ID   B1MR93_9INFA            Unreviewed;       449 AA.
AC   B1MR93;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   07-SEP-2016, entry version 45.
DE   RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00062759};
DE            EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063188};
GN   Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ACA48002.1};
OS   Influenza A virus (A/chicken/Yunnan/1083/2003(H5N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=496744 {ECO:0000313|EMBL:ACA48002.1};
RN   [1] {ECO:0000313|EMBL:ACA48002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/chicken/Yunnan/1083/2003 {ECO:0000313|EMBL:ACA48002.1};
RX   PubMed=18216109; DOI=10.1128/JVI.02468-07;
RA   Wang J., Vijaykrishna D., Duan L., Bahl J., Zhang J.X., Webster R.G.,
RA   Peiris J.S., Chen H., Smith G.J., Guan Y.;
RT   "Identification of the progenitors of Indonesian and Vietnamese avian
RT   influenza A (H5N1) viruses from southern China.";
RL   J. Virol. 82:3405-3414(2008).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00062942}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00063168}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00561320}; Single-pass type II membrane
CC       protein {ECO:0000256|SAAS:SAAS00561320}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00561294}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00561099}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CY029379; ACA48002.1; -; Viral_cRNA.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd15483; Influenza_NA; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   InterPro; IPR033654; Sialidase_Influenza_A/B.
DR   InterPro; IPR011040; Sialidases.
DR   Pfam; PF00064; Neur; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448743};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00449120};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448849};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448685};
KW   Host membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00449348};
KW   Hydrolase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448424};
KW   Membrane {ECO:0000256|SAAS:SAAS00448618, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448775};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00449168,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00448371,
KW   ECO:0000256|SAM:Phobius};
KW   Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00448515}.
FT   TRANSMEM      7     34       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   449 AA;  48984 MW;  7D7EFE877FDE9CCD CRC64;
     MNPNQKIITI GSICMVTGIV SLMLQIGNMI SIWVSHSIHT GNQHQAEPIS NTNFLTEKAV
     ASVTLAGNSS LCPISGWAVH SKDNSIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL
     NDKHSNGTVK DRSPHRTLMS CPVGEAPSPY NSKFESVAWS ASACHDGTSW LTIGISGPDN
     GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT VMTDGPSNGQ ASYKIFKMEK
     GKVVKSVELD APNYHYEECS CYPDAGEITC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG
     VFGDNPRPND GTGSCGPVSS NGAYGVKGFS FKYGNGVWIG RTKSTNSRSG FEMIWDPNGW
     TETDSSFSVK QDIVAITDWS GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKESTIWTSG
     SSISFCGVNS DTVGWSWPDG AELPFTIDK
//