ID A0A0G2EDM0_9EURO Unreviewed; 1157 AA.
AC A0A0G2EDM0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN ORFNames=UCRPC4_g03919 {ECO:0000313|EMBL:KKY21002.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY21002.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY21002.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY21002.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY21002.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY21002.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. 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}.
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:KKY21002.1}.
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DR EMBL; LCWF01000089; KKY21002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EDM0; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR Gene3D; 1.20.5.1430; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR036133; EB1_C_sf.
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:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 1.
DR Pfam; PF03271; EB1; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF140612; EB1 dimerisation domain-like; 1.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51230; EB1_C; 1.
DR PROSITE; PS50919; MIR; 3.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|PROSITE-ProRule:PRU00576};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 681..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..394
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 416..475
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 485..541
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 906..1007
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1064..1141
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51230"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 130107 MW; C00676DD399B9310 CRC64;
MASTVHEVDG KRTTRSSKSP RPSRNLRSEA VERKPTKKAD YGSEGVTDND ILLLPGSDYS
ILAAVTIIAA AVRIFRIYQP TSVVFDEVHF GGFASKYIKG KFFMDVHPPL AKMLIALVGW
LAGFDGDFDF KEIGKDYIEP KVPYVAMRLL PAILGVLTIP TMFLTLKAYG CRTMTAVLGA
GLLIFENALV TQSRLILLDS PLIFCTAFTA LAFTCFTNQH EQGPSRAFDP TWWFWLVMTG
LGLGATVSIK WVGLFTIAWV GSLTVLQLWV LLGDTNTVTP RLWFKHFFAR MFCLIIIPVA
FYVGMFAIHF VCLVNPGDGD GFMSSEFQAT LNSKGMQAVP ADVAFGSTVS IRHHNTQGGY
LHSHPSMYPG GSNQQQITLY PHKDDNNLWL LENQTQPVDA LNVTIPGPQA WSNLPTEWIR
DGDILKLYHT PTHRRLHSHD VRPPVTEADW QNEVSAYGYE GFEGDANDLF RVEIIRSMSD
GAVAKQRLRT IETKFKLVHV MSGCVLFSHK VKLPDWGYEQ QEVTCARGGT LPNSVWYVES
NEHPMLGEDA EKVNYRDPGF LGKFWELQQV MWTTNAGLVE SHTWDSRPPS WPVLRRGINF
WGKDHHQIYL LGNPAIWWAS TAAIAIYVFF KGLSVLRWQR GYRDYDNTNF KRFDYEIGMT
VIGWAFHYFP FFLMARQLFL HHYLPALYFA IMAMCQIYDF GANRIATLGI RNHPEIGRTI
AVLYLAFCIA VFTMYAPLIY GNKWTQNECK SVKLFETWDF DCNTFLMDYS HYAEDGLIDA
GKVQKTPKVA PAKDEKPAQQ VIQQEQKEDE GKVTPQPSLE QKIIGREQKV EYRDENGNIL
DDEQVSSLAA EGKVTFKTKY ETRTRLVDEA GKEVYDEIAP QHPDVEGQNP DTKGVPEDQA
RVAEFSVLLQ ELLAWLNSLL QLNITKVEQC GTGAAYCQVF DSIYMDVPMS RVKFNVNTEY
AYIQNFKVLQ NVFTRHGIDR MVPVESLVKC KMQDNLDFLQ FTKRYWDQYF PGHDYDAVAR
RKNAPASAAP AAGGRVSAGA GARKPGVTSA VKPRVGSAAG GAVVGGASGA AVARLKEENA
GLQEAITGLE RERDFYFSKL RDIELLIQQA IEADPEIEKD DNSILKHIQS ILYSTEEGFE
IPAEGEGELA ADEAETF
//
