ID M1QSW4_CTEID Unreviewed; 1107 AA.
AC M1QSW4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ADAR1-like protein {ECO:0000313|EMBL:AGG20156.1};
OS Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Ctenopharyngodon.
OX NCBI_TaxID=7959 {ECO:0000313|EMBL:AGG20156.1};
RN [1] {ECO:0000313|EMBL:AGG20156.1}
RP NUCLEOTIDE SEQUENCE.
RA Yong L., Yu H.C.;
RT "Molecular characterization and expressive analysis of a novel gene, highly
RT similar to ADAR1, in Ctenopharyngodon idella.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KC206049; AGG20156.1; -; mRNA.
DR AlphaFoldDB; M1QSW4; -.
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:0048856; P:anatomical structure development; IEA:UniProt.
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:SF145; DEAMINASE ACTING ON RNA (ADAR)-1, PUTATIVE-RELATED; 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; 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 2: Evidence at transcript level;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 251..317
FT /note="Z-binding"
FT /evidence="ECO:0000259|PROSITE:PS50139"
FT DOMAIN 410..475
FT /note="Z-binding"
FT /evidence="ECO:0000259|PROSITE:PS50139"
FT DOMAIN 639..707
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 755..823
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 880..948
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 1016..1052
FT /note="A to I editase"
FT /evidence="ECO:0000259|PROSITE:PS50141"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 121246 MW; 5E9094B92694492C CRC64;
MSRGRGGFNK DCQRSFLPPP QGKPQFHYYT TTGHPRGPRV PSPGSVSGSY QHPSLYSSYP
GAPGVPPHGR PFPPSPSEPP LWASPQHSSD QISDSNGVSF RQHQVQFLRG QSAHAPQFRG
PQQRGSQTSS QGEEVSTGPL HYQTGYRDFK TSGNSFGRRD CYSRGRGNWQ REHNFGPKKK
SGWNHPQQKG QYYPNQHTKH YWNTQVDDVS FGLHSLSLGD RITRVDNSDA LSCSSSASKV
SSSPDSVRES LYLTPEIQQQ VFAFLKSLGP DETVHARALG KKLNLPKTIV NKALYALLRT
NQAVKQGEIP PLWRLCKVED SEPIKGRDQS LSSKDLEKEP GQSSSINQES REHPTSTGAP
SASQILFEAD GNINDQSEDS EGDDTSDTLF PVQDQQILLP AVQLETLSTM AESKDSKEKI
LQYLYEVGTG NALVIAKNLG LRSAKQVNPT LYAMEKQGDV RRNTEVTPPT WALSAHRQEK
MDRQRKVAAT ARQDVNNAEM LNLAAEGIAD ETSVKLEADD EFDFGPVPME GGENPLVDML
DNNNIFGNTE LDMPGLEPIP PKPSELSTST YQPPPHQFSY YQDMASNGGE RLQWASDDIP
EFLNTIRSEV AVSLAAPPPP SQSLESSRFQ KLKEARSKNP VSGLMEFAQH LGHTCEFLLL
DQSGPSHDPR FRMQVMLDGR RFPPAEGSNK KVAKKDAAAT TLRILWREMK GAGGDEEEEP
SFEGAESTTD LAEDMPSGTD TPPQALSRSL PGGKNPVSVL MEHSQRSGNA IQFIKTGQEG
PPHDPRFMFR VKVGDRLFQE ASAPSKKAAK QLAAEGAVKE LMGDGLLHLN KPPGTFHSLG
DNESQPAIPA CPSLPPLTAS ELQAAHEAGV GDLINHLNNN AVSGLLEYAR ARGFAAEIRL
VGQSGLSHEP KFTYQAKLGG RWFPAVCASN KKQGKQEAAD AALRVLIGEA EKAARTGELT
PELPVSGSTM HDQIAMLSHQ RFNALTARIQ HSLLGRKILA TIVMRNGSDT LGTVVSLGTG
NRCVKGEELS LRGDTVNDCH AEIISRRGFI RYQLAAELSL SLTVNPIIHF SSHSTAFSVS
FFKMKESYFT AAHKYIDFIF AVLKMLL
//
