ID A0A2K6BS39_MACNE Unreviewed; 1226 AA.
AC A0A2K6BS39;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Adenosine deaminase RNA specific {ECO:0000313|Ensembl:ENSMNEP00000014221.1};
GN Name=ADAR {ECO:0000313|Ensembl:ENSMNEP00000014221.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000014221.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000014221.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6BS39; -.
DR SMR; A0A2K6BS39; -.
DR Ensembl; ENSMNET00000038424.1; ENSMNEP00000014221.1; ENSMNEG00000031204.1.
DR GeneTree; ENSGT00940000157243; -.
DR OMA; ERMQMKR; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000031204; Expressed in spleen and 12 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; cd19914; DSRM_DRADA_rpt2; 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:UP000233120};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 136..202
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 213..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 136341 MW; A5B8DAA221358537 CRC64;
MRPRLSRKGY SLNGYYPHPF QGYEHRKLRY QQPGPGSSPN SFLLKQIEFL KGQIPEAPVI
GKQTPSLPPS LPGLQPRFPV LPASSTRGRQ VDIRGVPRCV HLGSQGLQRG FQHPSPRGRI
PPRRGVDCLS SHFQELSINQ DQEQRILKFL EELGEGKATT AHDLSWKLGA PKKEINRVLY
SLAKKGKLQK EAGTPPLWKI AVSTQAWNQH SRVVRPDGHS QGAPNSDPNL EPEDRNSTSV
SEDLEPFISV SAQAWNQHSG VVRPDGHSQG APNSDLEPED RNSTSALEDP LEFFDMAEIK
EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR
ERMQIKRNTN SVPETAPAAI PETKRNTEFL TCNIPTSNAS NNIVTTEKVE NGQEPVIKLE
NSQEARPEPV RLKPPVHNNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP
SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV
INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHCSTE KESEKTTESQ
TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV
SAPSKKVAKQ MAAEEAMKAL HGEATNSMTS DDQPEGMISE SLDNLESVMP NKVRKIGELV
RYLNTNPVGG LLEYARSHGF AAEFKLVDQS GPPHEPKFIY QAKVGGRWFP AVCAHSKKQG
KQEAADAALR VLIGENEKAE RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF
HDQIAMLSHR CFNTLTNSFQ PSLLGRKILA AIVMKKDSED MGVVVSLGTG NRCVKGDSLS
LKGETVNDCH AEIISRRGFI RFLYSELMKY NPQTAKDSIF EPAKGGEKLQ IKKTVSFHLY
ISTAPCGDGA LFDKSCSDRA MESTDSRHYP VFENPKQGKL RTKVENGEGT IPVESSDIVP
TWDGIRLGER LRTMSCSDKI LRWNVLGLQG ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI
CCRVTRDGSA FEDGLRHPFI VNHPKVGRVS VYDSKRQSGK TKETSVNWCL ADGYDLEILD
GTRGTVDGPR NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK
KSLKDMGYGN WISKPQEEKN FYLCPV
//
