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. 2000 Dec;74(23):11240–11246. doi: 10.1128/jvi.74.23.11240-11246.2000

FIG. 1.

FIG. 1

Amino acid sequence alignment of XcGV-MMP, human Str1, and P. lividus HE using the program Clustal W. The box encloses the consensus zinc-binding motif. The P-R-C-G-(V/N)-P-D sequence, presumably involved in the cysteine switch, is underlined. A hemopexin-like motif and a proline-rich region of Str1 are underlined with double and dotted lines, respectively. White letters within black boxes indicate identical amino acid residues, and shaded boxes denote conserved substitutions. Dashes indicate gaps in the sequence. Amino acid numbers are indicated on the left. The human Str1/MMP-3 sequence and sea urchin HE accession numbers are U78045 and S12805, respectively. The protein motifs were analyzed using the PROSITE motif database.