ID   YR659_MIMIV             Reviewed;         525 AA.
AC   Q5UR16;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   23-FEB-2022, entry version 54.
DE   RecName: Full=Putative EGF-like domain-containing protein R659;
DE   Flags: Precursor;
GN   OrderedLocusNames=MIMI_R659;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
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: Secreted {ECO:0000305}.
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DR   EMBL; AY653733; AAV50920.1; -; Genomic_DNA.
DR   RefSeq; YP_003987180.1; NC_014649.1.
DR   SMR; Q5UR16; -.
DR   GeneID; 9925304; -.
DR   KEGG; vg:9925304; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PROSITE; PS01186; EGF_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..525
FT                   /note="Putative EGF-like domain-containing protein R659"
FT                   /id="PRO_0000247410"
FT   DOMAIN          317..359
FT                   /note="EGF-like"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        411
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        321..330
FT                   /evidence="ECO:0000250"
FT   DISULFID        324..345
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  57973 MW;  1BA669B8C0816696 CRC64;
     MGNKWCGIFL TILLLAQMSQ TIFGQNPNIP ADDHHGAVPP ELVMSAVVLK DGRIANYYIN
     ATVIETEFNN NPCPCVNQTE LKAERLKVLK LWSAYTNYDQ QYILDSYEQF ATPDTLPDGT
     VNQFLHQFVV NGYATYSANS VAAEYALQAN DANIHLFSEL DPVSVEWQAD NITVIYKIIT
     NYTLPGLPGA PILDGFVNTH YVKFVPCKAE IWIDIMTQDS LVSTYLAAAQ SNHPASDICD
     KIQQACTGPN QVYDSYESCL NYMSVVVNHT SFCPTGSLIA NSSGCHYFHA SSALNYPEIH
     CQHVRPYDSP TCQDFCLTQG CGNCDSNAEC VFVSGSNSIV PKYQCKCKSG YVGNGTHCSP
     VTCSAQWQCP SEYNYGSCQN GLCGCNSGNG FKWVPDQATV NSHQACQCSE NETVQWYNGV
     PECMPIGRCR YVWQCPQAAT QYTSITCTKY GQNALVPFNT CLCNYGYDNL GFSYKCQCSV
     PKREIWSNVR QGTLCLAPNE CTDNYHCASN NCQVQPGQWL GTCAA