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Database: UniProt
Entry: A0A087RD61_APTFO
LinkDB: A0A087RD61_APTFO
Original site: A0A087RD61_APTFO 
ID   A0A087RD61_APTFO        Unreviewed;       476 AA.
AC   A0A087RD61;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
DE   Flags: Fragment;
GN   ORFNames=AS27_13672 {ECO:0000313|EMBL:KFM11415.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM11415.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM11415.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM11415.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000427};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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DR   EMBL; KL226300; KFM11415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087RD61; -.
DR   STRING; 9233.A0A087RD61; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 2.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF22; SIALIDASE-4; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT   DOMAIN          36..260
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
FT   REGION          333..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         476
FT                   /evidence="ECO:0000313|EMBL:KFM11415.1"
SQ   SEQUENCE   476 AA;  52591 MW;  3ED194D00444BA6F CRC64;
     MGSRHFPART VLFEKESNGV TYRVPALLYL PCVAKLLAFA EERLSADDAH ANLLVLRRGT
     IYRSYVEWED MRVLETATLQ HHRSMNPCPL YDEFTGTLFL FFITVLGRTP EAYQIVTGQN
     VTRLCCVTSA DQGLSWSMAT DLTQQVIGGA IKDWATFALG PGHGIQLRSG RLLVPAYSYH
     IDCKECFGQL CRTTPHSFAF YSDDHGRGWR FGEFIPNLQT GECQLVSVDE EDGSNVLYCN
     ARSPLGFRVQ ALSTDDGAVF HGGQLVQRLV EPPHGCHGSV VGFPAPFVYV PDASRDTVMP
     LQGSAHRLLP RMLPRFRYLP IQRAAGDELP ALATGSHHEP AEPEEGCPTS GHHGHAHGST
     SVRGDPRATP SPAALFQAPT WVLYSHPTSP MSRVNMGVHL STFPRDAESW TEPWVIYEGP
     SAYSDLAYME LPYNEASISG GPAIAFACLY ENGTRSPYEQ ISFSMFTLHD VLQNIP
//
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