A2QX45 (DCL22_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dicer-like protein 2-2

Including the following 2 domains:

1. Endoribonuclease dcl2-2
   EC=3.1.26.-
2. ATP-dependent helicase dcl2-2
   EC=3.6.4.-

Gene names

Name:	dcl2-2
ORF Names:	An11g07590

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	1362 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons By similarity.
Sequence similarities	Belongs to the helicase family. Dicer subfamily. Contains 1 Dicer dsRNA-binding fold domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 2 RNase III domains.
Sequence caution	The sequence CAK40801.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Antiviral defense
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Antiviral protein Helicase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	RNA processing Inferred from electronic annotation. Source: InterPro defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW regulation of defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease III activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1362	1362	Dicer-like protein 2-2		PRO_0000306788
Regions
	Domain	30 – 197	168	Helicase ATP-binding
	Domain	343 – 505	163	Helicase C-terminal
	Domain	536 – 630	95	Dicer dsRNA-binding fold
	Domain	889 – 1033	145	RNase III 1
	Domain	1075 – 1258	184	RNase III 2
	Nucleotide binding	43 – 50	8	ATP By similarity
	Motif	139 – 142	4	DEAH box

Sequences

	Sequence		Length	Mass (Da)
	A2QX45 [UniParc]. Last modified October 2, 2007. Version 2. Checksum: D233E94793C21EB3	FASTA	1,362	153,885
	10 20 30 40 50 60 MTSSTDYHAD STPGTTSNME LRIREYQLEM LNESLKRNLI VVMPTGTGKT QVAILRILAD 70 80 90 100 110 120 IDKGNSDKFV WLLCPTVALS EQQYIQYATV FLPSGAEDKA IWDNALSGIK IAVSTYQVLY 130 140 150 160 170 180 DALSHGFVKL SQMSLLIFDE AHHCKKDHVA NKIMQVHYHK QHQSGVQNLP KILGLTASPI 190 200 210 220 230 240 LSDLSSLEIV ESNLGSICKT PRQYYAQLLQ FTNRPLILPR LPTYTIPNCS VKAPILEKLC 250 260 270 280 290 300 GILSSEDEVP SSSKMKSKQL KHIRRFMQTS ESINQELGIW AATEYMRKSI MHFKESMRMG 310 320 330 340 350 360 AEKTNISNYG KDFAMEILTR LGKLQDCSPA IQPEEISPMC QCLLDELSKA YREGFCGLVF 370 380 390 400 410 420 VTQRATVLAL KWLIENHPLT SHLFTCGTFI GMSTTQYSKT ELGNLHDIRN QTETLEKFRQ 430 440 450 460 470 480 GSLNLIITTD ALEEGIDVPA CNTVLNFNCQ LSLKSFIQRR GRARRENSQF IIIMEDESGP 490 500 510 520 530 540 RYLKRLEMEE IELVQKLQNA ERRQIPANEL DFDKYERISL SLDIDRTGAQ LIMREAVGYL 550 560 570 580 590 600 YNFCSKLPAQ LYVSNKPLFT YERNNYGRFR AVVKLPSNLD PSLQSFSSSR SWSRLKYARE 610 620 630 640 650 660 DAALQAYKAL YQAGLVNDYL VPTQVSDHLE GDIIFRSHYS IQNQLDPWQD IALLWKLDSQ 670 680 690 700 710 720 LYAHNLRIIR PEEDEIHLHM ILPTQLDTTI HIPLFIDYCT TYTAILTPGH PITTDISLCQ 730 740 750 760 770 780 QVTNLIFQSV YRDHCSRRNL DYAFLLVPEL EETKLIEFLE RYSGSVSLTE LLNQEATPSA 790 800 810 820 830 840 LGLLRSHTRP SRPLLVEPWV AGECFLPDEL SISSFDAKVK YMTNRRNFLS HGNLAAGKST 850 860 870 880 890 900 NCEARIGLEA NVKSMSVRDF FVDKLPSMFA QVALFTPSIS HEVEVYMIAQ ILRQELSLRS 910 920 930 940 950 960 VTPWQRIDLL AIAIRPTSIE HRATFRLLAF IGDAFMKYLF AMQLFLHHHL WHEGLLSSLK 970 980 990 1000 1010 1020 QRNLSDAGLA HAIHQSGLGK FLISKHLNGK RWVPPLVSGI EPASNEARQR SIGAATLADM 1030 1040 1050 1060 1070 1080 TKAVVGAAFT DGGLNQAAAC ASVMFPKLKS WNASSLHDGT YSKTRPENAV ASTAIVDMEE 1090 1100 1110 1120 1130 1140 LLGYTFTDKS LAVESMTHPS CTGLVQTTSY RRLSFLGASV LEWIVVSYLH RHAQVMNPQR 1150 1160 1170 1180 1190 1200 MQSLKSAFTN NTFLTFIAIT FHQVREQNHI DVDDEHNVHK NVTTCSIRLW DFLRLHSDAL 1210 1220 1230 1240 1250 1260 STELSDFVQK SSEKADAIKH ELWEQRFYPW VRLRALGDMR VLSDIIQSIF GAVFIDSQAT 1270 1280 1290 1300 1310 1320 LASCDALAEK LGIVPLLEHF ISHQITTDHP KDTLQAILPG RKVSYQICVD KVHPGTLRCS 1330 1340 1350 1360 ALADSSEIAS VEGQMNDEVI KMQAAETAVR LLRKGFALSE TS

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270243 Genomic DNA. Translation: CAK40801.1. Sequence problems.
3D structure databases
ProteinModelPortal	A2QX45.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1111.
HOGENOM	HOG000129941.
OrthoDB	EOG45MRG9.
Family and domain databases
Gene3D	1.10.1520.10. 3 hits.
InterPro	IPR005034. Dicer_dsRNA_binding_fold. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000999. RNase_III_dom. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF03368. dsRNA_bind. 1 hit. PF00271. Helicase_C. 1 hit. PF00636. Ribonuclease_3. 2 hits. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00535. RIBOc. 2 hits. [Graphical view]
SUPFAM	SSF69065. RNase_III. 2 hits.
PROSITE	PS51327. DICER_DSRBF. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS00517. RNASE_3_1. False negative. PS50142. RNASE_3_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCL22_ASPNC

Accession

Primary (citable) accession number: A2QX45

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 2, 2007
Last modified:	May 1, 2013
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program