ID   ALG3_PHANO              Reviewed;         609 AA.
AC   Q0TVF9;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE            EC=2.4.1.258;
DE   AltName: Full=Asparagine-linked glycosylation protein 6;
DE   AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE   AltName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
GN   Name=ALG3; ORFNames=SNOG_16505;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC       linkage to Man(5)GlcNAc(2)-PP-Dol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC         dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC         Xref=Rhea:RHEA:29527, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:12627, Rhea:RHEA-COMP:12628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515,
CC         ChEBI:CHEBI:132516; EC=2.4.1.258;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ALG3 family. {ECO:0000305}.
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DR   EMBL; CH445373; EAT76110.2; -; Genomic_DNA.
DR   RefSeq; XP_001806617.1; XM_001806565.1.
DR   AlphaFoldDB; Q0TVF9; -.
DR   STRING; 13684.SNOT_16505; -.
DR   EnsemblFungi; SNOT_16505; SNOT_16505; SNOG_16505.
DR   GeneID; 5983549; -.
DR   KEGG; pno:SNOG_16505; -.
DR   eggNOG; KOG2762; Eukaryota.
DR   HOGENOM; CLU_448416_0_0_1; -.
DR   InParanoid; Q0TVF9; -.
DR   OrthoDB; 1122031at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   Gene3D; 1.20.1290.10; -; 1.
DR   InterPro; IPR029032; AhpD-like.
DR   InterPro; IPR007873; Glycosyltransferase_ALG3.
DR   PANTHER; PTHR12646; PTHR12646; 1.
DR   Pfam; PF05208; ALG3; 1.
DR   SUPFAM; SSF69118; SSF69118; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..609
FT                   /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT                   mannosyltransferase"
FT                   /id="PRO_0000350932"
FT   TOPO_DOM        1..388
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..430
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        452..467
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..549
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        550..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        571..609
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   609 AA;  68416 MW;  9077801D747BB97D CRC64;
     MSKLSPALKQ LINAAHSRPG PVPAPPRIQA VYQRIQEEAT ERKLGRPSWL GISTAATMTM
     NSPESMIALY NSTSASRPEN ESVQIAEFMR EIGLKCIGFN GIPRTINMLN AFRASLPPTI
     ASSLNTTPTR SPSPQNILDT NTRGRALWDA IYRPLETKLI DKLGDAHPDL PVFIINQEYG
     GLFTDPPGKP GAKVGRVTTS LVAITCLRAQ QGVGPQVLSH VFGLRKGWED GTWKEEPEAG
     SEEAIRWLVS DEGCTWVLEK VDELVEALGG GAGTLSPAID EKPKELTTTK TMSLINRVRD
     LATNDEHTRW MIPLLLVVDA ALCGVVIEKI PYTEIDWTTY MQHIALIIKG ERDYTKITGS
     TGPLVYPGAH VWIYKQLFKI TDEGRDIQRA QYIFALVYLG TLALVFQCYR KARVPPYVFP
     LLILSKRLHS IFLLRCFNDC FAVLGLFAAL FCYQRDQWHV GSFLFATGLN VKMSLLLPLP
     AMGVLMIMKL GSREAMTHAM IIFQTTVLFG YPFRKAAFSY FGRAFELSRQ FTYKWTVNWR
     FVSEETFLSK PFALGLLSVH VTLLITFFLT RWIKPSKRTP KQFLKIIMPQ AEPRDQDTMA
     LRITPNLHT