ID A0A0H1BPQ5_9EURO Unreviewed; 745 AA.
AC A0A0H1BPQ5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 03-MAY-2023, entry version 27.
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=EMPG_11542 {ECO:0000313|EMBL:KLJ13519.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ13519.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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:KLJ13519.1}.
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DR EMBL; LDEV01000290; KLJ13519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1BPQ5; -.
DR STRING; 2060906.A0A0H1BPQ5; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053573; 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:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 3.
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:UP000053573};
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 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 232..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 285..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 606..627
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 674..692
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 704..723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 340..394
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 406..462
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 470..528
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 85225 MW; 5631FB25F655B7B3 CRC64;
MAAHETATAT GTSQNPDLRR RNVPGSEKDG SGVKRNSPLE LDEKRKKQAP RKSTFIDVLD
EWEFIIAPLI FTAFSFFTRM WRIGISDIVT WDEAHFGKFG SHYLKREFYF DVHPPLGKML
VGLSGYLAGY NGSFEFKSGE KYPPELNYTF MRLFNSFFGA VCVPLAYFTA RELNLRRPAV
WLITLMVLCE NSYATISRFI LLDSMLLCFT FTTTLCWARF HRLQNKSFSL EWFAWLFLTG
LSIGCVCSVK WVGFFVTALV GIYTAEDLWN KFGDLKMPKV VLAEHLAARV VGLIIIPLLV
YMFSFYLHFL ILENSGPGDA QMSSLFQANL RGTNVGKDSP LEIALGSKVT LKNMGYGGGL
LHSHVQTYPE GSTQQQVTCY HHKDTNNDWF IYPNRQEPTF DPNDPLKYVA DKDVIRIIHA
QTGRNLHSHA VSAPVTKSHN EVSCYGNTTV GDEKDHWRVE VVSDVASKDR SKIRTLTTSF
RLRHAVLGCY LRAGTVNLPQ WGFKQIETTC IKENNPRDTY THWNVESHVN ERLPPGDPGS
YKSPFLKDFI HLNVAMMTSN NALIPDPDKQ DDLASQFWQW PILHVGLRMC SWDDNVIKYF
LLGNPIVYWG GTLSLGLLGA ILAWYLIRWQ RGYDELSLAD MDHIYYSGLY PAIGWFLHYF
PFVAMARVTY VHHYYPALYF TILSLGFCMN WFTQKLPRSV EWAVYAVLYA AVIGLFVLFR
DIVFGMQGSS SKWAHLGWFS TWRIA
//
