ID A0A0B7NAD4_9FUNG Unreviewed; 393 AA.
AC A0A0B7NAD4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN Name=PARPA_05861.1 scaffold 20154 {ECO:0000313|EMBL:CEP11954.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11954.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11954.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11954.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI
CC during GPI precursor assembly. {ECO:0000256|ARBA:ARBA00024708}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363075}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC subfamily. {ECO:0000256|ARBA:ARBA00006065}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363075}.
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DR EMBL; LN727218; CEP11954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NAD4; -.
DR STRING; 35722.A0A0B7NAD4; -.
DR OrthoDB; 37262at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR22760:SF4; GPI MANNOSYLTRANSFERASE 3; 1.
DR Pfam; PF03901; Glyco_transf_22; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 393 AA; 45980 MW; 89B46B6AE7CA06DA CRC64;
MVQTTIQPTS TISSRTFIFV TCLLFRLLNA YYTRTYDNPD EYWQGHEVAH ELVFGNGYLT
WEWREKIRSF LHPITIALAY KVVQLLGLQN THVLVAAPRY FQATLAAVAD VATYTLAKKV
IGNDIALSML FTTLCSWFNF QMAARTLSNS MEMVFTIIAL NYWPLPGIVK TTGKSWAYKW
IDLAISGGPF TAMFKQRIYT WVVVIYSLLP HKEFRFIFPI VPLMLMIAAY GIQQTGSPRW
RKRIMLFLVF TQLPMALYTS IWHQRGVVDV MLWMRSQPRN ISVGVLMPCH STPWYSIIHD
NIPMWFLTCE PPLGESNELD EADQFYANPT EFLKTHQKDR LWPTTHLLLF DNLIPKIREY
LDKEGYKECQ RFFNSHFHDD ERRRGDVVLV KQR
//