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Database: UniProt
Entry: A0A2Y9MC03_DELLE
LinkDB: A0A2Y9MC03_DELLE
Original site: A0A2Y9MC03_DELLE 
ID   A0A2Y9MC03_DELLE        Unreviewed;      1174 AA.
AC   A0A2Y9MC03;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Double-stranded RNA-specific adenosine deaminase isoform X1 {ECO:0000313|RefSeq:XP_022414943.1};
GN   Name=ADAR {ECO:0000313|RefSeq:XP_022414943.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022414943.1};
RN   [1] {ECO:0000313|RefSeq:XP_022414943.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022414943.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022414943.1; XM_022559235.2.
DR   AlphaFoldDB; A0A2Y9MC03; -.
DR   STRING; 9749.A0A2Y9MC03; -.
DR   KEGG; dle:111166955; -.
DR   InParanoid; A0A2Y9MC03; -.
DR   OrthoDB; 118472at2759; -.
DR   Proteomes; UP000248483; 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:UP000248483};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          130..196
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50139"
FT   DOMAIN          241..305
FT                   /note="Z-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50139"
FT   DOMAIN          451..519
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          562..630
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          674..742
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          834..1169
FT                   /note="A to I editase"
FT                   /evidence="ECO:0000259|PROSITE:PS50141"
FT   REGION          203..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1174 AA;  130512 MW;  4C014B39F779697D CRC64;
     MDPRQGCSLN RYQTHPVQGY EHSKLRHQQP GLGSYPNSFR LQQIEFLKGQ LPEAPLIGKQ
     APSLPLFLPG LGPRFPGPPA RGGYLQIPGV LRGVPLRSQV LPGGFQHPTP RGWVQPWRGV
     DTLSSRFREL TISQDQEQRI LELLEELGER KATTALDLAR KLQAQKKEIN RVLYSLAKKG
     KLHREAGTPP LWRLSVPVQA WNQPSQVARA DSHSQGAPSS DFSLETEDRS LTSGLEDPPE
     PLDMAEIKEK ICDYLFNVSN SSALNLAKNI GFTRARDVTA VLIDLERQGD VYRQGTTPPI
     WHLTDKKRER IQIKRNTNNV PETTQAAIQE TRKIAELPTC NLPASDASNS MDTTEKVENG
     QEPVVKLETR QEVTPEPIKL KPPVHDNGPS KTGYVDFENG QWATDDIPDD LNSIHAAPGE
     FRAIMEMPSF YSHGLPRCSP YKKLTECQLK NPISGLLEYA QFASQTCEFN LIEQSGPPHE
     PRFKFQVVIS GREFPPAEAG SKKVAKQDAA MKAMTILLEE AKAKDSGRSE ESYYCSSEKE
     SEKTAESQTT TPSATSFLSG KNPVTTLLEC VHKLGSSCEF RLLSREGPAH DPKFQYCVAM
     GTHTFPTASA PSKKAAKQMA AEEAMKALQG EATGSTSSDD QPGSMNTESF DNLESVMPSK
     VRRISELVRY LNTNPVGGLL EYARSHGFAA EFKLVDQSGP PHEPKFVYQA KVGGRWFPAV
     CAHSKKQGKQ EAADAALRVL IGEDEKAERM GFTEVTPVTG ASLRRTMLLL SRSPEAQPKT
     LPLTGSTFHD QIAMLSHRCF NALTNSFQPS LLGRKILAAI IMKKDSEDLG VVVSLGTGNR
     CVKGDSLSLK GETVNDCHAE IISRRGFIRF LYSELMKYNP QTAKDSIFEP AKGGEKLQIK
     KTVSFHLYIS TAPCGDGALF DKSCSDRAVE STDSRHYPVF ENPKQGKLRT KVENGEGTIP
     VESSDIVPTW DGIRLGERLR TMSCSDKILR WNVLGLQGAL LTHFLQPVYL KSVTLGYLFS
     QGHLTRAICC RVTRDGSAFE DGLRHPFIVN HPKVGRVSVY DSKRQSGKTK ETSVNWCLAD
     GYDLEILDGT RGTVDGPRNE LSRVSKKNIF LLFKKLCSFR YRRDLLRLSY GEAKKAARDY
     EIAKNYFKKS LKDMGYGNWI SKPQEEKNFY LCPV
//
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