ID A0A0D1X584_9EURO Unreviewed; 1700 AA.
AC A0A0D1X584;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase {ECO:0000313|EMBL:KIV82851.1};
GN ORFNames=PV11_04921 {ECO:0000313|EMBL:KIV82851.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV82851.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV82851.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV82851.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}. Nucleus {ECO:0000256|PROSITE-
CC ProRule:PRU00475}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008715}.
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DR EMBL; KN846952; KIV82851.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1X584; -.
DR HOGENOM; CLU_002631_2_0_1; -.
DR OrthoDB; 1382023at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR PANTHER; PTHR32075; ISWI CHROMATIN-REMODELING COMPLEX SUBUNIT YPL216W-RELATED; 1.
DR PANTHER; PTHR32075:SF6; ISWI CHROMATIN-REMODELING COMPLEX SUBUNIT YPL216W-RELATED; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIV82851.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 204..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 695..803
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 1088..1151
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1322..1353
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 946..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1700 AA; 194497 MW; C5A46895A7BA241C CRC64;
MAAVVSVTTN RFRDKTPITP EQRPAKSTKQ PGSDQWPSLF QTAVVATALK VLMFPAYKST
DFEVHRNWLA ITHSLPVKQW YYEATSEWTL DYPPAFAVFE WLLSQPASLI DSAMLQVKNL
NYDSWATVSF QRGSVIATEL LLVYALHKYT ETSPLSTRRQ SHAVALSILL SPGLLIIDHI
HFQYNGFLYG VLLLSIVLAR KESTMLYSGI LFAVLLCLKH IYLYLAPAYF VYLLRVYCLQ
PKNMLQPRFA NITKLGISIV GIFAAAFGPF AAWGQLEQLK SRLFPFARGL CHAYWAPNVW
AVYSFIDRLL IIAAPYLRLD IDQSAVNSVT RGLVGDTSFA ALPDISARTC FALTLSFQII
ALTKLWLVPT WDAFVGAITL CGYASFLFGW HVHEKAILLV IIPFSLLAVK DRSHLASFRP
LAVAGHVSLF PLLFTAAEFP IKVAYTISWL IIFLYAFDQL APAPSRRRFF LLDRFGVLYI
AISIPLMAYC SLLHGMVFGD RYEFLPLMFI STYSAIGVLG SWLGFMVLNR SANGFYDATS
KCLRRVWRAM YRRDARHFYH GYGKHCREWN KIDHKVLWVP LTPLILMLPT SSTSASIISP
VQILTLPYKT TRGIIRLHPA SIAHSGTPTG SSPHTKSYYA VAVSLNPSRT LPLLPPSQTR
DSPQGSLDRS LARMVLFKRK PVRYLPHPYI DDQECDVWVI SESNEVFTSY DAYLERMDFF
KSKKFTCEVT GRSGLNFFDA LRSEQAGSRE IDEAFPQALR EPVLRRVQFS TTSRVDNLVE
EVFNEFKNDF YPGELVTVIL DDSSRLNGRV RDKAKFAEIR RPDGVVARNA FSRYFVRLID
RPDEEALVDD QHIARDRKIF TKQMLRSFIK NAVTREGWIG APWLVKPEIA ERFRIDTNVP
PHLQYSSKVA AKKAEKKHAS VEQQQDGMFG IWQPHRLPDL QPALKSRKGQ QHQQQQPAQM
DSPMGMYPDY PHMHVMPDPG LLPRSWDYMQ PPPPPPPGYD SYYQGYPNQH MPPNGHYYPP
QAPPQPVPQK QVAVEIPPTP PPPIKYPIDD LDVEPVRDGT HRPALKFVAE EQCLDDKSVD
DVIPGLREET VGLLLEIWNT LNVYCQVLKL DSFTFDDFVE AMLFSSVEAD CELLIEVHCA
VLKQLVHSEH NNEGAIQISL PDLPHSDDEE EESEEEESKL PTPTPEPEYP AKRTRSSLNK
VKFADEQPEP VKEEEVDTVP HRAAEMLGEY SWIDRLRKRD LIDGGWELVM VGLLHQLAGR
DRLTDRCNRI LRHLAPLDAE PTIETARIQY ATMDINLRAD ALQMICQLFL ETKTVKDFLE
EMSNTMTQYR KLKIEHQRAR KEALTKLKEL QVERRVLAPE PEKSPTPVPE LEEAMEAEKA
EEGDISIPDS EDEELMVTRS LRRGNDRAAE RKRKREQEQE RREKAAEAKQ NKGSKEYQKV
LKQIEKEREK VQAAEDAILV VDNDLREADC PRTRVLGKDR FCNRYWWFER NAMPHGGLPD
SSTAKAEYAN GRLWVQGPDD MEREGFIELS EPDKNAYYRR FQMTPAERKA MEEGPTTLMK
AKQWGFYDTA EELDMLIGWL DSRGYRELKL QKELTMQRDV IIKHMEKRAA YLAPREESEE
PPTRMSTRTK THLSDKTHRC LRWRNTSAIA ELGHRHVDPP PKPRPRGKKN ASLEETKSSG
PPALNRQGKP ATRQGARYNF
//
