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Protein

Probable RNA helicase armi

Gene

armi

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable RNA helicase required for axial polarization of the oocyte during early and mid oogenesis. Plays a central role in RNA interference (RNAi) process, a process that mediates mRNA destruction of translational repression. Required for the assembly of the RISC complex, a complex required for target RNA destruction or repression. May be required in the RISC assembly to unwind miRNAs, in the production of single-stranded miRNA from the double-stranded miRNA, a key step in RISC formation. Required both for the translational control of oskar (osk) mRNA and cytoskeletal polarization in the oocyte. Required for somatic primary piRNA biogenesis.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi723 – 730ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA helicase activity Source: UniProtKB

GO - Biological processi

  • dorsal appendage formation Source: FlyBase
  • embryonic axis specification Source: UniProtKB
  • germarium-derived egg chamber formation Source: FlyBase
  • long-term memory Source: FlyBase
  • microtubule organizing center organization Source: FlyBase
  • negative regulation of DNA damage checkpoint Source: FlyBase
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  • oogenesis Source: FlyBase
  • pole plasm protein localization Source: FlyBase
  • RNA interference Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Helicase, Hydrolase
Biological processRNA-mediated gene silencing
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable RNA helicase armi (EC:3.6.4.13)
Alternative name(s):
Protein armitage
Gene namesi
Name:armi
ORF Names:CG11513
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0041164. armi.

Subcellular locationi

GO - Cellular componenti

  • axon Source: FlyBase
  • cytoplasm Source: UniProtKB
  • cytosol Source: FlyBase
  • dendrite Source: FlyBase
  • mitochondrion Source: FlyBase
  • neuronal cell body Source: FlyBase
  • P granule Source: FlyBase
  • synapse Source: FlyBase
  • Yb body Source: FlyBase

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000807081 – 1188Probable RNA helicase armiAdd BLAST1188

Proteomic databases

PaxDbiQ6J5K9.
PRIDEiQ6J5K9.

Expressioni

Tissue specificityi

Abundant in oocytes and syncytial blastoderm. Expressed at low level throughout development, including somatic tissues. First apparent early in oogenesis, in the cytoplasm of stem cells and mitotically dividing cystoblasts. In regions 2a and 2b of the germarium, it is most concentrated in the center of the germline cysts, where the pro-oocyte is located. In stage 1 and early stage 2 egg chambers, it accumulates at the anterior of the oocyte, near the ring canals. It also extends through the ring canals forming a branched structure that links the early oocyte with adjacent nurse cells. In stage 3 cysts, it accumulates at the posterior cortex and localizes to extensions that pass through the oocyte into the nurse cells. Through stages 4 to 7, it continues to be somewhat enriched at the posterior cortex of the oocyte, but at significantly lower level. In stage 9 to 10 egg chambers, it is found throughout the cytoplasm of the oocyte and nurse cells, with slight enrichment at the oocyte cortex.1 Publication

Gene expression databases

BgeeiFBgn0041164.
ExpressionAtlasiQ6J5K9. differential.
GenevisibleiQ6J5K9. DM.

Interactioni

Subunit structurei

Forms a complex with piwi and fs1Yb; this interaction is required for proper piRNA loading and nuclear localization of piwi. The interaction of piwi and fs1Yb is likely to occur via armi.

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi63920. 1 interactor.
IntActiQ6J5K9. 7 interactors.
MINTiMINT-8075720.
STRINGi7227.FBpp0100102.

Structurei

3D structure databases

ProteinModelPortaliQ6J5K9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi862 – 865DEAG box4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1804. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00800000124068.
InParanoidiQ6J5K9.
KOiK18432.
OMAiNFRNYDR.
OrthoDBiEOG091G03T8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR026127. SDE3.
PANTHERiPTHR10887:SF416. PTHR10887:SF416. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.

Sequencei

Sequence statusi: Complete.

Q6J5K9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTYVSKFFT NPDRNREDIL ESLDRENSFL DQKLMEEKMD QQLKANPNEI
60 70 80 90 100
NGVLSNKIAE LTHGLSEMDV SKESSCTARK GVITSLDGDR GVIDKDVLFE
110 120 130 140 150
TKVAEDIILD LHVGCVVEYL TFTTGEAMRV VKVKSILEHS WEDTSQKEIE
160 170 180 190 200
KAVDNLKNEK PTFFNTETRS VLGLISQRLA SSIDVETEYG QLTVELDNIE
210 220 230 240 250
MNFIPTNGDR VRLECNIQLD DGFVDKQGEI LEVTKLFPTR IQEGEKCIVE
260 270 280 290 300
RVYVHMVVLG PETYILKTDL PTGTDLHLGD IVLADLIECQ YSKFTRRAIK
310 320 330 340 350
ITPLEKNFGA TKLTQQSSMG SSGSGKAVTV TGVNRFITAE LWQKESVSLK
360 370 380 390 400
LTNNLNRTLR LESITVCNDS ESQLSVVSPL ESKEISSGSE ITVTFEIHTQ
410 420 430 440 450
FLGEAIEKYV LNFDLLKVRR VFTVIVCKTK EEVAEAEKRM IAAEALMAPG
460 470 480 490 500
RNSQERSRFY ANQVWCNKVD VIPGQQIVTK RRFVALRLGC FEVPKELRQI
510 520 530 540 550
CLTSERRQEM IKAIEQHYSF LTEPLSIKTY MHRFRLLLHL EEIECFVNFR
560 570 580 590 600
NYDRDRAHFL RDGEFLTLQI ENLAERRPSL VIGDTLRVIN PWSDPDSQTT
610 620 630 640 650
KSYEGIIHKV LFDRILLKFH SSFQEKYNGE DYRLEFYFSR YSFRKQHHAI
660 670 680 690 700
SKIVGVMGED FLFPSKVTKR ENPQLDVYMK DDDMYLYDSK LEWYNQSLNS
710 720 730 740 750
IQKRAVFNIL RGEAENIPYV LFGPPGSGKT MTLIETLLQL VRNLPGARIL
760 770 780 790 800
VGTPSNSSAD LVTKRLIDSK ALLQGDFIRL VSYNQVEKDL IPPEIMSYCA
810 820 830 840 850
TSDVGAVGSC EDKMMVTESG LKLRCQAKFI GTHRITISTC TTLGNFLQLG
860 870 880 890 900
FPAGHFTHVL FDEAGQCTEP ETMVPIVMLT KKRSQVVLSG DPRQLQSIVT
910 920 930 940 950
SRIASKMGFS ISFLERLLER SPYRKDLQRF PESSGYNPLV LTKLLYNYRA
960 970 980 990 1000
LPSIMSIYSR LFYDDELIPV LSEKDSRESR LLSKLRCVFE SEKDIPQAHG
1010 1020 1030 1040 1050
TFFYGIIGEN RQNNDSPSWF NPQEVREVFL MTIALYRANV TADQIGIITP
1060 1070 1080 1090 1100
YQKQVKMLRS MFIGTDVVMP KIGSVEEFQG QERDIILIST VRSSEEILRM
1110 1120 1130 1140 1150
DARFSLGFVR CSKRLNVAVS RARAMMIIFG NPHLLAVDEC WRQLILFCVK
1160 1170 1180
NNAYFGCDLP QMVINQKDEV PVCLETFVPS LNTTDDLN
Length:1,188
Mass (Da):135,658
Last modified:July 9, 2014 - v4
Checksum:iBA1D8F4305825B0A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti522T → K in AAT12000 (PubMed:15035984).Curated1
Sequence conflicti527I → V in AAT12000 (PubMed:15035984).Curated1
Sequence conflicti905S → L in AAT12000 (PubMed:15035984).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY598469 mRNA. Translation: AAT12000.1.
AE014296 Genomic DNA. Translation: AAF47775.2.
AE014296 Genomic DNA. Translation: AAX52729.1.
RefSeqiNP_001014556.1. NM_001014556.3.
NP_647816.2. NM_139559.4.
UniGeneiDm.15753.

Genome annotation databases

EnsemblMetazoaiFBtr0100641; FBpp0100102; FBgn0041164.
FBtr0309841; FBpp0301575; FBgn0041164.
GeneIDi38427.
KEGGidme:Dmel_CG11513.
UCSCiCG11513-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY598469 mRNA. Translation: AAT12000.1.
AE014296 Genomic DNA. Translation: AAF47775.2.
AE014296 Genomic DNA. Translation: AAX52729.1.
RefSeqiNP_001014556.1. NM_001014556.3.
NP_647816.2. NM_139559.4.
UniGeneiDm.15753.

3D structure databases

ProteinModelPortaliQ6J5K9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63920. 1 interactor.
IntActiQ6J5K9. 7 interactors.
MINTiMINT-8075720.
STRINGi7227.FBpp0100102.

Proteomic databases

PaxDbiQ6J5K9.
PRIDEiQ6J5K9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0100641; FBpp0100102; FBgn0041164.
FBtr0309841; FBpp0301575; FBgn0041164.
GeneIDi38427.
KEGGidme:Dmel_CG11513.
UCSCiCG11513-RA. d. melanogaster.

Organism-specific databases

CTDi38427.
FlyBaseiFBgn0041164. armi.

Phylogenomic databases

eggNOGiKOG1804. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00800000124068.
InParanoidiQ6J5K9.
KOiK18432.
OMAiNFRNYDR.
OrthoDBiEOG091G03T8.

Miscellaneous databases

GenomeRNAii38427.
PROiQ6J5K9.

Gene expression databases

BgeeiFBgn0041164.
ExpressionAtlasiQ6J5K9. differential.
GenevisibleiQ6J5K9. DM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR026127. SDE3.
PANTHERiPTHR10887:SF416. PTHR10887:SF416. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiARMI_DROME
AccessioniPrimary (citable) accession number: Q6J5K9
Secondary accession number(s): Q59E56, Q9VZP4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 9, 2014
Last modified: March 15, 2017
This is version 104 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.