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Database: UniProt
Entry: A0A3N4Z449_9MICO
LinkDB: A0A3N4Z449_9MICO
Original site: A0A3N4Z449_9MICO 
ID   A0A3N4Z449_9MICO        Unreviewed;       393 AA.
AC   A0A3N4Z449;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Dolichol-phosphate mannosyltransferase {ECO:0000313|EMBL:RPF19962.1};
GN   ORFNames=EDD34_0536 {ECO:0000313|EMBL:RPF19962.1};
OS   Myceligenerans xiligouense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Myceligenerans.
OX   NCBI_TaxID=253184 {ECO:0000313|EMBL:RPF19962.1, ECO:0000313|Proteomes:UP000280501};
RN   [1] {ECO:0000313|EMBL:RPF19962.1, ECO:0000313|Proteomes:UP000280501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15700 {ECO:0000313|EMBL:RPF19962.1,
RC   ECO:0000313|Proteomes:UP000280501};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (NOV-2018) 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:RPF19962.1}.
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DR   EMBL; RKQZ01000001; RPF19962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4Z449; -.
DR   OrthoDB; 9810303at2; -.
DR   Proteomes; UP000280501; 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   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:RPF19962.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280501};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RPF19962.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..176
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          242..359
FT                   /note="GtrA/DPMS transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04138"
FT   REGION          369..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   393 AA;  42589 MW;  F467A853AD3AAB37 CRC64;
     MAITVVVPTF NEGPNVAELV RRLDEALGAM PGSCVLFVDD SRDDTPSVIE RVAAGQAARG
     GIPVRMIHRE VADGGLSGAV VAGLRSVETE WAVVMDGDLQ HPPELAPVLA TRGRDAGLDV
     VVASRYIGGG DAGGLDGYWR RAVSTVSALL ARSMFPLRLR NVTDPLTGFF AVRVGAIDLD
     TLRPRGFKIL LEVLARGKRV LAVGEEPFVF GERYAGRSKA TLRMGLRYLE QLASLRFGRM
     SRFAIIGGMG AVWNVLILWA LTAFGMHYVI AAVIAAVVTM SVNFALQERF VFRDLRAEGR
     HGFWSRLAHS FAFNGTEAAV RLPVLWWIVE VTGMWPVLVQ AVTLVVAFLL RFVFHAQVVY
     RPRRTQPPLG GALSSSQPGD GLLGASSADK RVQ
//
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