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Database: UniProt
Entry: A0A0Q9W2T8_DROVI
LinkDB: A0A0Q9W2T8_DROVI
Original site: A0A0Q9W2T8_DROVI 
ID   A0A0Q9W2T8_DROVI        Unreviewed;       976 AA.
AC   A0A0Q9W2T8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=Dvir\GJ20888 {ECO:0000313|EMBL:KRF79388.1};
GN   ORFNames=Dvir_GJ20888 {ECO:0000313|EMBL:KRF79388.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF79388.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:KRF79388.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
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. {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; CH940648; KRF79388.1; -; Genomic_DNA.
DR   RefSeq; XP_015029502.1; XM_015174016.1.
DR   AlphaFoldDB; A0A0Q9W2T8; -.
DR   SMR; A0A0Q9W2T8; -.
DR   EnsemblMetazoa; FBtr0444768; FBpp0401081; FBgn0208024.
DR   InParanoid; A0A0Q9W2T8; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
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   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:UP000008792}.
FT   DOMAIN          162..271
FT                   /note="SERRATE/Ars2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12066"
FT   DOMAIN          783..954
FT                   /note="SERRATE/Ars2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04959"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..976
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        283..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  110350 MW;  C13F3B003FAA2201 CRC64;
     MADSDDEYDR KRRDKFRGER DSYRPERRDE RRPMGGGANS RDEWSERNPF RGSSAAGGGG
     GGGARHRPDY SDYRGSGPRP RYGSPGREMP PAKRMRPDWG ESEMRSNPRF GYDPYLVQAW
     NDHYQSLHSA YSHSSHPSSA RESAPNVVNS DTQTQPAMLT LKQFLDTQDE NISDSEVMRK
     YTEYKTDFKR QQLNEFFVAH KDEEWFKNKY HPEDSVRRSE EQRGFLKRRT DVFLELLENG
     TIGSVKVDSS QADSLVRVLD TCVIKLEGGT DEDLKILDEK PKETPVVYER KSESTEASVV
     AKREPESPKQ TKSEKGADEE QPVVVSPQRK SLRPVNSDEE NWDDENDEMA AVPDAAKNEQ
     QTEIVAAKPA KVQGDDDSIK SGSDKKLKKK KIKKRNRNSS DDESSSSSSF ESDSDSDDEK
     LKAKYDVEEG LRADQKAEAQ KDKEEAATVA KANPLPPDSP QPEGGTALQD AAAIKSEQSD
     EQQEKDAEQP AELQADEPAA AKNGEEPEKT EKNEVETKST ADDVTETIDL DKVKDGPQPR
     ALHRTSSIFL RNLAPSITKA EIEAICTRFS GYLRVAIADP LVERRWYRRG WITFTRDVNI
     KEICWSLNNQ RLRDCEMGAI VNRDLSRRVR PANGITAHKQ IVRADIKLCA KIAMNLDERF
     KLWSEADSTQ QQPDAESKPS ADATNGSGGS STTYGFNSKN PVLQNITDYL IEEASAEEEE
     LLGLAGDNKD GEGEPIERDE QLISVLDRLV LYLRIVHSVD YYNHCEYPYE DEMPNRCGII
     HARGPPPMRV TSNDVQEYIK AYDGKLQQFL TKSVQLSDDE IKELGAKNPE TEVEKFVQAN
     TQELAKDKWL CPLSGKKFKG PEFIRKHIFN KHEEKVDEVR KEVQYFNNYL RDPKRPQLPE
     HPGSSKRTES ESGRGSGGYR PPMYPPFSAM PYGFAPPMMG GGGRGGRNFP PVRRPGGFDY
     RARSHYRDLD APQEPY
//
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