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Database: UniProt
Entry: G3QW58_GORGO
LinkDB: G3QW58_GORGO
Original site: G3QW58_GORGO 
ID   G3QW58_GORGO            Unreviewed;      1226 AA.
AC   G3QW58;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Adenosine deaminase RNA specific {ECO:0000313|Ensembl:ENSGGOP00000007007.3};
GN   Name=ADAR {ECO:0000313|Ensembl:ENSGGOP00000007007.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000007007.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000007007.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000007007.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000007007.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; CABD030006587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004026877.1; XM_004026828.2.
DR   AlphaFoldDB; G3QW58; -.
DR   SMR; G3QW58; -.
DR   Ensembl; ENSGGOT00000007193.3; ENSGGOP00000007007.3; ENSGGOG00000007156.3.
DR   GeneID; 101134621; -.
DR   KEGG; ggo:101134621; -.
DR   CTD; 103; -.
DR   eggNOG; KOG2777; Eukaryota.
DR   GeneTree; ENSGT00940000157243; -.
DR   OrthoDB; 118472at2759; -.
DR   TreeFam; TF315806; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000007156; Expressed in frontal cortex and 6 other cell types or tissues.
DR   GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd19913; DSRM_DRADA_rpt1; 1.
DR   CDD; cd19915; DSRM_DRADA_rpt3; 1.
DR   Gene3D; 3.30.160.20; -; 3.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR002466; A_deamin.
DR   InterPro; IPR044456; ADAR1_DSRM_1.
DR   InterPro; IPR044457; ADAR1_DSRM_3.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR042371; Z_dom.
DR   PANTHER; PTHR10910:SF107; DOUBLE-STRANDED RNA-SPECIFIC ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR10910; EUKARYOTE SPECIFIC DSRNA BINDING PROTEIN; 1.
DR   Pfam; PF02137; A_deamin; 1.
DR   Pfam; PF00035; dsrm; 3.
DR   Pfam; PF02295; z-alpha; 2.
DR   SMART; SM00552; ADEAMc; 1.
DR   SMART; SM00358; DSRM; 3.
DR   SMART; SM00550; Zalpha; 2.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 3.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR   PROSITE; PS50137; DS_RBD; 3.
DR   PROSITE; PS50139; Z_BINDING; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          133..199
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50139"
FT   DOMAIN          293..357
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50139"
FT   DOMAIN          503..571
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          614..682
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          726..794
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          886..1221
FT                   /note="A to I editase"
FT                   /evidence="ECO:0000259|PROSITE:PS50141"
FT   REGION          208..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1226 AA;  135953 MW;  AE6E7120719E44D9 CRC64;
     MNPRQGYSFN GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ
     TPSLPPSLPG LQPRFPVLLA SSARGRQVDI RGVPRGVHLG SQGLQRGFQH PSPRGRNLPQ
     RGVDCLSSHF QELSIYQDQE QRILKFLEEL GEGKATTAHD LSGKLGTPKK EINRVLYSLA
     KKGKLQKEAG TPPLWKIAVS TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED
     LLEPFIAVSA QAWNQHSGVV RPDGHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK
     EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR
     ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS NNMVTTEKVE NGQEPVIKLE
     NRQEARPEPV RLKPPVHYNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP
     SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV
     INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ
     TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV
     SAPSKKVAKQ MAAEEAMKAL HGEASNSMAS DNQPEGMISE SLDNLESMMP NKVRKIGELV
     RYLNTNPVGG LLEYARSHGF AAEFKLVDQS GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG
     KQEAADAALR VLIGENEKAE RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF
     HDQIAMLSHR CFNTLTNSFQ PSLLGRKILA AIVMKKDSED MGVVVSLGTG NRCVKGDSLS
     LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ IKKTVSFHLY
     ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL RTKVENGEGT IPVESSDIVP
     TWDGIRLGER LRTMSCSDKI LRWNVLGLQG ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI
     CCRVTRDGSA FEDGLRHPFI VNHPKVGRVS VYDSKRQSGK TKETSVNWCL ADGYDLEILD
     GTRGTVDGPR NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK
     KGLKDMGYGN WISKPQEEKN FYLCPV
//
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