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Database: UniProt
Entry: A0A1D7Y6A4_9ACTN
LinkDB: A0A1D7Y6A4_9ACTN
Original site: A0A1D7Y6A4_9ACTN 
ID   A0A1D7Y6A4_9ACTN        Unreviewed;       625 AA.
AC   A0A1D7Y6A4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   ORFNames=BFF78_08635 {ECO:0000313|EMBL:AOR31101.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR31101.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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DR   EMBL; CP017248; AOR31101.1; -; Genomic_DNA.
DR   RefSeq; WP_069777749.1; NZ_CP017248.1.
DR   AlphaFoldDB; A0A1D7Y6A4; -.
DR   KEGG; spun:BFF78_08635; -.
DR   Proteomes; UP000094960; Chromosome.
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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..625
FT                   /note="exo-alpha-sialidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009102609"
FT   DOMAIN          461..600
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   DOMAIN          461..595
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|SMART:SM00282"
FT   REGION          273..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  67490 MW;  CEF431B2D9D10E1F CRC64;
     MPSGLRARLR SALATALSTA ALLLAPLATP QAAHAQPTSA SPKFEQQVLF KAAQDPGYAC
     FRIPAIVKTA DGTLLAFAEG RVLNCGDAAD IDIVLKRSTD GGRTWGPLQV VNDGGGDTHG
     NPAPIVDRAT GRVWLAETYN TGRTDSASCS IPCDRTPHLQ YSDDDGATWS APRDLSPEIL
     PADWNSWYAT GPVHGIQLTK GRYAGRLVFG VNTETWDGGR VTANHAALIV SDDHGGHWRI
     GATDTWPIAD DGTFRQKPSE LALAERGDGS LLVSGREQDG TDLGHRTQAV SRDGGSSFTA
     TFHDLPDLYA PQVQGSLLRL GNRLLLACPA DPDRRRTMMI RSSYDGGRTW DSVDRGTVVT
     TDWSGYSDLV RVDADTVGLI YEGGAVDARG EIRFARFTED WLAPRRGPDP VTADLAPHAR
     PAAVLGGAEE TEGVFGGALR FDGSDDAVRL PYRSALPLGR KDFTASLWFR YTATTGEQPL
     LWMGGVGTSQ PQVWVRGEPS NHRIQGLITV RDGAIAPQTA YVRTNTAYND GEWHHLVLRR
     GEGRLSLFVD GMQSSVDDIP GSVSRNSPFG VHIGQRMDSR AFFTGAIDEV HVWDRALTDQ
     ELSDPKALRS PKDTVLWLPL DHVSG
//
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