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
//