ID A0A1S3I952_LINUN Unreviewed; 689 AA.
AC A0A1S3I952;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Double-stranded RNA-specific editase 1 isoform X1 {ECO:0000313|RefSeq:XP_013394718.1};
GN Name=LOC106162125 {ECO:0000313|RefSeq:XP_013394718.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013394718.1};
RN [1] {ECO:0000313|RefSeq:XP_013394718.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013394718.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013394718.1; XM_013539264.1.
DR AlphaFoldDB; A0A1S3I952; -.
DR STRING; 7574.A0A1S3I952; -.
DR EnsemblMetazoa; g30901.t1; g30901.t1; g30901.
DR EnsemblMetazoa; XM_013539264.1; XP_013394718.1; LOC106162125.
DR GeneID; 106162125; -.
DR KEGG; lak:106162125; -.
DR InParanoid; A0A1S3I952; -.
DR OMA; FCMNVSK; -.
DR OrthoDB; 118472at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0004000; F: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; cd19895; DSRM_RED1_rpt1; 1.
DR CDD; cd19898; DSRM_RED1_rpt2; 1.
DR Gene3D; 3.30.160.20; -; 2.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR044458; ADAR2_DSRM_1.
DR InterPro; IPR044459; ADAR2_DSRM_2.
DR InterPro; IPR014720; dsRBD_dom.
DR PANTHER; PTHR10910:SF62; AT07585P-RELATED; 1.
DR PANTHER; PTHR10910; EUKARYOTE SPECIFIC DSRNA BINDING PROTEIN; 1.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 75..141
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 226..289
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 359..683
FT /note="A to I editase"
FT /evidence="ECO:0000259|PROSITE:PS50141"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 75506 MW; 65F82CCFC09A3FF2 CRC64;
MRRTGFGEPQ PDFIDEEIKK QRQEAEQGQA EDIPTQEDSD GDIEMLPGGR KRPFPDQLDG
GGKKKKRKKT SGPPLPKNAL MQLNEIKPGL QYKVMSQSGP VHAPTFIISV EVNGQAFEGV
GNTKKRAKLN AAEKALRSFV QFPNASEAMQ AMGKQMVTNA DFTSDAAENA DLIFNSFESN
QQHGDNQNGN GTQVALNIDG AMHPAPASLN GSGLPKPIPP QPSGKNPVMI LNEQRPGLKY
EFVSEMGESH AKSFTMEVTV DGETFQGSGR NKKVAKAHAA QAALSKIFNL EISQAPALQP
VVGPNFSGTA PAILADLVVG AVHEKFAELT NNMTTPQSRR KVLAGIVQTR KDEPGKVITL
STGTKCINGE HINDHGYGLN DCHAEIIARR CLLRYFYSQL KLHVNNENSE ESIFAPKDGG
GYRLKDDVNF HLYISTSPCG DARIFSPHEL GQDDNSDRHP NRRARGQLRT KIESGEGTIP
VKANSPVQTW DGVLQGERLL TMSCSDKLAR WNVLGVQGAL LSHFVDPIYF SSVILGSLYH
REHLSRALYI RLGSIEDLPQ PYQLYTPLLS GISNPESRQP GKAPGFSVNW CIGDPSLEVV
NATTGKTEDG QPSRVCKHAL YRCFHELFGK VSAASGQTEL PRFYVEAKAN AVDYQLAKQK
LFKAFETQGL GAWIKKPMEQ DHFELVPTS
//