ID A0A421DEL3_9EURO Unreviewed; 1465 AA.
AC A0A421DEL3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CFD26_106897 {ECO:0000313|EMBL:RLM00544.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLM00544.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLM00544.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM00544.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00475}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008715}.
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:RLM00544.1}.
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DR EMBL; NIDN02000014; RLM00544.1; -; Genomic_DNA.
DR STRING; 1245748.A0A421DEL3; -.
DR OrthoDB; 332390at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-ARBA.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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:0031509; P:subtelomeric heterochromatin formation; IEA:TreeGrafter.
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; 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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000215289};
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 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 486..594
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 851..914
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT REGION 761..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1086..1120
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 798..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..944
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1138
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1465 AA; 169740 MW; 0549E6FDB5D77870 CRC64;
MADIYPSLAQ CAIVATAFKI LLFPAYKSTD FEVHRNWLAI THSLPVKEWY YEKTSEWTLD
YPPFFAAFEW LLSQAARYVD PAMLVVENLK YDSWQTVYFQ RATVILTELV LLYALNRFIK
SAPQANKHLA HIASLSIFLS PGLLIIDHIH FQYNGFLYGV LVLSIVLARK QSTLLYSGIL
FAVLLCLKHI YLYLSLAYFV YLLRAYCLDP KSVFRPRFGN ILKLGLSVIG VFGIAFGPFA
HWNQLLQLKD RLFPFSRGLC HAYWAPNIWA MYSFADRVLI PLAPRLGLPI NHEALTSVTR
GLVGDTSFAV LPEITKEQTF ALTFLFQLLP LIKLWLRPDW DTFVGAITLC GYASFLFGWH
VHEKAVLLII IPFSLIALKD RRYFSAFRPL AVAGHVSLFP LLFTAAEFPL KTVYTVWWLV
LFLFVFDQVA PVSERPRIFV FDRLSLLYLT VAIPLIIYCS LAHHLIFGWD RYEFLPLMFM
SSYSALGVWV IPETNEVFTN YEPYLQRMDF YKQKRFICEI TGHSGLTFFE ALRSEMEESR
EVNSAFPDAL KEPILRRIQF STVSRVDSLV DEIYEEFKQD FYPGEPVLIL LEDNTRLHGM
IRDKANFAEQ RYPDGTLKTP AYATYLVKVL DRPNEEALLD QDHITRDRKT FTKQMLRAFI
KNNVTRESWN GAPWLVKPSI AEEYKIPTEV PKHLQYGARV AEKKAQKKAD QEGFFGFFSS
QQLPELKPAA KGQKTKLSPQ DLARSKEAQY LEYQRSLNGD PTFVVSHKTS NAPSRPIKPQ
EEKKPQPVPT VIVKTEPPKP PTPPPIKYPI EDLEIPPDRE KKKQRPPLKF LTVDENDDPD
DEELLHDKIE MQSVGLLLET WNTLNVYCEV FQLDSFTFDD FLQAMRFSSD EVECELFAEI
HCAVLKKLVN AENDDDGAVQ VSLPDLPDAE SDDSEAEEED EEEKEPSPEP EPVVTRMTTR
SSLAKAEAEN LKAQANRSRA NSEEIKVHRA AEVFGDYGWI ERLRKRDFRN GGWEMVMVGL
LHQLSARPRM AKVCNDILKH LAPLDAEPTQ ETVQSQYATL NINLRVQALE IICMLSLETK
AIRNYLEECS NQMTEFRKEK IEYQRARKVA LEELRRLHQE RKALQPEQEQ SPSPVPELEA
LDDSKMTGAD GDSEQVMDTE DDDTPQQRSL RGGLDRILER KRKQEEERER KEQLAKQPKG
SKQYQRVLKK IEDQKATVEK LEKKIEVVDN DLREADCPRT RCLGKDRFCN RYWWFERNAM
PYGGMPNSST AEAHYANGRL WVQGPDEMER VGFIDVPDDQ RKQYQKEFHT TPAERKKNEE
GPTRLSAAHE WGYYDDPDAI DKLIEWLDSR GNRESRLLKE LQLQRDHIVK YMKCRKDYLE
QTAERAESEE PTKRMTTRNK TYVDDHKHRC LKWRNTTALS ENGHLHIDAS RPSKRAKRVT
DEPKEIKTTN RQGRPLTRQG TRYNF
//
