COLL5_MIMIV
ID COLL5_MIMIV Reviewed; 812 AA.
AC Q5UPS6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 29-SEP-2021, entry version 57.
DE RecName: Full=Collagen-like protein 5;
GN OrderedLocusNames=MIMI_R241;
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 -!- FUNCTION: May participate in the formation of a layer of cross-linked
CC glycosylated fibrils at the viral surface thus giving it a hairy-like
CC appearance. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Virion.
CC -!- PTM: May be hydroxylated on lysine by the viral-encoded procollagen-
CC lysine,2-oxoglutarate 5-dioxygenase. {ECO:0000305}.
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DR EMBL; AY653733; AAV50514.1; -; Genomic_DNA.
DR RefSeq; YP_003986737.1; NC_014649.1.
DR GeneID; 9924848; -.
DR KEGG; vg:9924848; -.
DR Proteomes; UP000001134; Genome.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 2.
PE 4: Predicted;
KW Collagen; Glycoprotein; Hydroxylation; Reference proteome; Repeat; Virion.
FT CHAIN 1..812
FT /note="Collagen-like protein 5"
FT /id="PRO_0000059420"
FT DOMAIN 69..128
FT /note="Collagen-like 1"
FT DOMAIN 143..502
FT /note="Collagen-like 2"
FT DOMAIN 506..565
FT /note="Collagen-like 3"
FT REGION 71..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 812 AA; 78147 MW; 52CB0CB9034270DE CRC64;
MNYQYTNYCC QSNITLPNSL TCTNAKIYVD VGRPNNCLGN DGDLYLDTNT NNLYYKIDGV
WTLVSNLRGA SGAQGVKGDP GSNGSKGTKG EKGDKGDKGS KGDNGEKGEK GDAGLNGLDG
SKGDKGDDGS KGSKGNKGDA IKGEKGDKGE IGDKGDKGED GLKGVKGDVG DKGDKGDKGD
LGLKGVKGDK GITGDKGDKG EIGEKGNKGD KGDVGVKGDD GTKGEKGEKG TKGDKGNKGD
KGEDGLKGEN GDIGDKGDKG SKGEDGLKGD KGDIGDKGDK GSKGEDGLKG SKGDKGEIGN
KGDKGDKGDI GIKGDKGDIG DKGDKGDPGL KGEKGEKGDK GDIGDKGETG SKGSKGDKGD
KGDKGDVGDK GSKGDKGDIG EKGDKGSKGD KGDKGDKGDK GDLGDKGDKG DKGETGEKGS
KGDKGDKGDK GETGSKGDVG LKGSKGDKGD KGIKGDVGDK GDIGITGDKG DKGVKGDKGD
IGLKGDKGDK GTKGDKGSKG DNGSKGETGA KGDKGDKGDK GIKGDTGTKG VKGDKGSKGD
KGDLGDTGIK GDKGEKGDPG IKGEAGTNSP FIGTFIDNVP GSGTTIVPFG AIFAYLSAAG
GGGGGGGISD GNGSPGGGAA GTVYLYPLTV TSGLVVNYTI GSGGTAGTPV AAGGAGGNTT
ITIGTLNFTL NGGGGGGIGG TVGAINGGAG GSVTTPLGTT PGGSGGVGNG GPLPGNGQVG
LFAFSGAGGG QARTNGASTG GFPGGQTDSN TFGGGGGGAS GFAKGGDGEQ EIPTTIPAQS
GTLGSGGGGP TDVSASGGRG GDGFVRLDYY SA