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Database: UniProt
Entry: A0A3L8SF98_CHLGU
LinkDB: A0A3L8SF98_CHLGU
Original site: A0A3L8SF98_CHLGU 
ID   A0A3L8SF98_CHLGU        Unreviewed;       494 AA.
AC   A0A3L8SF98;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=DRBM domain-containing protein {ECO:0000259|PROSITE:PS50137};
GN   ORFNames=DV515_00008235 {ECO:0000313|EMBL:RLW01150.1};
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:RLW01150.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW01150.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW01150.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW01150.1};
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:RLW01150.1}.
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DR   EMBL; QUSF01000023; RLW01150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SF98; -.
DR   STRING; 44316.ENSEGOP00005011050; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   CDD; cd19871; DSRM_DUS2L; 1.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR044463; DUS2_DSRM.
DR   PANTHER; PTHR45936; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR   PANTHER; PTHR45936:SF1; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF01207; Dus; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT   DOMAIN          370..437
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          449..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  55805 MW;  70E80F2DB4FFD4A9 CRC64;
     MTVNTPLCFR GKKILAPMVR VGTLPMRLLA LDYGADIVYC EELIDIKMLQ CKRVINEVLE
     TVDFVAPNDR VVFRTCERER ERVVFQMGSA DAERALAVAK LVESDVAGID INMGCPKEYS
     TKATYAGGMG AALLSDPDKI ESILTTLVKG ICKPVTCKIR ILPSVEDTVN LVKRIEKTGI
     AAIAVHGRKK EERPQHPVHC DVIKAISEAV SIPVIANGGS HDFIKEYADI ETFQKATAAS
     SVMIARAAMW NPSVFRKEGF CPLKDVMQDY IKYAVRYDNH YTNTKYCLCQ MLREQLETTQ
     GKKLHAAQST QEICEAFEMG DFYEEATAIF EAKKTSLETK TQDEDDQVED PDVIKMAVRF
     DKREYPPQIT PKMYLLEWCR KEKHPQPVYE TVQRPVDRLF CSVVTVAEQK YRSALWDKSK
     KLAEQAAAIV CLRTLGVPEG KLCEGENHLM NKRKRGDQEH SISRDHGEDL AEPSHKKANF
     IEETSDMNVP KMPR
//
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