ID YL288_MIMIV Reviewed; 204 AA.
AC Q5UPX2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Putative B-type lectin protein L288;
GN OrderedLocusNames=MIMI_L288;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC Mimivirus bradfordmassiliense.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AY653733; AAV50560.1; -; Genomic_DNA.
DR RefSeq; YP_003986790.1; NC_014649.1.
DR SMR; Q5UPX2; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR GeneID; 9924903; -.
DR KEGG; vg:9924903; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond; Glycoprotein; Lectin; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..204
FT /note="Putative B-type lectin protein L288"
FT /id="PRO_0000071259"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 52..200
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 69..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 118..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 171..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 204 AA; 22170 MW; 6B7367A3DB6D0421 CRC64;
MSKTTFIIIA VIIILLLLAL LGFLFYWRHR YRHTPTPPSS GPPVTPATPA SITKAMQSGW
GTIENQGNCL TATSNPGANT SIELQTCINP SSDNSSQQWK MTGNNSFISK LDPNGTYCLD
VDGTASVGSS DQIHFWQCQQ QDTTKMGWTP KITTNNPLNY QLVNNKTTSA CLDASPGINK
QPILQTCGAN TTASQQWVFK PISS
//
