ID A0A2P7YRI3_9ASCO Unreviewed; 1764 AA.
AC A0A2P7YRI3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN ORFNames=C7M61_002510 {ECO:0000313|EMBL:PSK38576.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK38576.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK38576.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK38576.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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:PSK38576.1}.
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DR EMBL; PYFQ01000005; PSK38576.1; -; Genomic_DNA.
DR STRING; 418784.A0A2P7YRI3; -.
DR EnsemblFungi; C7M61_002510_t1; PSK38576.1; C7M61_002510.
DR VEuPathDB; FungiDB:C7M61_002510; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000241107; 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-EC.
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; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 2.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
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 1056..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1101..1123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1170..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1195..1215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1227..1244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1250..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1282..1303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1602..1626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1647..1665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1677..1696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1717..1735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1335..1401
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 1407..1465
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 494..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 732..787
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 822..856
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 494..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1764 AA; 201698 MW; F656C006495A8B85 CRC64;
MSGSSRSLLR NIASVFENWS NNKNWDKAPS QDIKDLNDSI YAYKEKHNLL SSLSSQLNNE
LRSIHSKYID ESLEISKEVL FLDILTRLLP VLSADEIKVW LSTYLLPAIE STGFDISFVS
KAREFVRLVL AETYPTDDPQ LRNRRAAIAR MVLGYILRIY LGTDQEAYGL IGLKYKDASS
KDEDTHENIE KVRFMETNCA ITLREYGQRY SEDYFSLLNT YFHLVDNRLK TLSLITSFVA
SNTFHSKAII KTPLFKSILV CLLNDQSETI IACALSLMVM LMGKLCDKIA TYLPDLLVIY
TRLLLWLGPT KEGNSKEMTP KAHVEKEEWI IAEPDLEMVA MSSHLYHNDE FNLLYYTTLL
YAFFPMNFMR FGRSPFQFWS EYRPKVLSEK RYHDYPDILQ IISSRTKEFC EQMRLHPNFL
QQVSAEEELD SPLKWILKDN EGVDISEDDI MLRSLRLNPT YMLWLPDRFV LPKYFYEKLE
ELLIISPAAS SNLGPQFSKD TRSGSHWSAN VSSNKSSKRG SVDVALDDML TPRRSSLVPS
SLLSDKSPNE PRIKFKNVDY SLSKSGPGTA SPKPSQNDSF TASETDSGVL DLFSAHEKLY
KMSTTRRNSV QQDLQNPQVA TGNFQATSKS ASALLNQQLK GKNNEEVSSS KGGALEFYQR
ELLLCKNELE FTIYMKYLNK LNYIKLKTQM SELSRKLAEA ITSSPSEQLK TKNNENLRSS
LEELQSSSKA ALMHSQAEIA KLSERVVDLQ KSLEAVTVAL TQSRDENEVL QNDYDTCKQS
VELIEAELRG LKIKQTADAN ESATPPITRE FTHTPETSSP FITEHEEELQ NLRTELEMAR
SQNHTIQREI RDLEEKLDLT VRGYEKQVAS LKLDLGGAVR EQVRHYERRI QELNTTIMKY
ATSIEEKNNM IVQLSTSKPI KIPGGRDMQE SESSPVKPRN IPVPSRQSRN LEYGIPDQRT
SRNMQDFFET RSSSGSLMRS SASAQLVQPS TRPQAVYRLP TTLSIPIIKG RGGYQKRSKR
KKTGSVTPTQ AETVAASIEN DEKTTLISTR KESDNVYWIA MAVLTAAAAA VRFTLLSHPA
KVVFDEVHFG KFASYYLERT YFFDLHPPFA KLLIAFAGWL VGYDGAFKFE NIGDNYVENN
VPYLAYRSLL AVQGTLVVPV IFLTMKTLGF TVSACILSSA LVLFDNAHII DSRLILLDAT
LILSVALTMF TYCKFSTYRR QPFTKWWWIW LLSTGVALSC VISTKYVGVF TYFTIGIAVV
HELWILLDIK KGLTLEEFAQ HFLARFFSLI VFPFTIYLFW FYLHFAILTK SGPGDAFMSS
DFQETLEESP LAKYSKAVHY HDILTVEHKE TEAFLHSHNL TYPLRYENGR ISSNLQQVTC
VYDQEGQEIK DVNSQWEIIP TKEVGNNQAV YTNDVVRFRH IGTGGYLLTH DVASPLLSTN
EEFVVVHNDV AEKRYNETLF RLRYAEANNK NKRALVKTKA TPLRVVHVDT VVAMWTHDDE
VLPDWALEHQ EVSGNKKVQD KDNTWTFDTI VNLKEEDPRN HFTPKKVKTM PFLKKWWELQ
GLMFVHNNKL SSEHPFASQP DAWPLAVSGV SFWNDNENRR QIFFIGNVIG FWVQVGFLAV
YVGFVLADLV TQRRAHEIIT PQARSRLYNT LGFLFIGWAA HYFPFYLMGR QKFLHHYLPA
HLIAALFTGG AVEFLCTNKT AHNKKGMPPA AIDKVRLIGA TVTVVIGTAW FLWYMRAMTY
GHFAMAAEEV KKRQWLDIKF HYAK
//
