<?xml version="1.0" encoding="utf-8"?>
<journal>
<title>Iranian Journal of Fisheries Sciences</title>
<title_fa>مجله علوم شیلاتی ایران</title_fa>
<short_title>IJFS</short_title>
<subject>Agriculture</subject>
<web_url>http://jifro.ir</web_url>
<journal_hbi_system_id>1</journal_hbi_system_id>
<journal_hbi_system_user>admin</journal_hbi_system_user>
<journal_id_issn>1562-2916</journal_id_issn>
<journal_id_issn_online>2322-5696</journal_id_issn_online>
<journal_id_pii></journal_id_pii>
<journal_id_doi>10.18869/acadpub.ijfs</journal_id_doi>
<journal_id_iranmedex></journal_id_iranmedex>
<journal_id_magiran></journal_id_magiran>
<journal_id_sid></journal_id_sid>
<journal_id_nlai></journal_id_nlai>
<journal_id_science></journal_id_science>
<language>en</language>
<pubdate>
	<type>jalali</type>
	<year>1403</year>
	<month>5</month>
	<day>1</day>
</pubdate>
<pubdate>
	<type>gregorian</type>
	<year>2024</year>
	<month>8</month>
	<day>1</day>
</pubdate>
<volume>23</volume>
<number>5</number>
<publish_type>online</publish_type>
<publish_edition>1</publish_edition>
<article_type>fulltext</article_type>
<articleset>
	<article>


	<language>en</language>
	<article_id_doi></article_id_doi>
	<title_fa></title_fa>
	<title>Research Article: Characterization and phylogenetic analysisof a g-type lysozyme gene variant from the skin mucus of grass carp (Ctenopharyngodon idella)</title>
	<subject_fa>Genetics</subject_fa>
	<subject>Genetics</subject>
	<content_type_fa>پژوهشي</content_type_fa>
	<content_type>Orginal research papers</content_type>
	<abstract_fa></abstract_fa>
	<abstract>&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;The g-type lysozyme is one of the three major diverse lysozyme types recognized in the animal kingdom including fish. Using the RT-PCR technique, a 555 bp cDNA fragment encoding a g-type lysozymewas isolated from the skin mucus of &lt;i&gt;Ctenopharyngodon idella&lt;/i&gt; using homolog primes. The cDNA named Ci-Kh, codes for 185 amino acids with a predicted molecular weight of 20.49 kDa and theoretical pI of 9.13. The sequence consists of one cysteine residue with no predicted signal peptide. Domain analysis showed e-value of 3.74e-107 with the conserved domain of lysozyme-like superfamily (cd01021) between amino acid residues 12 to 184. Multiple alignment with the lysozyme genes from other fish species revealed &lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;that this protein have a goose egg white lysozyme (GEWL) domain containing two conserved catalytic residues (&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;Glu73 and Asp97) &lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;and N-acetyl-D-glucosamine binding site (&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;Glu73, Asp85, Asp97&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;, Tyr100, His101, His102, Ile119, Tyr147, Asn148)&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;span lang=&quot;TR&quot; style=&quot;font-size:11.0pt&quot;&gt;&lt;span calibri=&quot;&quot; style=&quot;font-family:&quot;&gt;&lt;span style=&quot;color:black&quot;&gt;. Protein structure prediction software revealed a prediction of 58% and 42% of &lt;i&gt;a&lt;/i&gt;-helical and random coils for the coding sequence of Ci-Kh, respectively.The 3D model of Ci-Kh revealed that this protein was mainly composed of five main helices and random coils. Phylogenetic analysis indicated that Ci-Kh matched the group of five grass carp g-type lysozyme transcript variants with 86-99% similarity. Among the five variants of this gene, Ci-Kh sequence had the highest and lowest genetic distance with &lt;i&gt;C. idella&lt;/i&gt; variant X2 (8.6%) and X3 (1.1%) sequences, respectively. We conclude that Ci-Kh as a different variant of g-type lysozyme cannot be ruled out.&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;</abstract>
	<keyword_fa></keyword_fa>
	<keyword>G-type lysozyme, Skin mucus, Ctenopharyngodon idella</keyword>
	<start_page>757</start_page>
	<end_page>770</end_page>
	<web_url>http://jifro.ir/browse.php?a_code=A-10-1538-4&amp;slc_lang=en&amp;sid=1</web_url>


<author_list>
	<author>
	<first_name>A.</first_name>
	<middle_name></middle_name>
	<last_name>Jolodar</last_name>
	<suffix></suffix>
	<first_name_fa></first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa></last_name_fa>
	<suffix_fa></suffix_fa>
	<email>jolodara@yahoo.com</email>
	<code>100319475328460052604</code>
	<orcid>100319475328460052604</orcid>
	<coreauthor>Yes
</coreauthor>
	<affiliation>Shahid Chamran University of Ahvaz</affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


</author_list>


	</article>
</articleset>
</journal>
