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NCBI Reference Sequence: NP_501913.1
Identical Proteins FASTA Graphics
LOCUS NP_501913 347 aa linear INV 04-DEC-2024 DEFINITION Prostaglandin E synthase 2 [Caenorhabditis elegans]. ACCESSION NP_501913 VERSION NP_501913.1 DBLINK BioProject: PRJNA158 DBSOURCE REFSEQ: accession NM_069512.8 KEYWORDS RefSeq. SOURCE Caenorhabditis elegans ORGANISM Caenorhabditis elegans Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. REFERENCE 1 (residues 1 to 347) AUTHORS Sulson,J.E. and Waterston,R. CONSRTM Caenorhabditis elegans Sequencing Consortium TITLE Genome sequence of the nematode C. elegans: a platform for investigating biology JOURNAL Science 282 (5396), 2012-2018 (1998) PUBMED 9851916 REMARK Erratum:[Science 1999 Jan 1;283(5398):35] REFERENCE 2 (residues 1 to 347) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (04-DEC-2024) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 3 (residues 1 to 347) AUTHORS WormBase. CONSRTM WormBase Consortium TITLE Direct Submission JOURNAL Submitted (17-OCT-2024) WormBase Group, European Bioinformatics Institute, Cambridge, CB10 1SA, UK. Email: help@wormbase.org REFERENCE 4 (residues 1 to 347) AUTHORS Sulson,J.E. and Waterston,R. TITLE Direct Submission JOURNAL Submitted (03-MAR-2003) Nematode Sequencing Project: Sanger Institute, Hinxton, Cambridge CB10 1SA, UK and The Genome Institute at Washington University, St. Louis, MO 63110, USA COMMENT REVIEWED REFSEQ: This record has been curated by WormBase. The reference sequence is identical to CAA94368. FEATURES Location/Qualifiers source 1..347 /organism="Caenorhabditis elegans" /strain="Bristol N2" /db_xref="taxon:6239" /chromosome="IV" Protein 1..347 /product="Prostaglandin E synthase 2" /calculated_mol_wt=40161 Region 65..138 /region_name="Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold" /note="The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox...; cl00388" /db_xref="CDD:469754" Region 183..334 /region_name="GST_C_mPGES2" /note="C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; cd03197" /db_xref="CDD:198306" Site order(184,188,195,200,259,261) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:198306" Site order(194,198,222..223,226,292,301,304..305) /site_type="other" /note="N-terminal domain interface [polypeptide binding]" /db_xref="CDD:198306" Site order(205..206,209..210,219,222..223,305,309) /site_type="active" /note="GRX-like active site [active]" /db_xref="CDD:198306" CDS 1..347 /gene="pges-2" /locus_tag="CELE_R11A8.5" /standard_name="R11A8.5" /coded_by="NM_069512.8:1..1044" /note="Confirmed by transcript evidence" /db_xref="GeneID:177925" /db_xref="WormBase:WBGene00011239" ORIGIN 1 mrffgvrtvq iaslagfswg gsklddiqta klrtcpiqvq qpekvqndvl lsrkvinhld 61 ksnlklrlyq yetcpfcckv rafldyhgfs yevvevnpvt rsqikfstty kkvpilrsge 121 ttmtestlii stlatylqrp dqsldqiiqm ypavdstnek gkpvlnypnk ffvmkgkvdg 181 danmasaree rewrewvdnw fihlispnvy rnwnesvetf rwfeqvgdwh rtfpawervl 241 avyvgaaamf llsktlkkkh nindereelr kacrdwmaai gpnrqflggd epnladlsly 301 gamnsfygcs afkevileek iaewwrkmda lvknhdgrka lesrsqk //
Whole sequence Selected region from: to:
Conserved Domains
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