ID   SRRT_CAEBR              Reviewed;         715 AA.
AC   A8XEG9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Serrate RNA effector molecule homolog;
DE   AltName: Full=Arsenite-resistance protein 2 homolog;
GN   ORFNames=CBG12064;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and
CC       the primary microRNAs (miRNAs) processing machinery. Contributes to the
CC       stability and delivery of capped primary miRNA transcripts to the
CC       primary miRNA processing complex, thereby playing a role in RNA-
CC       mediated gene silencing (RNAi) by miRNAs (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
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DR   EMBL; HE601540; CAP31104.1; -; Genomic_DNA.
DR   RefSeq; XP_002646350.1; XM_002646304.1.
DR   AlphaFoldDB; A8XEG9; -.
DR   SMR; A8XEG9; -.
DR   STRING; 6238.CBG12064; -.
DR   PRIDE; A8XEG9; -.
DR   EnsemblMetazoa; CBG12064.1; CBG12064.1; WBGene00033072.
DR   GeneID; 8588347; -.
DR   KEGG; cbr:CBG_12064; -.
DR   CTD; 8588347; -.
DR   WormBase; CBG12064; CBP17383; WBGene00033072; -.
DR   eggNOG; KOG2295; Eukaryota.
DR   HOGENOM; CLU_008560_1_1_1; -.
DR   InParanoid; A8XEG9; -.
DR   OMA; FYRRGWA; -.
DR   OrthoDB; 525905at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_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.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..715
FT                   /note="Serrate RNA effector molecule homolog"
FT                   /id="PRO_0000385227"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  81592 MW;  AA80DE16A4E2F221 CRC64;
     MDSDDDGDRR RDKFARERRD DDSYRRSGGG GGGYSRYDNK RPAGRREDYQ VKRSRGDEGD
     DGFDPVRGDR NGNGAEPSSE NSIYSGPLLP FKRFLTNQED DISEEDAIKK YNEYKNEHRK
     FQLDRFFRAH KDEEWFRLKY KPEEAKKVKE VQLENVQKRL QIFNELKEQG QFDKFTLDFE
     DAEAILRMLD SVVVKLENGS EDDLKAVLAQ KLDDESLADV KKENKDAAEK VEDQVKDEVK
     EEPNEEQEEG AIDDETDKAS NKVNIHKTCS VFLRNIPPGL TYEELESTCK KYPGFLRLAL
     TDGIAERRFY RRGWATFKRD VNIKEICWGL NAHRLRETDL NAIINRDITR RVRTNNGVAA
     HKQVALNDLK LAVKLTALYD KKLGLFNAAD ESESDREKDI RMGVDLVAAS TNPLVKEIKS
     IVPKDTLNDI SEEEAELLGV SNGGDSQSDK VRYERDDTIL KALDLLIIYL RIVHSIDFYN
     HGHYAQEDSM PNRCGLIHVR GQPPSGASIN TDENGDLIVP QKFINDFISG FNSRIDKGLI
     EKQYVSEEDM EKMGKKDGEK EVEAFIAINT VELAKDKWLC PLSGKKFKGP EFIRKHLQSK
     HEDKLEEARA EADFFNNYLA DAQRPVDLEP KHMPHMSRDD HRGGGGDRGY GRERDDDRGP
     GGGRSSFGNG SYDRRPPFPP RHSLGGRGGG GRMFDDAPRR QPVSYRDLDA PDDIP