ID A0A1I1H742_9ACTN Unreviewed; 471 AA.
AC A0A1I1H742;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Dolichol-phosphate mannosyltransferase {ECO:0000313|EMBL:SFC19784.1};
GN ORFNames=SAMN05421773_102280 {ECO:0000313|EMBL:SFC19784.1};
OS Streptomyces aidingensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=910347 {ECO:0000313|EMBL:SFC19784.1, ECO:0000313|Proteomes:UP000199207};
RN [1] {ECO:0000313|EMBL:SFC19784.1, ECO:0000313|Proteomes:UP000199207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5739 {ECO:0000313|EMBL:SFC19784.1,
RC ECO:0000313|Proteomes:UP000199207};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; FOLM01000002; SFC19784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1H742; -.
DR STRING; 910347.SAMN05421773_102280; -.
DR Proteomes; UP000199207; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd06442; DPM1_like; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR007267; GtrA_DPMS_TM.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398:SF2; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43398; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF04138; GtrA; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:SFC19784.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFC19784.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..248
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 317..431
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 50171 MW; DA834D85D0CF5AAB CRC64;
MNPFPAQPTT TGPATTDSTG TDSTGTGSAA TGRDAAPAGS EDTAAGSIPP AAPGAAGAAR
TGRRTAVWPL ENVRPGSVTL IIPTFNEAGN VPELLRQLSA SVPAGLDCSV LFVDDSKDDT
PQVIAREAVH CPFPVSVLHR EVAEGGLGGA VVAGIKAADT DWVVVMDADL QHPPSLVPEL
VAAGEHSGAE LVVASRYIRG GSRAGLAGGY RIAVSRASTW LAKGLFPRRL RGVSDPMSGF
FAIRRAIVTA ETLRPLGYKI LMELTVRCRP GTVTEVPFVF QDRFAGESKS TAKEGIRFLR
HLVELRTASA TARMAVFGLI GLTGFLPNLL ALHLLTAGGL HYLPAVVIAN QCGVVWNFLL
TELLLFRHRR GHRHWADRAG RFAVLANADL VLRVPLIAVL VERMGVAVLP ATALALLTTF
VLRFAATEVL VYLPRRSRRS RRRAERAAAR QEQQEQEQQE QRTQPAPAAV V
//
