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Database: UniProt
Entry: E5A158_LEPMJ
LinkDB: E5A158_LEPMJ
Original site: E5A158_LEPMJ 
ID   E5A158_LEPMJ            Unreviewed;      1763 AA.
AC   E5A158;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBX97514.1};
GN   ORFNames=LEMA_P106450.1 {ECO:0000313|EMBL:CBX97514.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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; FP929131; CBX97514.1; -; Genomic_DNA.
DR   RefSeq; XP_003840993.1; XM_003840945.1.
DR   STRING; 985895.E5A158; -.
DR   CAZy; GT57; Glycosyltransferase Family 57.
DR   EnsemblFungi; CBX97514; CBX97514; LEMA_P106450.1.
DR   GeneID; 13280882; -.
DR   eggNOG; KOG1245; Eukaryota.
DR   eggNOG; KOG2576; Eukaryota.
DR   HOGENOM; CLU_002631_0_0_1; -.
DR   InParanoid; E5A158; -.
DR   OMA; SSTEWAY; -.
DR   OrthoDB; 5488939at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
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; 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:UP000002668};
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        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        413..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        481..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          693..804
FT                   /note="WAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51136"
FT   DOMAIN          1163..1226
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   REGION          587..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          978..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1427..1486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1678..1763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1388..1422
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        592..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1089..1110
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1236..1251
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1459..1486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1678..1721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1731..1750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1763 AA;  199803 MW;  5418EC3C6BB211DE CRC64;
     MPELFPSIAQ CAIVATALKV LLFPAYKSTD FEVHRNWLAL THSLPVNQWY YEKTSEWTLD
     YPPFFAYFEW LLSQAAAHVD AAMLQVEALG YDSWQTVYFQ RATVILTELL LVYALHLHVK
     TSKSKSTSHA AALSILLSPG LLIIDHVHFQ YNGFMYGMLV LSIVLARNNS TQLLSGLLFA
     LLLCFKHIYM YIAPAYFVYL LRAYCLGLRS SFPYFNIRFL NCIKLGVGII AVLAAAFGPF
     AQWGQLDQVF RRLFPFSRGL THAYWAPNVW ALYSFSDRVL IHLAPRLGLA VNYEAVNSVT
     RGLVGDSTFA VLPDIVPLTC FVLTLGAQIP VLLRLLFKPT WETFVGAVTL CGYASFLFGW
     HVHEKAILLV IIPFSLIALH DRRYLSAFRP LAVAGHVSLF PLLFTAAEFP VKTVYTIFWL
     VLFLLVFDRL VPASPKPRIF LLDRFSLLYI ALSIPLIAYC SLIHAIVFGP RFEFIPLMFT
     SSYSAIGVVG SWIGFLVVYF ELVSQYRPVH RKGQCVVARR VGQTVQGFAQ GDSQQSMLPD
     VTPAFDIAMP CWPTTLQDYL SAGFSLHVAL LYSCPLLYCP PPPPPQFESP EIHHQPTRRA
     FGTERRVSEP HSDSQGCDDF SIEVDWARIR SSCLPLAPHR GAIAPEHSFW ESGVVISDAL
     VATRHLSIVG DAVFYKRKPV KLLPEPKGLD DSTEVWVMQG TGEVFVDYEA YLIRRDYYLQ
     ANVFYMRSDW HVEPDLLRGQ GEREEQTEAV KEINEIFPKP LRKPVLGFVQ FRTETRMDDL
     VNAVYDHFKE EFFQDEVVTV EDGNNVRRRG VVTGFTDNNQ VHTMYHGQML TNAGYVGYII
     TMDDTKETVI KHKGADLQRD KKTYSKLILK QYLRATIKRD SWIGAPWMVK STLAKLYNIP
     TKAPDHRKTQ AAIAAQRQAM IDNVNGNGPP APPQSQQQAP NGHQPYQNGH HGPLPSPSQI
     QPGFHSFVAN GQHAYAQQQL PPPPLQQQQQ QHQQQQQQQH QHQHQQGHNQ SLVQFSRPPP
     YLQHPVSVHP MWNSGPLPYQ VHSAPPPFGF NHPPPQITGP LPPHLVHVLG MQHGGPALPI
     NVGYQTSFPH HPPQPPPQAP GPQPVQQLPQ PARPFVPAIK FPCEDLDIKD VGKTGVRPTL
     KFFSDDGPDG YQRPDDEKTG ILMKSIGPLL GAWETLNVHD TIYMLDSFTY DDFVDAMGFS
     SEETECELFV EVHCSVLKQI VNESGKIQAA LPNMTEAEDS EEEDSDQESS PEPEPEPPAR
     TTRSSLRRSE AQQLAVKPRT PTPEPPKDLH NASEFVEDFD WIEICKVRNF RHGNWQAIVV
     ALLYRFSFDP LLKEACDEIL AQLVPADEEN TVESIAAKYT NLDVNLRISA LDILLRMTVT
     TEAFRDQLIA AAQEMTRLRK EKIDYQRKRK EIEADIARME LDRKILLPEN TPASPPEAKE
     NDSMDVSMTS AADDSTLGNA DEEAAKGKMR PINKNKRKAA AEEARKEKAK KAKAAAELLK
     KQKEWEKLLT DIQKKRAELA ECEANICELD DDLRETLVHR SKVLGKDRFL NKYYWFEHNG
     MPFGGIPNSS TAEYGYANGR IWVQGPDKHE FQPNLEEPAL SQDKERLGFT IPERKAKEEG
     ETHLSSSTEW AYYDDPADID ALLAWLDERG LRERSLKKEI LLYKDHILTY MGKMREHLNK
     RTNKEKTKDE DAMSDIEDKP RISTRKKAAS ADKEKDSDGP RCLRWTNSMM REEYGHVHHD
     EYEPPRKTKA KATAKSSKSK GRR
//
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