ID A0A2V1AMM6_9ASCO Unreviewed; 483 AA.
AC A0A2V1AMM6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN ORFNames=CXQ85_001085 {ECO:0000313|EMBL:PVH18796.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH18796.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH18796.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH18796.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC {ECO:0000256|RuleBase:RU280819}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU280819}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU280819}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU280819}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000256|ARBA:ARBA00007559,
CC ECO:0000256|RuleBase:RU280819}.
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:PVH18796.1}.
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DR EMBL; PKFO01000001; PVH18796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AMM6; -.
DR STRING; 45357.A0A2V1AMM6; -.
DR EnsemblFungi; CXQ85_001085-t46_1; CXQ85_001085-t46_1-p1; CXQ85_001085.
DR VEuPathDB; FungiDB:CXQ85_001085; -.
DR OrthoDB; 228697at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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.
DR PIRSF; PIRSF017321; GWT1; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU280819};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU280819};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU280819};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280819};
KW Reference proteome {ECO:0000313|Proteomes:UP000244309};
KW Transferase {ECO:0000256|RuleBase:RU280819};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU280819};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU280819}.
FT TRANSMEM 22..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 82..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 391..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 429..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 456..474
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
SQ SEQUENCE 483 AA; 53428 MW; B5AC80F5290A21A1 CRC64;
MSLKEQKEQF VSNLNGGSIE EVYLVTGVAI AGYVAHAIFK KYLLPGLNWA SSGPLLWAIE
FFFDELLLLQ AITVYSSKVT KIYVNALGLA ALIFVYAIVE KGISKPRKQT QPKKSKAATD
EFLPRKSFIT AYRAHMLVIT NLAILAVDFH AFPRRFAKVE TWGTSLMDLG VGSFVFSMGL
ANSRGVIKKK LAVGQKKVSY GKLVIGNTVK ALPVLGLGLV RLVSVKSLEY QEHATEYGIH
WNFFVTLGLL PVVLGIIDPI LNVVPRFFVA LAIGSLYEWT LNNTALLSFL LDESNRFESL
FAMNKEGLWS FCGYFSIFIF GQSFGSFVLT SRPTPNNLWG SYSKGRGIHL FTVSTTEGLV
VMTLITHGLF YIARESFHTG GISRRLANLP YVLWVVSYNA VFLLGYDLVE RLTGPLSSTV
LDAINANGLA TFLLANLLTG LINMTINTLA VNEPTTYAIL IGYALVWTSV AVFLHQHKIY
IKL
//