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Database: UniProt
Entry: A0A1S3F234_DIPOR
LinkDB: A0A1S3F234_DIPOR
Original site: A0A1S3F234_DIPOR 
ID   A0A1S3F234_DIPOR        Unreviewed;      1122 AA.
AC   A0A1S3F234;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Double-stranded RNA-specific adenosine deaminase isoform X3 {ECO:0000313|RefSeq:XP_012870668.1};
GN   Name=Adar {ECO:0000313|RefSeq:XP_012870668.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012870668.1};
RN   [1] {ECO:0000313|RefSeq:XP_012870668.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012870668.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_012870668.1; XM_013015214.1.
DR   AlphaFoldDB; A0A1S3F234; -.
DR   GeneID; 105984887; -.
DR   CTD; 103; -.
DR   OrthoDB; 118472at2759; -.
DR   Proteomes; UP000081671; Unplaced.
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:UP000081671};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          130..192
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50139"
FT   DOMAIN          237..301
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50139"
FT   DOMAIN          403..471
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          514..582
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          619..687
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          779..1114
FT                   /note="A to I editase"
FT                   /evidence="ECO:0000259|PROSITE:PS50141"
FT   REGION          196..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  125020 MW;  FFEC63F1C34B037F CRC64;
     MDPRQGCSFT RYHIQPSQGY EHSRHRWQQP QPGSYSNSFR LQQIEFLKGQ LPEAPLIGRQ
     TSSLPPFLPG FWPRFPGPSA PGRHQEIWGV PRGEHLRSQG LHIRPQLPLP CGGVLPPTGV
     ERLSSHFQEL NISQDQEQRI LKLLKEKATT VHELARKLRA QKKEVSRVLY SLAKKGKLQK
     GTGTPPLWSI TTSFQAQDQP NSVVNPDNQS QGAPDSEPSL KAEEEDPTSD LEDPPEPFDM
     AEIKEKICNY LFNVPNSSAL NVARSIGFSK ARDVNTVLID LERQGDVYRQ GATPPIWYLT
     DKKRERMQIK RNTHSVPAAT PAAVPETQRN MALSTCHLPP SNKMVTTAKM ENGQGPVIRF
     ESRKEGRPMR LKPPVYHNGP SRAGPGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE
     FNLIDQSGPP HEPRFKFQVV ISGREFPPAE AGSKKVAKQD AALKAMTILL REAKAKDGGN
     LEDLSCCSLE DELEKTEEPE ASTPSATSLF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP
     AHDPKFQYCV AVGAQTFPTV SAPSKKVAKQ MAAEEAMKAL HEEATNMVDN QSGEMESLDN
     LEPNKIGRIG ELVRYLNTNP VGGLLEYARS HGFAAEFKLV DQSGPPHEPK FVYQAKVGGR
     WFPAVCAHSK KQGKQEAADA ALRVLIGENE KAERMGFTEV TPVTGASLRR TMLLLSRSPD
     AHPKTLPLSG STFHDQIAML SHQCFNALTN SFQPSLLGRK ILAAIIMKRD AEDMGVVVSL
     GTGNRCVKGD SLSLKGETVN DCHAEIISRR GFIRFLYSEL MKHNHRTAKD SIFELARGGE
     KLQIKKTVSF HLYISTAPCG DGALFDKSCS DRAVESTDSR HYPVFENPKQ GKLRTKVENG
     EGTIPVESSD IVPTWDGIRL GERLRTMSCS DKILRWNILG LQGALLTHFL QPVYLKSVTL
     GYLFSQGHLT RAICCRVTRD GKSFEHGLRY PFTVNHPKVG RVTVYDSKRQ SGKTKETSVN
     WCLADGFDLE ILDGTRGTVD GPGNELSRLS KKNIFLQFKK LCSFRYRRDL LKLSYGEAKK
     AARDYETAKN YFKKSLRDMG YGNWISKPQE EKNFYLCPVP ND
//
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