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Database: UniProt
Entry: W8AP59_CERCA
LinkDB: W8AP59_CERCA
Original site: W8AP59_CERCA 
ID   W8AP59_CERCA            Unreviewed;       867 AA.
AC   W8AP59;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Serrate RNA effector molecule homolog {ECO:0000256|ARBA:ARBA00017364};
DE   AltName: Full=Arsenite-resistance protein 2 homolog {ECO:0000256|ARBA:ARBA00030701};
DE   Flags: Fragment;
GN   Name=SRRT {ECO:0000313|EMBL:JAB90560.1};
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB90560.1};
RN   [1] {ECO:0000313|EMBL:JAB90560.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Geib S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB90560.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA   Calla B., Hall B., Hou S., Geib S.M.;
RT   "A genomic perspective to assessing quality of mass-reared SIT flies used
RT   in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT   California.";
RL   BMC Genomics 15:98-98(2014).
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   EMBL; GAMC01015995; JAB90560.1; -; mRNA.
DR   AlphaFoldDB; W8AP59; -.
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   GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR   CDD; cd00590; RRM_SF; 1.
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   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          28..137
FT                   /note="SERRATE/Ars2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12066"
FT   DOMAIN          673..840
FT                   /note="SERRATE/Ars2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04959"
FT   REGION          171..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB90560.1"
SQ   SEQUENCE   867 AA;  98996 MW;  05C0CC7411CDED05 CRC64;
     GHNHAPHASR EAPSSGDLQT QPAMLTLKQF LDTQDDGISD SEVLRKYSEY KIEFKRQQLN
     EFFVAHKDEE WFKNKYHPAD SVKRKEEQLN FLKKRVDVFN ELLVNGQVKA VSIDTSQTDP
     LLRLLDTVVI KLEGGTDDDL KILDEKPREY TFPERSFDKK PQHDDDVIIT SVGKKRNEDD
     EPKVVSPRPI RRAPLSDDEE NWDDDDAGDN KVTTDKGDVK KDHSDEEDKS DEEEKGRDKK
     SLKRKRTSSE SSSSSSSDSD SSSSSSSDEE DDEKVKDKYD LGRVKEEKDA EKNVADDVKE
     KEDVDKTIDA PQDKEVASVE NNLNGESEKE SQLSQNGMIL NEKAENSSEQ KDGEAEAEGE
     KDDSEKIAEP VPRDDDMKEA TFNNNNPKSE DAKEDKPDSN ERDEKEVDLE KKEINEPEDQ
     PETIDLDKVK DGPQPRALHR TSSIFLRNLA PSITKAEIET LCQRFDGYLR VAIADPLVDR
     RWYRRGWVTF KRDVNIKEIC WNLNNTRLRD CEMGAIVNRD LSRRVRPVNG MTAHKTIVRS
     DIKLCAKIAM NLDERFKLWD KNNQKNTEQT AENSKGNGDA AASYGFKSNN PVLQNITDYL
     IEEASAEEDE LLGISGENKE SEGEMIERDV QLISVLDSLI LYLRIVHSVD FYNHCEYPYE
     DEMPNRCGII HARGPPPSKV QANDIQDYIK NFESKMQTFL TKTTPIDDEE LKNLGSKDAE
     AEVEKFVQAN TQELAKDKWL CPLSGKKFKG PEFIRKHIFN KHTEKVDEVR KEVEFFNNYL
     RDPKRPQLPE HASSSKRTTS ESGGLGYRPS VYPPAFMPPY AAYAPPMMVP GRGGRGFGPG
     RRPPNKYRQL TQYRDLDAPQ EPVDIFN
//
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