ID A0A2S0JCU3_CAMFE Unreviewed; 348 AA. AC A0A2S0JCU3; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 10-OCT-2018, entry version 3. DE SubName: Full=Type II asparaginase {ECO:0000313|EMBL:AVK81266.1}; DE EC=3.5.1.1 {ECO:0000313|EMBL:AVK81266.1}; GN Name=ansB {ECO:0000313|EMBL:AVK81266.1}; GN ORFNames=C6B32_05305 {ECO:0000313|EMBL:AVK81266.1}; OS Campylobacter fetus subsp. testudinum. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1507806 {ECO:0000313|EMBL:AVK81266.1, ECO:0000313|Proteomes:UP000240030}; RN [1] {ECO:0000313|EMBL:AVK81266.1, ECO:0000313|Proteomes:UP000240030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=772 {ECO:0000313|EMBL:AVK81266.1, RC ECO:0000313|Proteomes:UP000240030}; RA Hou S.; RT "Complete Genome Sequence of Campylobacter fetus subsp. testudinum RT Strain 772, isolated from ascites of patient with peritonitis."; RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the asparaginase 1 family. CC {ECO:0000256|RuleBase:RU004456}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP027287; AVK81266.1; -; Genomic_DNA. DR RefSeq; WP_058909345.1; NZ_LFLP01000004.1. DR Proteomes; UP000240030; Chromosome. DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1170; -; 1. DR Gene3D; 3.40.50.40; -; 1. DR InterPro; IPR004550; AsnASE_II. DR InterPro; IPR036152; Asp/glu_Ase-like_sf. DR InterPro; IPR006034; Asparaginase/glutaminase-like. DR InterPro; IPR020827; Asparaginase/glutaminase_AS1. DR InterPro; IPR027475; Asparaginase/glutaminase_AS2. DR InterPro; IPR027473; L-asparaginase_C. DR InterPro; IPR027474; L-asparaginase_N. DR InterPro; IPR037152; L-asparaginase_N_sf. DR Pfam; PF00710; Asparaginase; 1. DR PIRSF; PIRSF001220; L-ASNase_gatD; 1. DR PRINTS; PR00139; ASNGLNASE. DR SMART; SM00870; Asparaginase; 1. DR SUPFAM; SSF53774; SSF53774; 1. DR TIGRFAMs; TIGR00520; asnASE_II; 1. DR PROSITE; PS00144; ASN_GLN_ASE_1; 1. DR PROSITE; PS00917; ASN_GLN_ASE_2; 1. DR PROSITE; PS51732; ASN_GLN_ASE_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000240030}; KW Hydrolase {ECO:0000313|EMBL:AVK81266.1}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 348 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015552509. FT DOMAIN 24 215 Asparaginase. {ECO:0000259|Pfam:PF00710}. FT REGION 111 112 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR001220-2}. FT ACT_SITE 32 32 {ECO:0000256|PROSITE-ProRule:PRU10099}. FT ACT_SITE 32 32 Acyl-ester intermediate. FT {ECO:0000256|PIRSR:PIRSR604550-50}. FT ACT_SITE 32 32 O-isoaspartyl threonine intermediate. FT {ECO:0000256|PIRSR:PIRSR001220-1}. FT ACT_SITE 111 111 {ECO:0000256|PROSITE-ProRule:PRU10100}. FT BINDING 78 78 Substrate. {ECO:0000256|PIRSR: FT PIRSR001220-2}. SQ SEQUENCE 348 AA; 37395 MW; 32903C360C2965D9 CRC64; MCLIKKVFIL MLITMSAMFA KPTIYILATG GTIAGSSASS LSSGYTSGTV TVDKLISAVP QINEIATIKG EQISNIGSQE MNNDVWLKLA KRVNELLDSK NVDGIVITHG TDTMEETAYF LNLVVKSDKP IVMVGAMRNS DSLSSDGPLN LYNAVNVAMS KDAVGKGVLV VMNDEIHAAR EITKTNTTSV DTFKSPNTGK IGTVIYGNVK FYMQSTRKHT KNSEFDISTI SSLPRVDIIF SHSNDNPDFV NAAVKNGAKG IINAGMGNGN IYPSALEALA KAVKQGVIVV RDSRVGSGET TNPGEIDDAK YGFLTSDNLN AQKARVLLMV ALTKTSDPKK IEEYFLTY //