SRRT_DROPE
ID SRRT_DROPE Reviewed; 951 AA.
AC B4H732;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=GL11804;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479216; EDW33565.1; -; Genomic_DNA.
DR RefSeq; XP_002026596.1; XM_002026560.1.
DR AlphaFoldDB; B4H732; -.
DR SMR; B4H732; -.
DR STRING; 7234.FBpp0175911; -.
DR EnsemblMetazoa; FBtr0177419; FBpp0175911; FBgn0149413.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR OMA; HLRMCEE; -.
DR PhylomeDB; B4H732; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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..951
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385220"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..893
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 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 951 AA; 107855 MW; 87E4271186A525BA CRC64;
MADSDDEYDR KRRDKFRGER ESYRTERRDE RRPIGGAGGG RDEWSERNPF RGGGAGGGGA
PRHRPDYSDY RGPGPRARYG SPVRDMPPPK RMRSDWGDGD GRPGPRYGGY DPYLMQAWTD
HYQSMHSAYH HASHPPPVRE LPIIGGDTLT QPAMLNLKQF LDTQDENISD SEVMRKYTEY
KTDFKRQQLN EFFVAHKDEE WFKNKYHPED SVNRSEEQRG FLRRRTDVFV ELLENGTIGS
VKVDSSHGDA LIRVLDTCVI KLEGGTDEDL KVLDEKPKEA LVFDRKPESV DPTTVVENTP
KSPKKEKEED ELPLIVSPQR IALKPVNSDD ENWDDAEVED APPKKPEEEE PKESEPIPEI
KQKQKKEKKK KIKKRKRNSS SDEESSSSES ESSSSSSEEE EEDDEKLKAK YDVEDGLRAE
QKAEAEKDQA EAAKAKLGSV SPKEEISPEK SAADPEVEGE AKEDGKQAEK SPKSDDEKKQ
ENGDAAKVES AAEPATGDAQ GEVKPVTIDL DKVNPPRDMH RTSSIFLRNL APSITKAEIE
ALCSRFSGYL RTAIADPLVE RRWYRRGWIT FTRDVNIKEI CWSLNNQRLR DCEMGAIVNR
DLSRRVRPAN GITAHKQVVR SDIKLCARIV MNLDEKFKLW SEGPLSKPSP ASDSEATAAN
GSGSSYGFNS KNPVLQNITD YLIEEASAEE EELLGLSGDR KDGEGEPIER DEQLLSVLDR
LVLYLRIVHS VDYYNHCEYP YEDEMPNRCG IIHARGPAPS RVTSNELNEY IKSYEGKLLQ
FLTKTALLSE DQIKDLGAKN ADTEVEKFVQ ANTQELAKDK WLCPLSGKKF KGPEFIRKHI
FNKHEEKVDE VRKEVQYFNN YLRDPKRPQL PEHPGSVKRP ETESVRGPGG YRPPMYTPMS
GMPYSFGGHM MGGGRGGRHF PPARRELPLE HHRRLVGYHD LDAPSNSDIF D
