ID   GWT1_CHAGB              Reviewed;         512 AA.
AC   Q2HCW8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=GPI-anchored wall transfer protein 1;
DE            EC=2.3.-.-;
GN   Name=GWT1; ORFNames=CHGG_01936;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC       ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
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DR   EMBL; CH408029; EAQ93701.1; -; Genomic_DNA.
DR   RefSeq; XP_001221157.1; XM_001221156.1.
DR   AlphaFoldDB; Q2HCW8; -.
DR   STRING; 38033.XP_001221157.1; -.
DR   EnsemblFungi; EAQ93701; EAQ93701; CHGG_01936.
DR   GeneID; 4386492; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   InParanoid; Q2HCW8; -.
DR   OMA; GLYVMQP; -.
DR   OrthoDB; 1202772at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:UniProt.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR009447; PIGW/GWT1.
DR   PANTHER; PTHR20661; PTHR20661; 1.
DR   Pfam; PF06423; GWT1; 1.
DR   PIRSF; PIRSF017321; GWT1; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..512
FT                   /note="GPI-anchored wall transfer protein 1"
FT                   /id="PRO_0000246288"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          118..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   512 AA;  55591 MW;  FD4EA223D85F74A4 CRC64;
     MANLADDLAA TAAKAAASPS YKQLKEDFVS NLSGGSVVEI AQVCAVAPVV SLLWSALQAR
     QTFFKPYNPL AFVVDFLLNV GALLLSVTLY SSVPLLLNIL LLVPAAAVYF SLSDNPSARR
     KKPQLPPNAQ SKASPGPPGA LSTKPFLTNY RGNMMVVTCI CILAVDFRLF PRRYAKVETW
     GTSLMDMGVG SFVYSAGVVA SRPVLKERAD GRSTPLATRL VRSLRHSLPL LALGVVRLLS
     VKGLDYAEHV TEYGVHWNFF FTLGFLPPFV ALFQSALRLV PSYAGLAILL GVLYQVVLET
     TELKAYILAG PRTDFLSMNR EGIFSFFGYL AIFLAGQDTG MLVLPRSLVP RDGAPGTTGS
     RRRALVLRLA GWSAIWITLY LLCTDYTYGA GLTVSRRLAN LPYILWVVAS NSALMLSFAL
     VDTFLFPAFY KAQDAKAEKE AYHTATSRVL QAYNRNGLAI FLLANLLTGL VNMTVRTLDV
     GRIPTMGILG GYMAVLTGVA VGLDMYNITI KL