ID A0A178BAX9_9PLEO Unreviewed; 567 AA.
AC A0A178BAX9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=IQ06DRAFT_238089 {ECO:0000313|EMBL:OAL07287.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL07287.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL07287.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL07287.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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->2)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
CC Evidence={ECO:0000256|ARBA:ARBA00034044};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
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.
CC {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
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DR EMBL; KV441705; OAL07287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178BAX9; -.
DR STRING; 765868.A0A178BAX9; -.
DR InParanoid; A0A178BAX9; -.
DR OrthoDB; 122000at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760:SF1; DOL-P-MAN:MAN(7)GLCNAC(2)-PP-DOL ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 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:UP000077206};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 181..210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 281..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 306..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 567 AA; 63192 MW; 04ECDDCE2F7C6152 CRC64;
MPLPTWPFYA LIPAVVLLHL FVSPYTKVEE SFNIQAIHDI LIHGIPNANA DQFFTANYDH
ISFPGSVPRT FAGALVLSGL SRPFVALMKS GEQVQLLVRG VLGLLNSVAL IAFGRSVQRA
FGTSAGVWFA LFQASQFHVI YYASRTLPNM FALVFSNLAL RSLLNTSSLP WNGYKGYRLS
LYLLTIAGIV FRSELAILVG TLTIYIFVVY RVSITGVILP AGLGGLVIGL LCTIPLDSFM
WQSFPLWPEW TAFYYNTIQG HSADWGISPW HYYFVNALPR LMLNPATYAL CIPVAVLNVA
TRQPSLDLLI PLLAFVSLYS FLPHKEWRFV IYVIPGLTAV AAGGASWIWN RRAKSFVYVI
LSLALVVSVL VSFAASTTIL ALSSLNYPGG AALDVLHHGI EHPDKPHFNV YFDNLACQTG
VTRFLESHRG AETVLDILEA QETLSKRVWT YDKTEDPSAV LDPMFWAKFD YVLVERPEKV
IGPWAVAHVE YGFGGVRILR PGETSGSQIE LSHGEGLTTT MATRWTDQIA EGWKRLEKLA
RQSVLRGYWV EVKMEPKIWI MANELPK
//
