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Database: UniProt
Entry: A0A0M9ZM54_9ACTN
LinkDB: A0A0M9ZM54_9ACTN
Original site: A0A0M9ZM54_9ACTN 
ID   A0A0M9ZM54_9ACTN        Unreviewed;       418 AA.
AC   A0A0M9ZM54;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dolichol-phosphate mannosyltransferase {ECO:0000313|EMBL:KOV63872.1};
GN   ORFNames=ADL01_28230 {ECO:0000313|EMBL:KOV63872.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV63872.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV63872.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV63872.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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}.
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:KOV63872.1}.
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DR   EMBL; LGDW01000426; KOV63872.1; -; Genomic_DNA.
DR   RefSeq; WP_053744795.1; NZ_LGDW01000426.1.
DR   AlphaFoldDB; A0A0M9ZM54; -.
DR   PATRIC; fig|1519490.3.peg.6161; -.
DR   OrthoDB; 9810303at2; -.
DR   Proteomes; UP000037738; 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:KOV63872.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOV63872.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        272..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        365..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..203
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          275..389
FT                   /note="GtrA/DPMS transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04138"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  44409 MW;  1B0A1C728BDA7431 CRC64;
     MTVSGTGAEE TEEQDHAAPD GAPDDAGPSA RTTVTVIIPT FNEAGNVEEL LTRLAAALPA
     HLDCAALFVD DSTDDTPAAI ERAALTCLFP VNVIHREVAT GGLSGAVVEG LKAAASEWIV
     VMDADLQHPP SLMPELVETG RRADADLVVA SRYAGGGSHA GLSGRYRVAV SRASTLVTKG
     LFPSALRGIS DPMSGFFAIR RSTVHAHADI LKPLGYKILL ELAIRCRPRV VAEVPFSFQE
     RFAGESKSTV REGMRFLAHL VSLRTATPVA RMVVFGLIGL TGFLPNLGAL AALTATGLHY
     LPAEVLANQF GVLWNFLFID LLLFRDRRGH RHWADRLGRF ALLANADLVL RIPLIALIVD
     GMGMAVLPAT ALALLTTFVI RFAATELLIY LPGRGGRAKE AGADASLASG KREKEGTP
//
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