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Database: UniProt
Entry: A0A158QRQ1_HAEPC
LinkDB: A0A158QRQ1_HAEPC
Original site: A0A158QRQ1_HAEPC 
ID   A0A158QRQ1_HAEPC        Unreviewed;      1255 AA.
AC   A0A158QRQ1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   10-MAY-2017, entry version 7.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:HPLM_0001789901-mRNA-1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Strongylida; Trichostrongyloidea; Haemonchidae; Haemonchinae;
OC   Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|WBParaSite:HPLM_0001789901-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001789901-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:HPLM_0001789901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00405920};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|SAAS:SAAS00405767}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000256|SAAS:SAAS00589955}.
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DR   WBParaSite; HPLM_0001789901-mRNA-1; HPLM_0001789901-mRNA-1; HPLM_0001789901.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000038042; Genome Assembly.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.780.10; -; 1.
DR   Gene3D; 3.90.550.10; -; 2.
DR   InterPro; IPR005873; Drp1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR001950; SUI1.
DR   Pfam; PF00535; Glycos_transf_2; 2.
DR   Pfam; PF00652; Ricin_B_lectin; 2.
DR   Pfam; PF01253; SUI1; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; SSF50370; 2.
DR   SUPFAM; SSF53448; SSF53448; 2.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   TIGRFAMs; TIGR01159; DRP1; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 2.
DR   PROSITE; PS50296; SUI1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000038042};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00484762};
KW   Glycosyltransferase {ECO:0000256|SAAS:SAAS00130854};
KW   Golgi apparatus {ECO:0000256|SAAS:SAAS00485149};
KW   Lectin {ECO:0000256|SAAS:SAAS00130858};
KW   Manganese {ECO:0000256|SAAS:SAAS00130855};
KW   Membrane {ECO:0000256|SAAS:SAAS00130924, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038042};
KW   Transferase {ECO:0000256|SAAS:SAAS00484751};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00130927,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00130919,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     93    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      530    643       Ricin B-type lectin.
FT                                {ECO:0000259|PROSITE:PS50231}.
FT   DOMAIN      722    781       SUI1. {ECO:0000259|PROSITE:PS50296}.
FT   DOMAIN     1218   1255       Ricin B-type lectin.
FT                                {ECO:0000259|PROSITE:PS50231}.
SQ   SEQUENCE   1255 AA;  142023 MW;  B1735E3212A89890 CRC64;
     MSVYLCFGVA ESTATKAFTT KSAYYRCNSS FLVIDTMFAL SADVLGNEWL PVGPRWLLPG
     LLSNLTSLTG AASRALHFMG FARFFIPRRK ENVLNALIVF AFCAGVIFYY RINDRIHLLG
     RKQSRPTKWS FEPEPVAPGT PGENGRAVIL KGEDKKQGEL DMKKWFMNVR ASDLMSLDRS
     LPDTRREECL DIHYDLKTLP QASVVIIFTD EAWSPLMRTV HSVVNRSPPQ LLKEVILLDD
     NSQREDLKEH LDEYVRRFDG LVRIVRKNVR HGLIRAKIAG AREATGDVVI FLDSHCEANV
     GWLEPLVQRI SEKRSAIICP IIDHIAAEDM SYSGDKYSTS VGGFSWALHF TWERMPEKER
     KRRQSPTEYI RSPTMAGGLL AANREYFFEV GAYDEEMDIW GGENLEISFR VWMCGGSIEF
     IPCSHVGHIF RAGHPYNMTG RGGNKDVHGT NSKRLAEVWM DEYKRLYYLH RHDLLNKDVG
     DLTSRKALRK RLGCKSFKWY LDNVIPGKFI LDEDVIAYGT LYTVVDGFRM CVDTLQRDEH
     YDHVLGVYPC QGKGSAPQLM SLSKAGHLRR ETNCAEVNFD KGHLGKIKMV HCKENSPTWQ
     YENSMLKETK YGLCLSTAGL QASDDVIVEQ CNSKSPHQKW FFVDPMAKCS MPLEYCEYSG
     MTDKCRKWSE ENAPEALEGL EISDENLEEK KHQKRGGKGT VKTVKKKVAA GGTKVTLQRE
     PRGKKSVTVI RGLASFEIDL KQASKLFAQK FACGSSVTGA DEIVIQGDVK DDLFDMIPAK
     WPQVPDYSKN RIGPGENGAP VILEGEEKLI GEQQIKTVFM NVLASDKISL DRSIPDSRSR
     ECLALSYPKH LPTASVVIIF TNEFFSSLLR TVHSVVNRTP PHLLKEIILV DDKSNRDELG
     PPLDEHLKRF GSLVTLIRST ERLGLIRAKI KGAKAATGDV IVFLDAHCEA NAGWIEPLLA
     RIQEERTAVV CPIIDSISDT NLAYLGGSHG GIGTFWWSLH YSISSMPKRE IERRKHPETD
     YIRSPTMAGG LFAVDRKYFF EIGAYDEEMD IWGGENLEIS FRVWMCGGSI ELIPCSHVGH
     IFRSGHPYDM TGRNDNKDVH GTNSKRLAEV WMDDYKRLFY VHRMGLKDLD VGDLTERKQL
     RERLKCKSFK WYLDNVIPEK FVPDENVYAY GHVRTERGLC LDTLQRLENK GTVILGVFGC
     QEGGSSAEGG FLRHKDRGLC LDVEGVEAGG DVTFTMCDEK KSSQKWSFDR YFELN
//
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