ID I3JGJ6_ORENI Unreviewed; 1208 AA.
AC I3JGJ6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Adenosine deaminase RNA specific {ECO:0000313|Ensembl:ENSONIP00000007987.2};
GN Name=adar {ECO:0000313|Ensembl:ENSONIP00000007987.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007987.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000007987.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR AlphaFoldDB; I3JGJ6; -.
DR STRING; 8128.ENSONIP00000030791; -.
DR Ensembl; ENSONIT00000007992.2; ENSONIP00000007987.2; ENSONIG00000006335.2.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157243; -.
DR HOGENOM; CLU_005382_0_1_1; -.
DR TreeFam; TF315806; -.
DR Proteomes; UP000005207; Linkage group LG11.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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; -; 2.
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; 2.
DR Pfam; PF02295; z-alpha; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00550; Zalpha; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS50139; Z_BINDING; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 254..320
FT /note="Z-binding"
FT /evidence="ECO:0000259|PROSITE:PS50139"
FT DOMAIN 341..406
FT /note="Z-binding"
FT /evidence="ECO:0000259|PROSITE:PS50139"
FT DOMAIN 539..607
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 716..784
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 852..1184
FT /note="A to I editase"
FT /evidence="ECO:0000259|PROSITE:PS50141"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 132459 MW; A44E9BDDAF99C244 CRC64;
MSRGRGGPSK EHYYRHPPPH VQARDNFHRP GTGVFYPRAG PQQIPHPSYY DGPAHPEAHI
QPSSPLIPST PPTPSHIKVV PNSVTHNSLY SQNHGAGSSP NSFHDKQREF LTGQISEAPQ
FRATVSRGGG GGGFVPNRSH STIYQPQSGY CRYPNPSNSS PRGRGGYSQD RRPYRPGAGS
SRGNLAPRHL NQNQFQGKNY NQHSSRQWRT QTDSLCDKFQ SLLLKDRPNR EGERFDRHPS
SSSSGNLSFC KPNITLTTEI QGEVHEALGA LKPSESISAK VLARKLHLPK KVVNKALYSL
EHLQKASKQG LTPPEWTLYR EPLRVEEDQT SSEPPQKPEE KSSAQEQKEQ IFKYLLQSRE
ATALNIAKNI GLKTAKQVNS TLYALEKQGE VVRNVEVNPP TWELSTHRRE RMERSLKAAQ
SNPAVLVKME VEEEEVSAIF SPSPLPPLPG LEVLTGGWIP DQILSEAPLS SASGKSENAN
EGQWSTDDIP EFLNAIRRET DAEKKAAEKA NAMGTVAVSV AAPPPQNLWA KLQEVRLKNP
VSGLMEYAQY LGQNCEFLLL DQSGPSHDPR FRMQVMLNGR LFPVAEASSK KVAKKDAAAA
TLRILVKEMQ GGTCTADEEN TGNVEQVMEL LPDTSVKIIF VTSVTKLFSL MFTSFFCTTA
SPVCLLQPQL PLGPSSGSDE SFSGATCPSL PPLTADELRA AHEAGVGDLI NHLNNNAVSG
LLEYARARGF AAEIRLVGQS GPPHDPKFTY QAKLGGRWFP PVCASNKKQG KQEAADAALR
VLIGEAERAA RTGELTPAEL PVSGSTLHDQ IAMLSHQRFN ALTTRIQHCL LGRKILATII
MRRGEGLGTV VSLGTGNRCV KGEELSLKGE TVNDCHAEII SRRGFIRFLY SELFKHYEGA
DDSIFEPAEN NKLRIKSDIT FHLYISTAPC GDGALFDKSC SEAGDEAQGH QPLFENVKQG
KLRTKVENGE GTIPVESSAI VPTWDGIQHG ERLRTMSCSD KILRWNVIGL QGALLTHFLD
PIYLKSITLG YLYSHGHLTR AVCCRLARDG EAFTQSLPAP FKLNHPEVGR VSVYDSTRHT
GKTKESSVNW SFPDQHSVEV LDGTKGKVDG TKLAVSRVSK SNLFHLFRSL CQRSGHTDLL
SLPSYAQAKM SAVSFQQAKQ QFFQALSAHG YGAWIGKPLE EKSFEAGEGN WNNGAPVGNS
NNVGAVEA
//