(data stored in SCRATCH zone)

EMBL: CU928166.PE59

CU928166.PE59        Location/Qualifiers
FT   CDS             complement(132053..134317)
FT                   /locus_tag="KLTH0B01650g"
FT                   /old_locus_tag="KLTH-ORF15784"
FT                   /product="KLTH0B01650p"
FT                   /note="similar to uniprot|P42934 Saccharomyces cerevisiae
FT                   YGR199W PMT6 Transfers mannose residues from dolichyl
FT                   phosphate-D-mannose to specific serine/threonine residues
FT                   of proteins in the secretory pathway dolichyl phosphate-D-
FT                   mannose:protein O-D-mannosyltransferase"
FT                   /db_xref="EnsemblGenomes-Gn:KLTH0B01650g"
FT                   /db_xref="EnsemblGenomes-Tr:CAR21424"
FT                   /db_xref="GOA:C5DCB3"
FT                   /db_xref="InterPro:IPR003342"
FT                   /db_xref="InterPro:IPR016093"
FT                   /db_xref="InterPro:IPR027005"
FT                   /db_xref="InterPro:IPR032421"
FT                   /db_xref="InterPro:IPR036300"
FT                   /db_xref="UniProtKB/TrEMBL:C5DCB3"
FT                   /protein_id="CAR21424.1"
FT                   /translation="MSSSGFLPKSSELNLRERRKNFDGDQLSDTDDNELHEKNDEKLVE
FT                   THGAELKKRKIAKFANMGGIAAITLLSFYVRFMKIDASDIVVWDEAHFGKFGSYYIKHE
FT                   FYHDVHPPLGKMLIALSEYLAGFDGNFDFSSGDPYPNGVNFKFMRQFNATFGALCAPIM
FT                   LLSAQNLGFSTLCSYLLGLMVALELSFISLSKFILLDSMLLFFTATTFHCITEVHKLRG
FT                   KQFTKKWSLWMLLLGISIGCVCSVKWVGLFVTVIAGVYTVADLLSYHYDKNMGRLRYYK
FT                   HWFIRIIDLIVIPFMIYLFCFKIHFTILSRSGTGDAATNTLFQVNLDGNNIEVGPRDVA
FT                   YGSELTIRSHGLSPNLLHSHVQLYPLGSGQHQVTGYGHSDDNNRWVVKFSRESGLSLDN
FT                   STILDSKHLLLRDNSEIRLVHKNTQANLHSHEIPAHVSKNSYEVSGYGDEVIGDTKDDW
FT                   VVEIVEQLDSSNSSLPQEDPSVLHPISTSFRLRHKELGCYLATTGLAYPAWGFKQAEIV
FT                   CKHSWTKRDKSTWWNVEDHWNPAMEKTEGYIPPKSKFWADFVLINFAMASSNNALVPDE
FT                   DKYDSLASEAWEWPILHVGLRMCGWGHHTVKYFLMGSPFQTWLSTGSLVAFVFIILRLA
FT                   YKWRRQSVLVTSDFLSKVGMQGILPFLAWLLHYLPFVAMGRVTYVHHYVPALYFALLVL
FT                   GFVLETCVPKRFYLNYIIYALLYAGCIYIYNLFSPIAQGMQGSAIDFRYLQWFNTWNIA
FT                   L"
     MSSSGFLPKS SELNLRERRK NFDGDQLSDT DDNELHEKND EKLVETHGAE LKKRKIAKFA        60
     NMGGIAAITL LSFYVRFMKI DASDIVVWDE AHFGKFGSYY IKHEFYHDVH PPLGKMLIAL       120
     SEYLAGFDGN FDFSSGDPYP NGVNFKFMRQ FNATFGALCA PIMLLSAQNL GFSTLCSYLL       180
     GLMVALELSF ISLSKFILLD SMLLFFTATT FHCITEVHKL RGKQFTKKWS LWMLLLGISI       240
     GCVCSVKWVG LFVTVIAGVY TVADLLSYHY DKNMGRLRYY KHWFIRIIDL IVIPFMIYLF       300
     CFKIHFTILS RSGTGDAATN TLFQVNLDGN NIEVGPRDVA YGSELTIRSH GLSPNLLHSH       360
     VQLYPLGSGQ HQVTGYGHSD DNNRWVVKFS RESGLSLDNS TILDSKHLLL RDNSEIRLVH       420
     KNTQANLHSH EIPAHVSKNS YEVSGYGDEV IGDTKDDWVV EIVEQLDSSN SSLPQEDPSV       480
     LHPISTSFRL RHKELGCYLA TTGLAYPAWG FKQAEIVCKH SWTKRDKSTW WNVEDHWNPA       540
     MEKTEGYIPP KSKFWADFVL INFAMASSNN ALVPDEDKYD SLASEAWEWP ILHVGLRMCG       600
     WGHHTVKYFL MGSPFQTWLS TGSLVAFVFI ILRLAYKWRR QSVLVTSDFL SKVGMQGILP       660
     FLAWLLHYLP FVAMGRVTYV HHYVPALYFA LLVLGFVLET CVPKRFYLNY IIYALLYAGC       720
     IYIYNLFSPI AQGMQGSAID FRYLQWFNTW NIAL                                   754
//

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