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Database: UniProt
Entry: A0A0L1KQ83_9EUGL
LinkDB: A0A0L1KQ83_9EUGL
Original site: A0A0L1KQ83_9EUGL 
ID   A0A0L1KQ83_9EUGL        Unreviewed;       527 AA.
AC   A0A0L1KQ83;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN   ORFNames=XU18_3014 {ECO:0000313|EMBL:KNH06077.1};
OS   Perkinsela sp. CCAP 1560/4.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC   Ichthyobodonidae; Perkinsela.
OX   NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH06077.1, ECO:0000313|Proteomes:UP000036983};
RN   [1] {ECO:0000313|EMBL:KNH06077.1, ECO:0000313|Proteomes:UP000036983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH06077.1};
RA   Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA   Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA   Cenci U., Lukes J.;
RT   "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT   endosymbiont Perkinsela sp. CCAP 1560/4.";
RL   Submitted (JUN-2015) 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}.
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:KNH06077.1}.
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DR   EMBL; LFNC01000191; KNH06077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L1KQ83; -.
DR   EnsemblProtists; KNH06077; KNH06077; XU18_3014.
DR   OrthoDB; 122000at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000036983; 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   ECO:0000313|EMBL:KNH06077.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036983};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNH06077.1};
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        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        200..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        236..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        367..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
SQ   SEQUENCE   527 AA;  60956 MW;  8DC921CA934D8844 CRC64;
     MLRISYRLHF SYDYMTTWLS SSGWLPLLSG IMAFLVMCWS IRLCPFTKVE ESFYIQAAHD
     FLYTTFDGSW DHIEFPGVVP RSFAGPAVLS TLVAPAVYFY EYWLGGCSEN TCPFQTKAHA
     QYLVRMTQAV VFLACNRFYA RALWKYTTES PTRTLFIYEL LSYSSFHIIF YGGRLLSNTF
     SLSGCLVGYG LWLRGQKRKA LFLLGLTAAI LRMDTLLVLA VFFSPKVFWV SKKTRLFLLT
     ELFLIIAVVS SFDGYVWRAN TLVIAELESM KYNVFEGKAT LWGTLPFYWY FAIALPKIFT
     AKLPLMAYAF FKEPCFRKNT IRAIVFVILY SFLPHKELRF IFPVIPIFHA HIALAISKYA
     NQRNKRVSFL CAFIILISVF HTVTAHIISS NNYPGGEFMT NFVLKSELSP NQEPRLIHYN
     CPRLKVLLDV YPCMTGITRF LELRQPNDIV FVKRRECQSI AEAVRAFLPN RFTHLLIETP
     TLPASSEMVF EDQKFQFDQA FECFDHVDWR KIRAVNRPVA ALYGNSL
//
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