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Database: UniProt
Entry: A0A091MP12_9PASS
LinkDB: A0A091MP12_9PASS
Original site: A0A091MP12_9PASS 
ID   A0A091MP12_9PASS        Unreviewed;       476 AA.
AC   A0A091MP12;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=N310_03972 {ECO:0000313|EMBL:KFP78428.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP78428.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP78428.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP78428.1};
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; KK833656; KFP78428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091MP12; -.
DR   Proteomes; UP000053537; 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:UP000053537}.
FT   DOMAIN          36..260
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
FT   REGION          332..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         476
FT                   /evidence="ECO:0000313|EMBL:KFP78428.1"
SQ   SEQUENCE   476 AA;  52555 MW;  2D315ADD58444CF9 CRC64;
     MGSRHFPART VLFEKESNGV TYRVPALLYL PCVAKLLAFA EERISADDAH ANLLVLRRGT
     IYGSYVEWED MRVLETATLQ HHRSMNPCPV YDEFTGTLFL FFITVLGRTP EAYQIVTGQN
     VTRLCCVTSA DQGLSWSTAK DLTQQVIGGT IKDWATFALG PGHGIQLRSG RLLVPAYSYH
     IDCKECFGQL CKTTPHSFTF YSDDHGRRWR FGEFIPNLQT GECQLVSVDE EDGSNVLYCN
     ARSPLGFRVQ ALSTDDGAVF HGGQLVQRLV EPPHGCHGSV IGFPAPLVYV PTTPQDPVMS
     LRGSAQRLLP GMLWGCQSLP TQEAAGDELH TVATSSHHEP DEPDEDCPTP GHHHHAHSGT
     LVQGDPAVPP GPTPFFQAPT WILYSHPTSS MSRVNMGVHL STFPRDAESW TEPWVIYEGP
     SAYSDLAYME LPYPEAPVAG GTAIAFACLY ENGMRSPYEQ ISFSMFTLHD VLQNIP
//
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