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UniProtKB/Swiss-Prot entry Q02834


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NANH_MICVI
Primary accession number Q02834
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Sialidase [Precursor]
Synonyms EC 3.2.1.18
Neuraminidase
Gene name
Name: nedA
From
Micromonospora viridifaciens [TaxID: 1881] 
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Micromonosporineae; Micromonosporaceae; Micromonospora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-647.
STRAIN=ATCC 31146 / DSM 43909 / FD 23988 / JCM 3267;
PubMed=1400240 [NCBI, ExPASy, EBI, Israel, Japan]
Sakurada K., Ohta T., Hasegawa M.;
"Cloning, expression, and characterization of the Micromonospora viridifaciens neuraminidase gene in Streptomyces lividans.";
J. Bacteriol. 174:6896-6903(1992).
[2]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
STRAIN=ATCC 31146 / DSM 43909 / FD 23988 / JCM 3267;
DOI=10.1016/S0969-2126(01)00255-6; PubMed=8591030 [NCBI, ExPASy, EBI, Israel, Japan]
Gaskell A., Crenell S., Taylor G.;
"The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll.";
Structure 3:1197-1205(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D01045; BAA00852.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45244; A45244.
3D structure databases
PDB
1EUR; X-ray; 1.82 A; A=43-407.[ExPASy / RCSB / EBI]
1EUS; X-ray; 2.00 A; A=43-407.[ExPASy / RCSB / EBI]
1EUT; X-ray; 2.50 A; A=43-647.[ExPASy / RCSB / EBI]
1EUU; X-ray; 2.50 A; A=43-647.[ExPASy / RCSB / EBI]
1W8N; X-ray; 2.10 A; A=47-647.[ExPASy / RCSB / EBI]
1W8O; X-ray; 1.70 A; A=47-647.[ExPASy / RCSB / EBI]
1WCQ; X-ray; 2.10 A; A/B/C=47-647.[ExPASy / RCSB / EBI]
2BER; X-ray; 1.80 A; A=47-647.[ExPASy / RCSB / EBI]
2BZD; X-ray; 2.00 A; A/B/C=47-647.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EUR; -.
1EUS; -.
1EUT; -.
1EUU; -.
1W8N; -.
1W8O; -.
1WCQ; -.
2BER; -.
2BZD; -.
ModBase Q02834.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004308; Molecular function: exo-alpha-sialidase activity (inferred from electronic annotation from EC).
GO:0007155; Biological process: cell adhesion (inferred from electronic annotation from InterPro).
GO:0008152; Biological process: metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002860; BNR.
IPR000421; Coagulation_factor_5/8-type_C.
IPR013783; Ig-like_fold.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 1.
Pfam PF02012; BNR; 5.
PF00754; F5_F8_type_C; 1.
Pfam graphical view of domain structure.
SMART SM00231; FA58C; 1.
SMART graphical view of domain structure.
PROSITE PS50022; FA58C_3; 1.
PS51318; TAT; UNKNOWN_1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q02834.
Other
LinkHub Q02834; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    37  37      
CHAIN   38   647  610     Sialidase. PRO_0000012032
REPEAT   102   113  12     BNR 1. 
REPEAT   175   186  12     BNR 2. 
REPEAT   239   250  12     BNR 3. 
REPEAT   287   298  12     BNR 4. 
REPEAT   348   359  12     BNR 5. 
DOMAIN   496   646  151     F5/8 type C. 
ACT_SITE   92    92        Proton acceptor (By similarity). 
ACT_SITE   260   260        Nucleophile (Potential). 
ACT_SITE   370   370        Nucleophile. 
BINDING   68    68        Substrate (By similarity). 
BINDING   276   276        Substrate (By similarity). 
STRAND   51    58  8      
STRAND   67    74  8      
STRAND   80    86  7      
STRAND   98   106  9      
STRAND   115   118  4      
STRAND   123   125  3      
STRAND   127   136  10      
TURN   138   140  3      
STRAND   143   152  10      
TURN   155   157  3      
STRAND   171   179  9      
STRAND   185   188  4      
HELIX   190   193  4      
STRAND   201   204  4      
STRAND   206   208  3      
TURN   216   219  4      
STRAND   221   228  8      
STRAND   234   243  10      
STRAND   260   265  6      
STRAND   271   275  5      
STRAND   282   289  8      
STRAND   300   306  7      
STRAND   313   318  6      
HELIX   327   329  3      
STRAND   331   336  6      
STRAND   339   352  14      
STRAND   359   367  9      
STRAND   371   375  5      
STRAND   381   385  5      
STRAND   388   396  9      
HELIX   398   401  4      
STRAND   413   415  3      
STRAND   420   428  9      
STRAND   431   433  3      
STRAND   435   437  3      
STRAND   439   443  5      
STRAND   448   454  7      
STRAND   462   470  9      
STRAND   478   487  10      
STRAND   492   503  12      
HELIX   506   508  3      
STRAND   510   515  6      
STRAND   520   522  3      
HELIX   526   530  5      
STRAND   552   571  20      
STRAND   582   593  12      
STRAND   595   602  8      
STRAND   610   626  17      
STRAND   637   645  9      
Sequence information
Length: 647 AA [This is the length of the unprocessed precursor] Molecular weight: 68830 Da [This is the MW of the unprocessed precursor] CRC64: DCC1FE5BC935B8AD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTANPYLRRL PRRRAVSFLL APALAAATVA GASPAQAIAG APVPPGGEPL YTEQDLAVNG 

        70         80         90        100        110        120 
REGFPNYRIP ALTVTPDGDL LASYDGRPTG IDAPGPNSIL QRRSTDGGRT WGEQQVVSAG 

       130        140        150        160        170        180 
QTTAPIKGFS DPSYLVDRET GTIFNFHVYS QRQGFAGSRP GTDPADPNVL HANVATSTDG 

       190        200        210        220        230        240 
GLTWSHRTIT ADITPDPGWR SRFAASGEGI QLRYGPHAGR LIQQYTIINA AGAFQAVSVY 

       250        260        270        280        290        300 
SDDHGRTWRA GEAVGVGMDE NKTVELSDGR VLLNSRDSAR SGYRKVAVST DGGHSYGPVT 

       310        320        330        340        350        360 
IDRDLPDPTN NASIIRAFPD APAGSARAKV LLFSNAASQT SRSQGTIRMS CDDGQTWPVS 

       370        380        390        400        410        420 
KVFQPGSMSY STLTALPDGT YGLLYEPGTG IRYANFNLAW LGGICAPFTI PDVALEPGQQ 

       430        440        450        460        470        480 
VTVPVAVTNQ SGIAVPKPSL QLDASPDWQV QGSVEPLMPG RQAKGQVTIT VPAGTTPGRY 

       490        500        510        520        530        540 
RVGATLRTSA GNASTTFTVT VGLLDQARMS IADVDSEETA REDGRASNVI DGNPSTFWHT 

       550        560        570        580        590        600 
EWSRADAPGY PHRISLDLGG THTISGLQYT RRQNSANEQV ADYEIYTSLN GTTWDGPVAS 

       610        620        630        640 
GRFTTSLAPQ RAVFPARDAR YIRLVALSEQ TGHKYAAVAE LEVEGQR 

Q02834 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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