ID A0A165K0P4_9BASI Unreviewed; 400 AA.
AC A0A165K0P4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=GPI-anchor transamidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CALCODRAFT_522367 {ECO:0000313|EMBL:KZT62510.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT62510.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT62510.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT62510.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV423916; KZT62510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165K0P4; -.
DR STRING; 1353952.A0A165K0P4; -.
DR InParanoid; A0A165K0P4; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000076842; 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:UP000076842};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..400
FT /note="GPI-anchor transamidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027627080"
FT REGION 302..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..335
FT /note="Acidic residues"
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 400 AA; 44092 MW; B5EFAF60ACD472C6 CRC64;
MLGRIPSGLL ALLLLLLSGA TTPGHEHTNN WAVLVCASRY WFNYRHMANT LGMYRTVKRL
GIPDSNIILM LADDAACNAR NHFPATVFAN ADRKLDLYGE NIEVDYRGYE VTVENFIRLL
TGRVSPTLPR SKRLLTDSRS NVFVYMTGHG GAEFLKFQDN EEISAFDVAD AFEQMWQKRR
YNELLFMVDT CQANTMYGKI YSPNILATGS SELKENSYSH HNDADIGVAV IDSFTHYILQ
YMEGENKTSK ATMKDLFDTF DPALIKSHAG VRSDLYPRPL DQVRITDFLG AVSKVDVLPS
DARAEDGTDQ LAGEGVLPPA VEDEDEEDED ELAGEREGEA ALPVLGGPTS ARVPPLPSAE
LSADQPAVWH MAGKEGPTLR AWGAAGAVLS LLVWRMAAAS
//
