SRRT_DROYA
ID SRRT_DROYA Reviewed; 944 AA.
AC B4NYV0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GE19427;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000157; EDW89801.1; -; Genomic_DNA.
DR RefSeq; XP_002090089.1; XM_002090053.2.
DR AlphaFoldDB; B4NYV0; -.
DR SMR; B4NYV0; -.
DR STRING; 7245.FBpp0264437; -.
DR EnsemblMetazoa; FBtr0265945; FBpp0264437; FBgn0236770.
DR GeneID; 6529076; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR OMA; HLRMCEE; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; B4NYV0; -.
DR Proteomes; UP000002282; Chromosome 2L.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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; 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.
PE 3: Inferred from homology;
KW Nucleus; Phosphoprotein; RNA-mediated gene silencing.
FT CHAIN 1..944
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385226"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 944 AA; 107503 MW; 6675E7D64691696E CRC64;
MADSDDEYDR KRRDKFRGER SDSYRTERRD DRRAVGGSTG ARDEWAERNP FRGGASAGGG
GARHRPDYSD YRGPGARPRY GSPGRDLPPA KRMRPDWGDG DVRANPRFGG YDPYLMQAWN
DHYQSMHSAF SHAGHAPPVR ESIGGGGSDT LTQPAMLNLK QFLDTQDENI SDSEVMRKYT
EYKTDFKRQQ LNEFFVAHKD EEWFKNKYHP EDSVKRSEEQ RGFLQRRTDV FVELLENGTI
GSVKVDSSQG DALIRVLDTC VIKLEGGTDE DLKVLDEKPK DLVVYERKTE PMESVKAMEK
AISSPKEEKI REEDPLPAVV SPQQKTARSV NSDEENWNDE DAVTKKDLGE HSKDTDSKPE
DKQLNKKKTK KRKRNSSDDD SSSSESSSSS DEEKLKEKYD VEDGLRAEQK AEAEKDRQEA
AKAKQEPESS KLEELVGKEI TEPKELDSKI NTVENDDTLK SPEMTPNPIK RTDNGNGNKV
EDEEKPSVDE NKVVETETID LDKIKDGQPR ALHRTSSIFL RNLAPSITRA EIEAVCNRFT
GYLRVAIADP LVERRWYRRG WITFMRDVNI KEICWGLNNQ RLRDCEMGAI VNRDLSRRVR
PANGLTAHKQ VVRSDIKLCA KIALNLDERF RLWAEVPTDD SNSARADESS ENGSGSTYGF
NSKNPVLQNI TDYLIEEASA EEDELLGLTG ENKDTEGEAI ERDEQLISVL DRLVLYLRIV
HSVDYYNHCE YPYEDEMPNR CGIIHARGPA PVRVTNNDVQ EYIKTYESKL QQFLTKTVLL
SDEEIKDLGA KDAETEVEKF VQANTQELAK DKWLCPLSGK KFKGPEFIRK HIFNKHDEKV
DEVRKEVQYF NNYLRDPKRP QLPEHPGTSK RPESESARGG GGGYRPPMYP PFSAMPYGFG
PPMMGGGRGG RNFPPARREL PLEHQRRLIG YHDLDAPANS DMFD
