SRRT_DROGR
ID SRRT_DROGR Reviewed; 1011 AA.
AC B4J497;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GH20949;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916367; EDW00577.1; -; Genomic_DNA.
DR RefSeq; XP_001985710.1; XM_001985674.1.
DR AlphaFoldDB; B4J497; -.
DR SMR; B4J497; -.
DR STRING; 7222.FBpp0154855; -.
DR PRIDE; B4J497; -.
DR EnsemblMetazoa; FBtr0156363; FBpp0154855; FBgn0128411.
DR GeneID; 6560148; -.
DR KEGG; dgr:6560148; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; B4J497; -.
DR OMA; HLRMCEE; -.
DR PhylomeDB; B4J497; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
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; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..1011
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385218"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..953
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 284..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1011 AA; 114437 MW; 17068B32308FCF3F CRC64;
MAESDDEYDR KRRDKFRGER DSYRPERRDD RRPMGGGAGN ARDEWAERNP FRGSAAAGGG
GGGGGVGGGG GARHRPDYSD YRGSGPRPRY GSPGREMPPA KRMRPDWGDG EMRANPRFGY
DPYLVQAWND HYQSLHSAYS HSGHAPSARE PPPSGISNSD TQTQPAMLTL KQFLDTQDEN
ISDSEVMRKY TEYKTDFKRQ QLNEFFVAHK DEEWFKNKYH PEDSVRRSDE QRGFLKRRTD
VFLELLNNGT ISNVKVDSSQ ADALVRVLDT CVIKLEGGTD EDLKILDEKP KDPAPVYERR
SERSERSEAT ESVVVTKREP ESPKHQTKSE KDDDDLPEVE SPQRKNVRPV NSDDEDWDDD
EEMPAAKSEQ QSELAAEKPA KQLNDEESMQ ANIDKNQKKS KKRKRTSSDD ESSSSSSSES
DSDSDDEKLI EKYDVEEGLR ADQKAEAEKD KEEEEERAAT AAAKAKQLPP DSPTPDEDVD
AAAVEEQKNE VVAIKTEVND EESQKTEQPA AEEEKSEQPK DDPEASSKNG EENEEEKAEK
SEADTATTKA AAAAADDDAM TETIDVDKLK DSLKPRALHR TSSIFLRNLA PSITKAEIET
ICTRFSGYLR VAIADPLVER RWYRRGWITF TRDVNIKEIC WSLNNQRLRD CEMGAIVNRD
LSRRVRPANG ITAHKQIVRS DIKLCAKIAM NLDERFKLWS EVDNADNAEL NPEELKEATN
GSGSYGFNSK NPVLQNITDY LIEEASAEEE ELLGLAGDSK DGEGEPIERD EPLIQVLDRL
VLYLRVVHSV DYYNHCEYPY EDEMPNRCGI IHARGPAPMR VTSNDVQEYI KSYEGKLQQF
LAKTVQLSDE NIKELGAKNP EKEVEKFVQA NTQELAKDKW LCPLSGKKFK GPEFIRKHIF
NKHEEKVDEV RKEVQYFNNY LRDPKRPQLP EHPGSSKRTE SESGRGSGGY RPPMYPPFSA
MPYGFAPPMM GGGGRGGRNF PQARREMPVE HQRRLIGYHD LDAPVNSDMF D
