ID   A0A0B0PXJ2_GOSAR        Unreviewed;       402 AA.
AC   A0A0B0PXJ2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative GPI-anchor transamidase {ECO:0000313|EMBL:KHG29169.1};
GN   ORFNames=F383_11697 {ECO:0000313|EMBL:KHG29169.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG29169.1, ECO:0000313|Proteomes:UP000032142};
RN   [1] {ECO:0000313|Proteomes:UP000032142}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN448309; KHG29169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0PXJ2; -.
DR   SMR; A0A0B0PXJ2; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000032142; 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; 2.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   3: Inferred from homology;
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..402
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002077795"
FT   TRANSMEM        382..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   ACT_SITE        201
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ   SEQUENCE   402 AA;  46202 MW;  D6A5CAD36A1B9E18 CRC64;
     METFINPKSL FHLLLLPCLL LYSSIAYNSS PVEAAMHTNN WAVLVCTSRF WFNYRHMANT
     LSLYRTVKRL GIPDERIILM LADDMACNTR NKYPAQVFNN ENHRLNLYGD NVEVDYRGYE
     VTVENFLRVL TGRHETAVPR SKRLLSDEGS HILLYMTGHG GDEFLKFQDS EELQSHDLAD
     AVKQMKEKHR FKELLIMVDT CQAATLFNQF QSPGVLAIGS SMKGENSYSH HLDSDVGVSV
     VDRFTYYTLA FFERLNIYDN ASLSSLFSSY NPSLLMSTAY YRKDLYKRRL EEVPVTNFFG
     SVMETIHTDA AYKALSRRNS GRFEDEMSLD QSVHHIERRM LIKVNDGDEI HDINPEGEEG
     ACKCPWSTFR NTFQKAENVD SLVNYGLVAM IPLLVISTWL VQ
//