ID A0A165DW89_9APHY Unreviewed; 553 AA.
AC A0A165DW89;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=GPI-anchor transamidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LAESUDRAFT_759990 {ECO:0000313|EMBL:KZT05757.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT05757.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT05757.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT05757.1,
RC ECO:0000313|Proteomes:UP000076871};
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; KV427628; KZT05757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DW89; -.
DR STRING; 1314785.A0A165DW89; -.
DR InParanoid; A0A165DW89; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000076871; 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:UP000076871};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..553
FT /note="GPI-anchor transamidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007856862"
FT ACT_SITE 165
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 553 AA; 61783 MW; 3309ACB15B042020 CRC64;
MSRLRFLLLV TLYIVSWLGA ATADGLIPSD HASQPAKDGG SAHTNNWAVL VCSSRYWFNY
RHMANALGMY RTVKRLGIPD SNIILMLADD AACNTRNKFP GCVYANQGRH LDLYGDNIEV
DYRGYEVTVE NFLRVLTGRM EPSVPRSKRL LTDDRSNIFV YMTGHGGNEF LKFQDNEEIS
AFDIADAFEQ MWQKKRYNEI LFMIDTCQAN SMFSKFYSPN ILATGSSEVH ENSYSHENDY
EIGVAVIDKF THYILQFMEG INKTSQASMK DLFDTYDFKK IESHAGVRSD LFNRPLEDTL
VTDFFGGVAQ AEVLSSAIDG PVLEPDAQLT SSAEAELELD MDMPFFGLPT ETANSSAAGA
PPLTSHGSPD LNLEDIIVAA SYSSHSTWAA KARGLRAWTS SLLVLALIGW PVLFCLDLFS
VQVQHWLPDP HIAPGRVIAL ETYQSAFPIN DPHQWVPVLP SFLFPFFVPV QAHDGAAEVM
EGIVGDAWAY HESGKDSFNS SRLDDCLDLT PQSANEALRR RLVYLPYRSS GFVFPAYQPS
SRNPSIWLPP RSP
//
