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Reviewed, UniProtKB/Swiss-Prot Q9VJ62 (NAF1_DROME)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    H/ACA ribonucleoprotein complex non-core subunit NAF1
Gene names
ORF Names: CG10341
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disapears during maturation of the complex and is replaced by GAR1/CG4038 to yield mature H/ACA snoRNPs complex By similarity.

Subunit structure

During assembly of the complex, component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the NAF1 family.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentNucleus
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

small nucleolar ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GbpQ9V3B21EBI-154062,EBI-115372

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564H/ACA ribonucleoprotein complex non-core subunit NAF1
PRO_0000315640

Regions

Compositional bias197 – 21620Ser-rich
Compositional bias516 – 56348Pro-rich

Amino acid modifications

Modified residue2501Phosphothreonine Ref.4
Modified residue2541Phosphoserine Ref.4
Modified residue4031Phosphoserine Ref.4
Modified residue4271Phosphothreonine Ref.4
Modified residue4291Phosphoserine Ref.4
Modified residue4321Phosphothreonine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9VJ62-1 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 283FB6B26F415044

FASTA56462,270
        10         20         30         40         50         60 
MESEQPAAVK ASAPIEEPQS TETAVELGKH STLKADLSID KLETATTEAT NAVVEPVEME 

        70         80         90        100        110        120 
QQVENELVNE STQAMTSTTT QEKVVGSVNN LVEEQQCVEM EFETSSDLVV QGSPSEESKK 

       130        140        150        160        170        180 
VASDASATVT APQVQPAPHV DSSPQASGLS LLAAYSSDDS DDEKVTPVQN GDNDVIEVPV 

       190        200        210        220        230        240 
TDPASSTTAY RPVVAVSSDD ESSKSSSSSS DSDSDSEGEY LTVLRKKIDK RINTVDCDED 

       250        260        270        280        290        300 
DEDFDEDGAT GDRSRRRQPP KVRGEMLLDD LPPIHQLEIT VPEDECVELG KVQSIVDQLV 

       310        320        330        340        350        360 
LVSVLPNSML FDLDTVLFLE KGRKVLGEVF DVLGQVSDPL YCVRFNSNKQ ILDRGIKIGD 

       370        380        390        400        410        420 
VVYCAPKTEH TQFVILSKLM QVRGSDASWE HDVEPPARYV DHSDDEEERE ARAEQRKRRQ 

       430        440        450        460        470        480 
RDRTNSTDSV DTVTSVATTA TKASSVAPPP RQRGRRGQRE SFRQSQRPSI NQHNQNQPQD 

       490        500        510        520        530        540 
EQYNFHPSYN PGSWHSNYYQ NYHQAAANFN MAQQHPGMPF PVPNYGYGMP YAMPPMYPHM 

       550        560 
YPPPPPFAPP PPNNQSHQGQ PPPS 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[4]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250; SER-254; SER-403; THR-427; SER-429 AND THR-432, MASS SPECTROMETRY.
Tissue: Embryo.

Cross-references

Sequence databases

AE014134 Genomic DNA. Translation: AAF53693.2.
AY051589 mRNA. Translation: AAK93013.1.
RefSeqNP_609898.1.
UniGeneDm.23213

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9VJ62. 4 interactions.

Genome annotation databases

EnsemblFBgn0032701. Drosophila melanogaster. [Contig view]
GeneID35125.
NMPDRfig|7227.3.peg.2858.

Organism-specific databases

FlyBaseFBgn0032701. CG10341.

Phylogenomic databases

HOGENOMQ9VJ62.
OMAQ9VJ62. SEGEYLT.

Family and domain databases

InterProIPR008696. NAF1.
[Graphical view]
PfamPF05492. NAF1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio791988.

Entry information

Entry nameNAF1_DROME
AccessionPrimary (citable) accession number: Q9VJ62
Secondary accession number(s): Q961H3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents