ID B2IP34_STRPS Unreviewed; 740 AA. AC B2IP34; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=Neuraminidase, putative {ECO:0000313|EMBL:ACB90105.1}; GN Name=nanC {ECO:0000313|EMBL:ACB90105.1}; GN OrderedLocusNames=SPCG_0853 {ECO:0000313|EMBL:ACB90105.1}; OS Streptococcus pneumoniae (strain CGSP14). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB90105.1, ECO:0000313|Proteomes:UP000001682}; RN [1] {ECO:0000313|EMBL:ACB90105.1, ECO:0000313|Proteomes:UP000001682} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGSP14 {ECO:0000313|EMBL:ACB90105.1, RC ECO:0000313|Proteomes:UP000001682}; RX PubMed=19361343; DOI=10.1186/1471-2164-10-158; RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.; RT "Genome evolution driven by host adaptations results in a more virulent and RT antimicrobial-resistant Streptococcus pneumoniae serotype 14."; RL BMC Genomics 10:158-158(2009). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. CC {ECO:0000256|ARBA:ARBA00009348}. 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; CP001033; ACB90105.1; -; Genomic_DNA. DR RefSeq; WP_000739353.1; NC_010582.1. DR AlphaFoldDB; B2IP34; -. DR SMR; B2IP34; -. DR CAZy; CBM40; Carbohydrate-Binding Module Family 40. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR KEGG; spw:SPCG_0853; -. DR HOGENOM; CLU_024974_0_0_9; -. DR Proteomes; UP000001682; Chromosome. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd15482; Sialidase_non-viral; 1. DR Gene3D; 2.120.10.10; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR002860; BNR_rpt. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR004124; Glyco_hydro_33_N. DR InterPro; IPR011040; Sialidase. DR InterPro; IPR026856; Sialidase_fam. DR InterPro; IPR036278; Sialidase_sf. DR InterPro; IPR023364; Trans_sialidase_dom3. DR PANTHER; PTHR10628; SIALIDASE; 1. DR PANTHER; PTHR10628:SF19; SIALIDASE; 1. DR Pfam; PF02012; BNR; 1. DR Pfam; PF13088; BNR_2; 1. DR Pfam; PF02973; Sialidase; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 3: Inferred from homology; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..740 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002778900" FT DOMAIN 98..269 FT /note="Glycoside hydrolase family 33 N-terminal" FT /evidence="ECO:0000259|Pfam:PF02973" FT DOMAIN 500..703 FT /note="Sialidase" FT /evidence="ECO:0000259|Pfam:PF13088" FT REGION 46..84 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 740 AA; 82260 MW; 9697B2A39CF98867 CRC64; MKKNIKQYVT LGTAVVLSAF VANSVAAQET ETSEVSTPEL VQPVAPTTPI SEVQPKSGNS SEVTVQPRTV ETTVKDPSSA TEETPVLEKN NVTLTGGGEN VTNELKDKFT SGDFTVVIKY NQSSEKGLQA LFGISNSKPG QQNSYVDVFL RDNGELGMEA RDTSSNKNHL VSRPASVWGK YKQEAVTNTV AVVADSVKKT YSLYANGTKV VEKKVDNFLN IKDIKGIDYY MLGGVKRAGK TAFGFNGTLE NIKFFNSALD EETVKKMTTN AVTGHLIYTA NDTTGSNYFR IPVLYTFSNG RVFSSIDARY GGTHDFLNKI NIATSYSDDN GKTWTKPKLT LAFDDFAPVP LEWPCDVGGR DLQISGGATY IDSVIVEKNN KQVLMFADVM PAGVSFREAT RKDSGYKQID GNYYLKLKKQ GDTDYNYTIR ENGTVYDDRT NRPTEFSVDK NFGIKQNGNY LTVEQYSVSF KNNKKTEYRN GTHVHMNIFY KDALFKVVPT NYIAYISSND HGESWSAPTL LPPIMGLNRN APYLGPGRGI IESSTGRILI PSYTGKESAF IYSDDNGASW KVKVVPLPSS WSAEAQFVEL SPGVIQAYMR TNNGKIAYLT STDAGTTWSA PEYLKFVSNP SYGTQLSIIN YSQLIDGKKA VILSTPNSTN GRKHGQIWIG LINDDNTIDW RYHHDVDYSN YGYSYSTLTE LPNHEIGLMF EKFDSWSRNE LHMKNVVPYI TFKIEDLKKN //