ID F9YRC5_CAPCC Unreviewed; 325 AA. AC F9YRC5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 02-SEP-2026, entry version 60. DE SubName: Full=Glycosylasparaginase beta chain {ECO:0000313|EMBL:AEK22483.1}; DE EC=3.5.1.26 {ECO:0000313|EMBL:AEK22483.1}; GN OrderedLocusNames=Ccan_03610 {ECO:0000313|EMBL:AEK22483.1}; OS Capnocytophaga canimorsus (strain 5). OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK22483.1, ECO:0000313|Proteomes:UP000008895}; RN [1] {ECO:0000313|EMBL:AEK22483.1, ECO:0000313|Proteomes:UP000008895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895}; RX PubMed=21914877; DOI=10.1128/JB.05853-11; RA Manfredi P., Pagni M., Cornelis G.R.; RT "Complete genome sequence of the dog commensal and human pathogen RT Capnocytophaga canimorsus strain 5."; RL J. Bacteriol. 193:5558-5559(2011). 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; CP002113; AEK22483.1; -; Genomic_DNA. DR RefSeq; WP_013996477.1; NC_015846.1. DR AlphaFoldDB; F9YRC5; -. DR STRING; 860228.Ccan_03610; -. DR KEGG; ccm:Ccan_03610; -. DR eggNOG; COG1446; Bacteria. DR HOGENOM; CLU_021603_0_1_10; -. DR OrthoDB; 9780217at2; -. DR Proteomes; UP000008895; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IEA:UniProtKB-EC. DR CDD; cd04513; Glycosylasparaginase; 1. DR FunFam; 3.60.20.30:FF:000005; N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase; 1. DR Gene3D; 3.60.20.30; (Glycosyl)asparaginase; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000246; Peptidase_T2. DR PANTHER; PTHR10188; L-ASPARAGINASE; 1. DR PANTHER; PTHR10188:SF6; N(4)-(BETA-N-ACETYLGLUCOSAMINYL)-L-ASPARAGINASE; 1. DR Pfam; PF01112; Asparaginase_2; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Hydrolase {ECO:0000313|EMBL:AEK22483.1}; KW Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303}; KW Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303}; KW Reference proteome {ECO:0000313|Proteomes:UP000008895}; KW Signal {ECO:0000256|PROSITE-ProRule:PRU00303}. FT CHAIN 16..325 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" FT /id="PRO_5049028250" FT ACT_SITE 182 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR600246-1" FT BINDING 210..213 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600246-2" FT BINDING 233..236 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600246-2" FT SITE 181..182 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|PIRSR:PIRSR600246-3" FT LIPID 16 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" FT LIPID 16 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" SQ SEQUENCE 325 AA; 34966 MW; 666929EDC2963353 CRC64; MKTIYFFTIS LLLVACKSNS SEKISEQDKS VNGKPVVIST WNHGLPANDV AWKILASGGS ALDAVEKGVM TAEADPEETS VGYGGYPDRE GNVTLDACIM DSQNNAGSVA CLKNIKHPIS VARLVMEKTP HVMLVGDGAK QFALSQGFKE EDLLTEKSKK AYEEWLKTSQ YKPIINIENH DTISMLALDE NGNLSGACTT SGMAWKMAGR VGDSPIIGGG LFLDNEVGAA AATGLGEAVI RTAGSAMVVE LMRHGKSPQE ACEIVTKRIY DLYKNTPELE HLQVGFIALS KGGEIGAFCV RKGFNYALQS KSQQNTLIDA TYMME //