ID A0A0J8RDH1_COCIT Unreviewed; 392 AA.
AC A0A0J8RDH1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=GPI-anchor transamidase {ECO:0000313|EMBL:KMU82591.1};
GN ORFNames=CIHG_00372 {ECO:0000313|EMBL:KMU82591.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU82591.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS016981; KMU82591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RDH1; -.
DR STRING; 396776.A0A0J8RDH1; -.
DR VEuPathDB; FungiDB:CIHG_00372; -.
DR eggNOG; KOG1349; Eukaryota.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054563; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..392
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028280338"
FT ACT_SITE 150
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 192
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 392 AA; 43699 MW; F6D8D264F30D64B6 CRC64;
MNLLLAFVYI LTLGLLLANG SAFVAATHTS NWAVLVSTSR FWFNYRHLAN VLSLYRTVKR
LGIPDSQIIL MLPDDMACNP RNAFPGTVYN NADRALDLYG DNIEVDYRGY EVTVESFIRL
LTDRLGEDVP RSKRLGSDAG SNVLVYMTGH GGDQFLKFQD SEEIGAWDLA DAFGQMWEKK
RYNELLFMID TCQANTMFTH FYSPNIIATG SSALDQSSYS HHADSDVGVA VIDRWTYYIL
EFLETQVTSP SSKLTLGDLF RIHTTSQRFT RSQAGRLRKD MDFFGNVQDV EIEAGQNVTA
DIREDLAAVA KLVEEWKQRE RAYFSNASST ESVSEQLSST AQKNRVTLSP VQTPTGAVRM
KDVNTWNKQA VGVSLLAGLG AVWLAGSLTA KS
//
