ID A0A098VTV5_9MICR Unreviewed; 320 AA.
AC A0A098VTV5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=DI09_15p250 {ECO:0000313|EMBL:KGG52558.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG52558.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG52558.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG52558.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG52558.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-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: 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:KGG52558.1}.
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DR EMBL; JMKJ01000066; KGG52558.1; -; Genomic_DNA.
DR RefSeq; XP_013238985.1; XM_013383531.1.
DR AlphaFoldDB; A0A098VTV5; -.
DR GeneID; 25258552; -.
DR VEuPathDB; MicrosporidiaDB:DI09_15p250; -.
DR HOGENOM; CLU_869002_0_0_1; -.
DR OrthoDB; 37262at2759; -.
DR Proteomes; UP000029725; 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; 1.
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:UP000029725};
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 74..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 320 AA; 36368 MW; 273CF45209700D32 CRC64;
MSVFAAITDY FIYVISLNNH GAEVAAWTLL TTLLSHFNFT YSTRASSNSI EACLSLLAYY
FWPWSGSDKV SKLFIPLCIV GIGTLIRPTL AILWVIPWVL LFFKLTEKTD MLRMITISVC
LIIGLGLFVD FVFYQRWLLT WYNFFCINLG DEGVSSYYGT HPLLWYFFCA IPILLGPLAP
FFVLGSELRF LLPIFPMMNM ITGIGFHRFY HSTKITHRKK AIFISASFAI SAIVSVLYCR
GFSTAGIAIT DHLNKIVGTK SVFFLFSHAA PLYAGVLRPE AKLDYVHMEP PFLKNFPHTM
PVCMTLSWHG NLWPQNAPML
//
