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SRRT_DROWI
ID   SRRT_DROWI              Reviewed;        1000 AA.
AC   B4MR46;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Serrate RNA effector molecule homolog;
DE   AltName: Full=Arsenite-resistance protein 2 homolog;
GN   Name=Ars2; ORFNames=GK21997;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
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DR   EMBL; CH963849; EDW74585.1; -; Genomic_DNA.
DR   RefSeq; XP_002063599.2; XM_002063563.2.
DR   AlphaFoldDB; B4MR46; -.
DR   SMR; B4MR46; -.
DR   STRING; 7260.FBpp0251140; -.
DR   PRIDE; B4MR46; -.
DR   EnsemblMetazoa; FBtr0419445; FBpp0377575; FBgn0223982.
DR   eggNOG; KOG2295; Eukaryota.
DR   HOGENOM; CLU_008560_0_0_1; -.
DR   InParanoid; B4MR46; -.
DR   OMA; HLRMCEE; -.
DR   OrthoDB; 525905at2759; -.
DR   PhylomeDB; B4MR46; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IEA:EnsemblMetazoa.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; ISS:UniProtKB.
DR   GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR   GO; GO:0030422; P:siRNA processing; IEA:EnsemblMetazoa.
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; Phosphoprotein; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..1000
FT                   /note="Serrate RNA effector molecule homolog"
FT                   /id="PRO_0000385225"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..414
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..927
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         83
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1000 AA;  113364 MW;  3BF4F4EE095078DE CRC64;
     MADSDDEYDR KRRDKFRGER SDSYRTERRD ERRPISSSGG ARDEWNPFRG SSAAGGGGGG
     GARHRPDYSD YRSPGGGGPR ARYGSPGREM PPAKRMRPDW PDEGMRSNPR FGGYDPYMMQ
     AWNEHYQSLH YSHGGGHMPI ARETSGPGIG NDTQTQPAML TLKQFLDTQD ENISDSEVMR
     KYTEYKTDFK RQQLNEFFVA HKDEEWFKNK YHPEDSVRRS DEQRGFLQRR SSVFVELLEN
     GTIGSVKVDS SQADPLVRVL DMCVIKLEGG TDEDLKILDE KPKEPLVFER KIEPIQTTAA
     LAAATATPKS PKKNENDNGV AVVVSPQKND LKPVNSDEEN WETDKKSDEN DKNDNEQGDG
     DKKGGESSKK QLKKKKKTKK RKRKSSDDDD DESSSSDSES SSSSEEEEDE EELKKKYDVE
     DGLRTEQKAE QEKDKKEEEA IKAANVEEQP KAEEVQEKIE DEKEKVEEEP KPDVKTEAEA
     VAEPDAEPKK EEEEKAKEPE DEEKKPETEE TSKMETENGE SKEETKPTPE PAVESAPAAD
     VIEMETETID LDKVKDGPQP RALHRTASIF LRNLAPSITK AEIEAICNRS PGYLRVAIAD
     PLVERRWYRR GWITFSRDVN IKEICWSLNN QRLRDCELGA IVNRDLSRRV RPTNGITAHK
     QVVRSDIKLC AKIAMNLDER FRLWVDEPAP AADGKGETAT DATNGSSSGA TTYGFNTKNP
     VLQNITDYLI EEASAEEEEL LGLSGDQNDV EGEPIVRDEQ LIAVLDRLLL YLRIVHSVDY
     YNHCEYPYED EMPNRCGIIH ARGPAPMKVT SNDIQEYIKS YEGKLQQFLT KTVLLTDDDI
     KDLGAKDAET EVEKFVQANT QELAKDKWLC PLSGKKFKGP EFIRKHIFNK HEEKVDEVRK
     EVQFFNNYLR DPKRPQLPEH PGTTKRPEFE PSRGAGGYRP AMYPPFGGLP YGFAPPMPMG
     GRGGGRGYQA RRELPLEHQR RVIGYHDLDA PANSDRENAF
 
 
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