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Database: UniProt
Entry: M7NL51_PNEMU
LinkDB: M7NL51_PNEMU
Original site: M7NL51_PNEMU 
ID   M7NL51_PNEMU            Unreviewed;       442 AA.
AC   M7NL51;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000256|ARBA:ARBA00015841};
DE            EC=2.4.1.142 {ECO:0000256|ARBA:ARBA00012611};
GN   ORFNames=PNEG_02334 {ECO:0000313|EMBL:EMR09388.1};
OS   Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS   (Pneumocystis carinii f. sp. muris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX   NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR09388.1, ECO:0000313|Proteomes:UP000011958};
RN   [1] {ECO:0000313|Proteomes:UP000011958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX   PubMed=26899007; DOI=10.1038/ncomms10740;
RA   Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA   Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA   Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA   Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA   Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA   Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA   Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT   "Genome analysis of three Pneumocystis species reveals adaptation
RT   mechanisms to life exclusively in mammalian hosts.";
RL   Nat. Commun. 7:10740-10740(2016).
CC   -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC       oligosaccharide for N-glycosylation. Involved in assembling the
CC       dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC       surface of the ER. {ECO:0000256|ARBA:ARBA00024899}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC         diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC         Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58472; EC=2.4.1.142;
CC         Evidence={ECO:0000256|ARBA:ARBA00001259};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
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:EMR09388.1}.
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DR   EMBL; AFWA02000013; EMR09388.1; -; Genomic_DNA.
DR   RefSeq; XP_007874337.1; XM_007876146.1.
DR   AlphaFoldDB; M7NL51; -.
DR   STRING; 1069680.M7NL51; -.
DR   GeneID; 19896027; -.
DR   VEuPathDB; FungiDB:PNEG_02334; -.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_0_0_1; -.
DR   OMA; CKLIIDW; -.
DR   OrthoDB; 1219598at2759; -.
DR   Proteomes; UP000011958; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR026051; ALG1-like.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR13036; BETA1,4 MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011958};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          254..419
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   442 AA;  50977 MW;  9796E365DEDA45EF CRC64;
     MIIWYIILFF AGFGLQKLLR SRYKNNRKIS QRSICLVALG DLGRSPRMQY HALSFSKHGF
     EVNLVGYQGS LLFPNIQESK NIHIIYIPFE PKFLNKCNLL PFLLSGPIKV FFQTFFLFFA
     LFYLPQSTEY LVLQNPPSIP SFGVTRLICS MRSIKLIIDW HNLGYSVLSL KLGSKHILTL
     LYKWYERVFG NCADIHFTVS YAMTTFLQEK WKYKSPIYTL HDRPPMHFKP LDNLEKSSFL
     STFVHTYDFD ISNEKTKLLV SSTSWTADED FSILLEAFIT FDRMNTILSK NREPLSILAI
     ITGKGPLRKF YEQKIKNLNL KYVKIVTAWL DAKDYPRFIG SADLGICLHT SSSGLDLPMK
     IVDMFGCGIP VCAIESPALP ELVKDGKNGI IFSSSNQLAN SLKKLFYSHE ELAKLKKGAM
     EETRYRWHNE WDAKIAPLFK KP
//
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