ID A0A3L8RV98_CHLGU Unreviewed; 1163 AA.
AC A0A3L8RV98;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Double-stranded RNA-specific adenosine deaminase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DV515_00015489 {ECO:0000313|EMBL:RLV88279.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV88279.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV88279.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV88279.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV88279.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV88279.1}.
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DR EMBL; QUSF01000186; RLV88279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RV98; -.
DR SMR; A0A3L8RV98; -.
DR STRING; 44316.ENSEGOP00005013914; -.
DR Ensembl; ENSEGOT00005016041; ENSEGOP00005013914; ENSEGOG00005011242.
DR OMA; ERMQMKR; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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:UP000276834};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 134..200
FT /note="Z-binding"
FT /evidence="ECO:0000259|PROSITE:PS50139"
FT DOMAIN 235..299
FT /note="Z-binding"
FT /evidence="ECO:0000259|PROSITE:PS50139"
FT DOMAIN 452..520
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 567..635
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 683..751
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 820..1158
FT /note="A to I editase"
FT /evidence="ECO:0000259|PROSITE:PS50141"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 128612 MW; C48AD000E0247064 CRC64;
MIRGAGRGRG SYLTQPRQNC PSTNRGLFKH PRTPQETNQE TFLHQQFLTE QDAEVSVLQG
QGSHKEWRTR GGRAAAPAPA GRGLPSSSRA AGRRLSSQHP RVETLPRYCP PQHHLQDNSR
RYSDAVRLNF QRLSLAGQDY EREILTVFRH LGEGRTCTAN DLAHKLKTKK KEINRVLYKL
LREGKLHKEG ETPPLWIIAS PSSGRERSPT DHSASCTDPA NCENRGEWST FGLGDAEMAE
TKEKICNYLF SVVETTALNL AKNIGFSRAK DINAFLSALE KLGDVHKQNA TPPRWSLTNR
KRERMQMRLK ASTIMQMADA TPPESGLPSS FVTLCPPEVT AALPAVIKEE KESAENEQKP
LGQVGQGNVG DMEADASKDT KPDFSSLSNY DNSENSKWTT DDIPDNLNAI SKQPDKSECI
MDSQCSPSYA AQFETAFPCT PAEKLIACQE KNPVSGLTEY SQYTYQHCDF IMLEQNGPSH
EPRFKFQAVI NGRQFPPAEA GSKKLAKQEA AANAMKVLMS EVENGRHSGI KCEEPFPSNS
SEPEQPLQLE PELSSAAAHL TLLPGKHPIS ILMEYGQKSG NIIEFQLLSQ EGPPHDPRFS
YCVKMGDQIF PAVVGNSKKG AKQMAAEVAV KILSGESVPH VLPEQPVVEP QSDQSMHNIT
TPDESKVVKT KGIGELIKYL NVNPVSGLLE YARSNGFAAE FKLIDQSGPP HDPKFVYQAK
VGGRWFPAVT AHNKKQGKQE AADAALRVLI GESEKTERME GMSVTELPVS GSTLHDQLAM
LSHQRFNSLT AHMQHSLLGR KILAAIIMRR GDKGLGVVVS IGTGNRCVKG EELSLKGETV
NDCHAEIISR RGFVRFLYSE LMKYDPSNPS SAEESIFEQA GGKKLKMKSS VTFHLYISTA
PCGDGALFDK SCSDQANEMG QPQHQPLFEN PKQGKLRTKV ENGEGTIPVE SSDIVPTWDG
IQHGERLRTM SCSDKILRWN ILGLQGALLS HFLEPVYLHS VTLGYLYSQG HLTRAICCRM
ERDGSTLKEK LQAPYHINHP EVGRVSVYDS ARQTGKTKES SVNWCLADES EVEILDGTKG
KVDGVKLEVS RVSKRKTFAL FQQLCAKNNR KDLQGFSTYS DAKGAATAYQ AAKQCFFSTL
EELGYGSWIR KPQEEENFSV LDV
//
