ID A0A177WSH3_BATDL Unreviewed; 792 AA.
AC A0A177WSH3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
GN ORFNames=BDEG_25770 {ECO:0000313|EMBL:OAJ42301.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ42301.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ42301.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ42301.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ42301.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ42301.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00034032,
CC ECO:0000256|RuleBase:RU367007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00033990,
CC ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367007}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222, ECO:0000256|RuleBase:RU367007}.
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DR EMBL; DS022307; OAJ42301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177WSH3; -.
DR STRING; 403673.A0A177WSH3; -.
DR VEuPathDB; FungiDB:BDEG_25770; -.
DR eggNOG; KOG3359; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000077115; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 2.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000077115};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 610..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 648..666
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 678..701
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 743..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 325..385
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 407..465
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 90660 MW; 039D5D2D0A5C2AC2 CRC64;
MTDIRHRKKG SVADPDESAT SIGLFPTDKK RFDSDHLRAA TLDNLNPIGK AISSDLYLAV
DQSGNELVSN FALFFVTALA VLTRTWMLHY PGEVVFDEVH FGKFASYYLR REYFFDVHPP
LGKMLLAGVG YIVGYDGHFL FDHIGDNYAE NNVPYLALRL WCALCGAAVV PISYMTLREI
GVSVMGAALG ALLLVFDNAL ITQSRLILLD SMLMLFCTMC IYFWVKFYKQ RHKVKMVGLF
TMGAIGIATL FDLWEILDID RGVTMRKVIK HFAARTLCLI IVPFGLYLLP FYIHFSILTK
SGPGDAFMSM RFQEGLTNNN NTAGAIAVMY GANITLVHGS TNHYLHSHYH NYPLRYDDDR
VSSQGQQVNA YAHSDVNSLW NMVPVDPDLY SLAKKYVPTK KEEERDIRYV RHNDIVRMYH
VSTKAYLITH DVASPMTTTN MEMTVVRDAE SERRYNETLW RVAIEDADPG DKLKSKKFLV
KLINVIHNVA LMTNKGALPD WGFKMQQTNG NKNIKDKSNI WRVDKVEHER IVNGTELGEE
TQKEKSGKPP LSFMAKFIEL QVQMVAHNSK LTKPHPYSSP PSHWPFVVRG ISFWEKKDGI
RQIYLIGNPI VWWLSIASVL FYVILWVVDR ICLRRGIDDF GHSARRWWDR AIGFLIIAWA
MHWLPFFLMG RMLFLHHYLP AFIFSTMVFA AMFDFILRVA FSGSYIPIRS TSDGGDDKII
KSATKKQEKL TSIWFAQAAT PGMVYYILAL VIFCAFGYVF WDFSPFCYGS GFPSVEILRA
HKWMTSWDLQ YA
//
