SRRT_DROMO
ID SRRT_DROMO Reviewed; 980 AA.
AC B4KLY7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GI21286;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and
CC RNA-mediated gene silencing (RNAi). Involved in innate immunity via the
CC short interfering RNAs (siRNAs) processing machinery by restricting the
CC viral RNA production. Also involved microRNA (miRNA)-mediated silencing
CC by contributing to the stability and delivery of primary miRNA
CC transcripts to the primary miRNA processing complex containing drosha
CC and pasha (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
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DR EMBL; CH933808; EDW10776.1; -; Genomic_DNA.
DR RefSeq; XP_002006841.1; XM_002006805.2.
DR RefSeq; XP_015020083.1; XM_015164597.1.
DR AlphaFoldDB; B4KLY7; -.
DR SMR; B4KLY7; -.
DR STRING; 7230.FBpp0170503; -.
DR EnsemblMetazoa; FBtr0172011; FBpp0170503; FBgn0144016.
DR EnsemblMetazoa; FBtr0422115; FBpp0380201; FBgn0144016.
DR GeneID; 6581083; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; B4KLY7; -.
DR OMA; HLRMCEE; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; B4KLY7; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:EnsemblMetazoa.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0030422; P:siRNA processing; IEA:EnsemblMetazoa.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR PANTHER; PTHR13165; PTHR13165; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 3: Inferred from homology;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..980
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385219"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 980 AA; 110954 MW; 8F72CC0224EB34A0 CRC64;
MADSDDEYDR KRRDKFRGER DSYRPERRDE RRPMGGAANS RDEWSERNPF RGSSAAGGGG
GGGGARHRPD YSDYRGSGPR ARYGSPGREM PPAKRMRPDW GDSEMRSNPR FGYDPYLVQA
WNDHYQSLHS AYSHAGHGPS VRETGPAGGG GVSGDTQTQP AMLTLKQFLD TQDENISDSE
VMRKYTEYKT DFKRQQLNEF FVAHKDEEWF KNKYHPEDSV RRSEEQRGFL KRRTEVFLEL
LENGTIGSVK VDSSQADALV RVLDTCVIKL EGGTDEDLKI LDEKPKDPPI VYERKSETTE
SAVVAKREPE SPKTEKDDDL PGASSPQHKS LRPVNLDEEN WDEDEPMEVH PQTGKDGEKS
DDRRSKEPED EESVKSDNEK KLKKKKIKKR KRNSSDDDSS SSSSSDSDTE SDDEKVKAKY
DVEEGLRADQ KAEALKDKEE AATAAKEKLL APESPQPEDV VDPKEALEIK SEASEESKQD
KTEQPVGQTE RPTTDNPAEK NGEEEGAKAE DKPEAGTQES TANEVTETID LDKVKDGPHP
RALHRTSSIF LRNLAPSITK AEIEAICKRF SGYLRVAIAD PLVERRWYRR GWITFTRDVN
IKEICWSLNN QRLRDCEMGA IVNRDLSRRV RPANGITAHK QIVRADIKLC AKIAMNLDDR
FKLWCDSNRS DAEDAEKKAG QEATNGSGAS SSPSYGFNSK NPVLQNITDY LIEEASAEEE
ELLGLAGDNK DGDGEPIERD ESLISVLDRL VLYLRIVHSV DYYNHCEYPY EDEMPNRCGI
IHARGPAPMR VTSNDVQEYI KAYDGKLQQF LTKTVQLSDE EIKELGAKNP ETEVEKFVQA
NTQELAKDKW LCPLSGKKFK GPEFIRKHIF NKHEEKVEEV RKEVQYFNNY LRDPKRPQLP
EHPGSSKRTE SESGRGSGYR PPMYPPFSAM PYGFAPPMMG GGGRGGRNFP PVRREMPLEH
QRRIIGYHDL DAPINSDMFD
