Hsl protein, gene, vector, cell, composition and use thereof, and method for improving herbicide resistance of crops

2:

• The HSL protein as claimed in claim 1, wherein the first amino acid sequence is an amino acid sequence selected from at least one of the following:
• (1a) an amino acid sequence derived from where the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO.1;
• (1 b) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, and the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO:
• 1;
• (1c) an amino acid sequence derived from where the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO.1;
• (1d) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into alanine shown in SEQ ID NO.1;
• (1e) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into tryptophan shown in SEQ ID NO.1.

6:

• The gene as claimed in claim 5, wherein a first amino acid sequence of the HSL protein is an amino acid sequence selected from at least one of the following:
• (1a) an amino acid sequence derived from where the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO.1;
• (1 b) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, and the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO:
• 1;
• (1c) an amino acid sequence derived from where the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO.1:
• (1d) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into alanine shown in SEQ ID NO.1;
• (1e) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into tryptophan shown in SEQ ID NO.1.

16:

• The method for improving the herbicide resistance of crops as claimed in claim 15, wherein a first amino acid sequence of the HSL protein is an amino acid sequence selected from at least one of the following:
• (1a) an amino acid sequence derived from where the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO.1;
• (1 b) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, and the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO:
• 1;
• (1c) an amino acid sequence derived from where the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into phenylalanine shown in SEQ ID NO.1:
• (1d) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into alanine shown in SEQ ID NO.1;
• (1e) an amino acid sequence derived from where the phenylalanine at site 140 is mutated into histidine, the leucine at site 204 is mutated into phenylalanine, the phenylalanine at site 298 is mutated into leucine and the isoleucine at site 335 is mutated into tryptophan shown in SEQ ID NO.1.