ID A0A1I8MJV3_MUSDO Unreviewed; 959 AA.
AC A0A1I8MJV3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Serrate RNA effector molecule homolog {ECO:0000256|ARBA:ARBA00017364};
DE AltName: Full=Arsenite-resistance protein 2 homolog {ECO:0000256|ARBA:ARBA00030701};
GN Name=101895569 {ECO:0000313|EnsemblMetazoa:MDOA005680-PA};
GN Synonyms=LOC101895569 {ECO:0000313|RefSeq:XP_005188622.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA005680-PA};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA005680-PA}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA005680-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005188622.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005188622.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025002}.
CC -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha.
CC {ECO:0000256|ARBA:ARBA00011796}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARS2 family.
CC {ECO:0000256|ARBA:ARBA00005407}.
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DR RefSeq; XP_005188622.1; XM_005188565.3.
DR EnsemblMetazoa; MDOA005680-RA; MDOA005680-PA; MDOA005680.
DR GeneID; 101895569; -.
DR VEuPathDB; VectorBase:MDOA005680; -.
DR OrthoDB; 4174205at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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; ARSENITE-RESISTANCE PROTEIN 2; 1.
DR PANTHER; PTHR13165:SF0; SERRATE RNA EFFECTOR MOLECULE HOMOLOG; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905}.
FT DOMAIN 151..260
FT /note="SERRATE/Ars2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12066"
FT DOMAIN 763..904
FT /note="SERRATE/Ars2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04959"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 109468 MW; 18A118F1946FB2C5 CRC64;
MADSDDEYDR KRRDKFRGER SSGDSYRSER RDDRRTGAGS AGGGRDDWPE RGGASGRPRP
DYRDYRGARD RYSPDREMPP AKRMRPGWGD DLRANHRYGP YDPYLLHAWN EHYAAHSLHS
AYGAGLSHGA HPRESAANSD MQTQPAMMTL KQFLDTQDDG ISDTEVLRKY NEYKLEFKRQ
QLNEFFVAHK DEEWFKNKYH PVDSVKRKDE QLNFLKKRVE VFEELLQNGM IQSVTVDTNQ
TDPLLRVLDT VVIKLEGGTD EDLKILDEKP KEASYPERIF DKKGDDDDVI ITSVEKKDDD
EPKCVSPKAT RRHSGSDNEE NWDDDSKSKK GEKKKKSLKR KRTSSDSSSS SSSDSDSSSS
SSSSEDEADD KVKSKYDLDD VKEDTKEEEE EENKEKNAEE PEKVKSADEE TEKKADSDNE
EKKLLENGSE EKEDLKEETE TKSNGNDADG DAKMEEGEEN KKEEEXEQKP DVKNDEEDEK
KEAVETETSA EDKKAIDDEQ PETIDLDKVK DGPQPRALHR TSSIFLRNLA PSITKSEIEA
VCQKFDGFLR VAIADPLVER RWYRRGWVTF KRDVNIKEIC WNLNNTRLRD CEMGAIVNRD
LSRRVRPVNG MTAHKTVVRA DIKLCAKIAM NLDEKFRLWQ SSNAESKGEG GSGENNSTAE
NTTDAHNTSN SSTYGFKTNN PVLQNITDFL IEEASAEEEE LLGISGENKE SEGEAIERDP
QLISVLDNLI LYLRIVHSVD FYNHCEYPYE DEMPNRCGII HARGPPPSKV SQNDIQDYIK
NFENKMQTFL AKTTTIEEEE LKNLGAKDAE NEVEKFIQAN TQELAKDKWL CPLSGKKFKG
PEFIRKHIFN KHGEKVEEVR KEVEFFNNYL KDPKRPQLPE HPGNNKRTTS ESSGGYRAPV
YPPAAYAPPY AAYAPPLMIP GRGGRGFGGP GRRDLPIEHQ RRIIGYHDLD APANFDMFD
//
