ID A0A0G2ESB4_9EURO Unreviewed; 412 AA.
AC A0A0G2ESB4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative gpi-anchor transamidase {ECO:0000313|EMBL:KKY25051.1};
GN ORFNames=UCRPC4_g02108 {ECO:0000313|EMBL:KKY25051.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY25051.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY25051.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY25051.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY25051.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY25051.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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}.
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:KKY25051.1}.
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DR EMBL; LCWF01000050; KKY25051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ESB4; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000053317; 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:UP000053317}.
FT REGION 338..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 412 AA; 46222 MW; D555DB9C808E5FCC CRC64;
MLIRHPSYFT PIAIVWFFFW YDVATCAHTS NWAVLVSTSR FWFNYRHLAN TLSLYRTVKR
LGIPDSQILL LLPDDMACNP RNAFPGTVYS NADRQTDLYG TNIEVDYRGY EVTVENFIRL
LTDRWPADVP ASKRLNTDSG SNILIYLTGH GGDQFLKFQD SEEIGAWDIA HAFAQMHEKK
RYNEILFMID TCQANTMFKH FYSPGIIATG SSELDQSSYS HHADLDVGVA VIDRWTYYIL
EFLETQVTGP GSDKTLGDLF DSYDESKIMS HPGVRWDLFP GGEQAGREKK LVDFFGNVQG
VEVGNTSWTD RQATIDSWKE DMEGLKRIIR DYESRHNDAN ASATDATQSA DAPKSEPASS
QSQTSKSNVK LQAAKLSTDT ATSTSWIRKA GGLAALSGLT GAWYFGGKVL PI
//