ID C0MCG2_STRS7 Unreviewed; 1546 AA. AC C0MCG2; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733}; DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733}; GN OrderedLocusNames=SZO_05310 {ECO:0000313|EMBL:CAW98510.1}; OS Streptococcus equi subsp. zooepidemicus (strain H70). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368}; RN [1] {ECO:0000313|EMBL:CAW98510.1, ECO:0000313|Proteomes:UP000001368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H70 {ECO:0000313|EMBL:CAW98510.1, RC ECO:0000313|Proteomes:UP000001368}; RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346; RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A., RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., RA Maskell D.J., Parkhill J., Waller A.S.; RT "Genomic evidence for the evolution of Streptococcus equi: host RT restriction, increased virulence, and genetic exchange with human RT pathogens."; RL PLoS Pathog. 5:E1000346-E1000346(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; FM204884; CAW98510.1; -; Genomic_DNA. DR KEGG; seq:SZO_05310; -. DR PATRIC; fig|40041.11.peg.562; -. DR eggNOG; COG2273; Bacteria. DR eggNOG; COG4409; Bacteria. DR HOGENOM; CLU_246588_0_0_9; -. DR Proteomes; UP000001368; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd08023; GH16_laminarinase_like; 1. DR CDD; cd15482; Sialidase_non-viral; 1. DR Gene3D; 2.120.10.10; -; 1. DR Gene3D; 2.60.120.200; -; 2. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR000757; GH16. DR InterPro; IPR011040; Sialidase. DR InterPro; IPR026856; Sialidase_fam. DR InterPro; IPR036278; Sialidase_sf. DR InterPro; IPR020610; Thiolase_AS. DR InterPro; IPR023364; Trans_sialidase_dom3. DR InterPro; IPR005877; YSIRK_signal_dom. DR NCBIfam; TIGR01168; YSIRK_signal; 1. DR PANTHER; PTHR10628; SIALIDASE; 1. DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1. DR Pfam; PF13088; BNR_2; 1. DR Pfam; PF00722; Glyco_hydro_16; 1. DR Pfam; PF04650; YSIRK_signal; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR SUPFAM; SSF50939; Sialidases; 1. DR PROSITE; PS51762; GH16_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:CAW98510.1}; KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21..42 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 260..550 FT /note="GH16" FT /evidence="ECO:0000259|PROSITE:PS51762" FT REGION 1242..1270 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1546 AA; 169787 MW; EC1A64DB75AB7E72 CRC64; MLFNPIGKEQ IRKYAIKKLS VGVASVCVGI GLAAGLPVVV YADDVSEVSL QQPTKAAVTE ISHEQEPQAT DTDSEALVVS EETTVDEAVV ANAVTSNAAD QTADEEKSNA PVELNKVANG GFDNDYVSNK NQWQYREGGH SVLTTENNNS YAEVTSGTLD EHILQKVSTT VGKTYTLEAD VKVEADTPHN GLYLTAKESN HNLQGPVIKE VSLTDTDGTW SHIKLSFTAT TSETFVGLVK RLEASSPETL AASASIDNVS VVEENDYELI WQDEFSGDQL NQENWGYELG SIRGNEQQHY TDSTENIYLE NGNLVLNVTE RKGEDRYANP RGGTSARQVI YDSGSVRTVG KQEFLYGRIE ARAKLPKGKG AFPAFWTLGA DFTLDGDIAS TQGYGWPSTG ELDIMELIGA PNGEHEGELA EGDQSNKTVY GTPHFYYVKG DADKDGSYSP TALGGNLTLS DDFYDDYHIF GINWYPDKIE WYVDGIVYNT MYLTGDERLE AAAAAFNKPQ YLQFNLATGG NWSKNAGYYL ASDETAFVID YVRYYQDAEQ KAASEAYYAS QPDLKGVKDL TMLEGTSPDL AQAVTTDQEG YVVDFSVENE YLFTNKGGNT NAALQAAGRD DLSALSELAP GIYNIYYSAV PYNADLGSTV TPTAKIAREV AILTVLPKEG LIGKKGEPLS TVALPANWQW VTPEEILGSA EHYQIKYTTE GGRAIYTSIE ASYISDQPIS DQASILVDLG NAILDATAEK AAVTDDEALS KLDDVMSLNQ GTVTIRYRLD TADTTVRSSS PLALLSISNQ ASANEYASFF IEPKNNKIGL EFKGAEVPIV KVGSGFNLLT NSDWQTISYV FTGSRLKIYL NGDLYGEADF AGFMKQLPWK ASADTLTIGG LKRTYDGESV LHWGLKGLVD QVLIDTDVYD LTDIAKAHQS TLRPVTGEKT NVWDKYDEGV FEYRIPSVVK TPSGTLIAAA DARKKHYNDW GDVATVVRIS HDDGKTWSNN ITVLDMPTQP YFTTQYSLAD WNTNMTQSAF SIDSTLLTDA SGKLYLLVDV FPESQGAVAS KAGSGYELIN GQYYLNLYDF DNNKYTVREG GIVYDQNGHQ TDMYVDEGNF ETAFSTRGNL YQTEAGEDIL LGNIYLRSGR TKQGITREGS QTAPLFTYMT SFLWLLTSED EGQTWSTPLD ITPQIKEDWM GFLGTGAAAG IEIDAVNAEG EQVKRLVFPI YYTNQQNATS ASLGRQSSAN IFSDDGGQTW QRGESPNDGR IYGHNQQTTS KDFDTSVTEL TENQIIQLNN GHLLQFMRNT GKTIVIARST DYGATWEDNP TVTDLPEPYV NLSAIHMMVD GKEYVVLSNP LGEPSGEQLT IRNQRMKGIL RVGEVLEDDS INWVASTIFE PKRFAYSSLV QLDDERVGLL YEYSGQITYS TFNIKQMISD QFREDKAEIE EVTITSAAPK QNGKASITIQ MTFNQPMFIL GDRQLAVTVN GVDKLASYVS GDGTDTAIFE LSLESMPEGP ITVLPQFDHT IVETKYGIRL TDDKAYTVSY PAAVTA //