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Database: UniProt
Entry: A0A1S3I952_LINUN
LinkDB: A0A1S3I952_LINUN
Original site: A0A1S3I952_LINUN 
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.
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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
//
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