDASE; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..402
FT /note="GPI-anchor transamidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027699420"
FT REGION 337..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 191
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 402 AA; 45074 MW; 29C1A02F43EA6FC0 CRC64;
MELRLFYPFL AALLAIFLAS SVSSAAHTSN WAVLVSTSRF WFNYRHLANV LSLYRTVKRL
GIPDSQIILM LPDDMACNPR NAFPGTVYNN ADRALDLYGD NIEVDYRGYE VTVESFIRLL
TDRLGDDVPQ SKRLGSDAGS NVLVYMTGHG GDQFLKFQDS EEIGAWDLAD AFGQMWEKKR
YNELLFMIDT CQANTMYTHL YSPNIIATGS SEIDQSSYSH HADSDVGVAV IDRWTYYILE
FLETQVTSAN SKRTLGDLFD SYDESKIHSQ PGVRWDLFPG GEAEGRLRTV MDFFGNVQEV
EVEAGSSVND TEHSVKEDLV AIAKLVEQWK EMEKEHMENI RGPSSVGQKK PTLPSETGSP
IHKLAGPMKM RDADDWSKRV IGLSLLFGIG GVWFAGSLRG RS
//
