SRRT_ANOGA
ID SRRT_ANOGA Reviewed; 967 AA.
AC Q5TUF1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2 homolog;
GN Name=Ars2; ORFNames=AGAP010382;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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 (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; AAAB01008849; EAL41034.3; -; Genomic_DNA.
DR RefSeq; XP_559074.3; XM_559074.3.
DR AlphaFoldDB; Q5TUF1; -.
DR SMR; Q5TUF1; -.
DR STRING; 7165.AGAP010382-PA; -.
DR PaxDb; Q5TUF1; -.
DR PRIDE; Q5TUF1; -.
DR GeneID; 1272662; -.
DR KEGG; aga:AgaP_AGAP010382; -.
DR CTD; 1272662; -.
DR VEuPathDB; VectorBase:AGAP010382; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; Q5TUF1; -.
DR OMA; HLRMCEE; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; Q5TUF1; -.
DR Proteomes; UP000007062; Chromosome 3L.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
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: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; 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; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..967
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385215"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 109612 MW; 38C31455B7A5F8CC CRC64;
MGDSDDEYDR KRRDKFRGER SAGGGGDSYG RGADRPDRSR GRDDWPDRVR PRQDYRDYRP
PPRDRGYSPA REGPTVKRMR GDTWGDEGRH RFGAHDGYGM YGYAHDHFGM HPTVGPYGHQ
HATHQREPVV SGDMQTQPCM MTLKQFLATQ DDSISDSDAI TKYNEYKLEF RRQQMNEFFV
AHKDEEWFKI KYHPEESQKR KEEQLSFLKR RCEVFLELLK SKEIGKVSVD ASNTDALLRL
LDTVVIKLEG GTEEDLKVLD IKPSVVEAAA RTPATLNEEK VKTESKVDAT AKELAVKMEE
DSSKQETETD VLSVPQSEED ARNGNSKIKE ELSKSMDDGN ENGDKSKSND AQKSEKEIAE
VEHEAHKHES EDRKKRSRSD SGSSSSSSSS SSSSESEEEK DERMNKEDNE DEENMRIPEE
EKKSDSADTM DNINRDKEVD EGKPVCDAED LNTADDRDDN ADQNKEQNEF EETTKDKNSS
DPVNDENKEN SDKKSQQEGD SKAETIDLAK DPADGGSRAL HRTSSIFLRN LAPSITKAEV
EAMCRRYNGF LRVAIADPLL ERRWFRRGWV TFKREVNIKE ICWNLNNIRL RDCELGAIVN
KDLSRRVRPV NGITCHKTVV RSDIKLGAKI AHNLDDKWGL WKETPTAASG TGEAGDKNGS
EVQPEESFGL QSKNPVLQNI TDYLIEEASA EEEELLGLSE DSKKVSEGEL IERDPQLIEV
LDRLILYLRI VHSVDFYNHC EYPYEDEMPN RCGIIHARGP PSQSKVMSNE IQEYIRTFEG
KMASFLTRMV DIDETDMKKL GAKDAEAEVE KFITANTQEL AKDKWLCPLS GKKFKGPDFV
RKHIFNKHAE KVEEVRKEVE YFNNYLKDSK RPQLPEHPGN AKKPGSEGAT SATANASVGA
GGYRNQPFGM SHSYAPMYAS YAAASMMAPN PRGRAGFGRG GRMGGPDYRP VIHYRDLDAP
REPDEFL