ID C4JY68_UNCRE Unreviewed; 966 AA.
AC C4JY68;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=GPI-anchored wall transfer protein 1 {ECO:0000256|ARBA:ARBA00014495};
GN ORFNames=UREG_07119 {ECO:0000313|EMBL:EEP82254.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP82254.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC {ECO:0000256|ARBA:ARBA00002531}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGW family.
CC {ECO:0000256|ARBA:ARBA00007559}.
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DR EMBL; CH476619; EEP82254.1; -; Genomic_DNA.
DR RefSeq; XP_002582346.1; XM_002582300.1.
DR AlphaFoldDB; C4JY68; -.
DR STRING; 336963.C4JY68; -.
DR GeneID; 8444563; -.
DR KEGG; ure:UREG_07119; -.
DR VEuPathDB; FungiDB:UREG_07119; -.
DR eggNOG; KOG0411; Eukaryota.
DR HOGENOM; CLU_306574_0_0_1; -.
DR InParanoid; C4JY68; -.
DR OrthoDB; 228697at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009447; PIGW/GWT1.
DR PANTHER; PTHR20661; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS W PROTEIN; 1.
DR PANTHER; PTHR20661:SF0; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS W PROTEIN; 1.
DR Pfam; PF06423; GWT1; 1.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 118..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 106018 MW; 548CECBBB3BA28AA CRC64;
MPFQKELHRC RNCLGLPFGH GRDSESPRMF RPKLFEPQSS SSRLDDIKIS PNGIGGEKSF
SLSSLYQNRD SLIPPGFDPK CKIPDMPPPI EPSDGVLPKR LFKKHTEIPI LGSSIGVVTR
DGRGRSRKAF VRTPKDRPTS DQQGKRLRSP LYYPNGGFSS DYVPLDKRRR HVPSQSSSST
LSSSSSSSSS SSSSSSSSSS SGSPSPSPSP SSPFSSPSRS HSRSHSSSSS SSSSSSSSSS
SSSSSSSASS LAPAPRPPRG PSSPPPVSSI FIPVKPPSAK PSPARRESRT PSPRPDSDPV
GRPSGPRRQH VTIAPDSRKA ATKEQRRPHI IIEPKERVAA PKSHPHITIT PRDDNSHPHE
PPRSPPRSPA RSPARSPAHS PTRSPAHSPT RSPTRSPPRS TSRSTSSSPS RPRVVEIAPK
KKVHFMDDDP TPKPQPFRTH GRPKLGANKT ICAPLGDPVL RGTYKYWTII NMTKSYKARK
EEFVSNLGGG DIWEINAVIF VAQSAVLLWS ALQSRRSFFS PYQVPALVTD FLLNVLAILF
ATTLYSTAPI LLNILLVTPA IFILLGRKRN QPPQKAKPPP QVVSASPHGA STSELDPFPV
RPFLTVYRGG MMVVTCLSIL AVDFRVFPRR FAKVENWGTS LMDLGVGSFV FSGGVVSARS
ILKSRDRSAG TLPRRLLASV RHSIPLFILG FVRLFSVKEL DYAEHVTEYG VHWNFFFTLA
FLPPFVELFH ALTTIIPSYE VLSLVVSVAY QVLLESTTLK EYILVSPRGP SLLSKNREGI
FSFIGYLAIF LSGRATGLRI IPRETQPSKS PDSQKKGLIR MATWTSIWTV LFMFNSHHVF
GLGASIPVSR RLANMPYVLW VIAFNNFQLF LFWILESLFF PLVYKAGDRK TEAERSDFAT
SRILRAFNKN GLTIFLIANL LTGAVNLGVN TLDASKEIAI CILIGYAALL TAISLALDYW
NVKLKI
//
