ID A0A1R1SSP8_9ACTN Unreviewed; 641 AA.
AC A0A1R1SSP8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN ORFNames=SPAR_01739 {ECO:0000313|EMBL:OMI41295.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI41295.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI41295.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI41295.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMI41295.1}.
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DR EMBL; ASQP01000026; OMI41295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1SSP8; -.
DR STRING; 67365.GCA_001704635_00945; -.
DR Proteomes; UP000186168; Unassembled WGS sequence.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR CDD; cd00110; LamG; 1.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..641
FT /note="exo-alpha-sialidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039324319"
FT DOMAIN 455..595
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 455..590
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 397..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 69483 MW; 88C187AE2CB0141F CRC64;
MFLAAAALAL IPIPVRAAEA ESSASAARTD FEQHVLFKSS QDSGYSCFRI PAVVKSKDGT
LLAFAEGRVN NCGDAGDIDL VLKRSTDGGR TWGPLQVINE GARDTHGNPA PVVDLRTGRI
LLASTYNTGR DDSQGCDVPC DRTPHLQYSD DDGVTWSTPR DLSDSLLPAS WNSWYATGPV
HGIQLTHGRY RGRLLFTINT ESHDGTRITA NHAALAYSDD GGDTWRVGAV DSWPVTADGT
FRQKPSEMTL VEREDGSVYV NGREQDGTDL GHRDFAVSRD GGESFTGPFR TIPDLYTPQV
QGSILRLRSE DRDGYSRLLL AAPADPDRRR TMTIRSSWNE GRDWDSADRG KVVTTDWSGY
SDMVRVSLDE VGLMYEGGAV DARDEIRFAR FTEDWLGPRR GPDPTTADRA PGARPATVLG
GPARTEGRFG RGLSFDGTDD AVHVPFRPSL PLGTRDFTVS LWFRYTAATG QQPFLWMGGI
GNKQPQVWLR GEPSSGRVRA LITTVNGTAT FTSASVSTGS AYNDGQWHHA ALIRAGGRLS
LAIDGGTPVS AADVPGPVTR TSPFGIHVGE AVDSRSHLTG ALDEVRVWGR ALSDTELRQV
REFNATPDGH GDPGDRGDRG GKDYSALVRL PLDRVRPADD R
//
