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Database: UniProt
Entry: A0A445BRH2_ARAHY
LinkDB: A0A445BRH2_ARAHY
Original site: A0A445BRH2_ARAHY 
ID   A0A445BRH2_ARAHY        Unreviewed;       461 AA.
AC   A0A445BRH2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=RNA-binding S4 domain-containing protein {ECO:0000259|SMART:SM00363};
GN   ORFNames=Ahy_A08g037696 {ECO:0000313|EMBL:RYR41285.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR41285.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR41285.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR41285.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in RNA = a pseudouridine in RNA;
CC         Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC         Evidence={ECO:0000256|ARBA:ARBA00000073};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000256|ARBA:ARBA00010876}.
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:RYR41285.1}.
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DR   EMBL; SDMP01000008; RYR41285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445BRH2; -.
DR   STRING; 3818.A0A445BRH2; -.
DR   Proteomes; UP000289738; Chromosome a08.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR21600:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          87..152
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   461 AA;  50547 MW;  5EBE5E23BBA2C2D3 CRC64;
     MLSVHSCGCC RVFAARAIQF QTTPSLFFST PNYKSRVGTA RRVAASSGFA GDSGSDLRQE
     TIADTRTNYA GVRLEETVDN GIRSGKLRLD SWISSRISGI SRARVQSSIR AGLVQVNGRV
     VDKVSFNVKA GDEISCTISE LQTLRAVPEN IPLDIVYEDE HVLVINKPAH MVILYIYPSV
     VHPAPGNTSG TLVNGILHHC NLPNVEYSKE EALSNTEDSD DEFNSFYTNA SSCEGLSSRP
     AVASIRPGIV HRLDKGTSGL LVVAKDEHSH MKLSEQFKLR TIKRVYVSLT AGLPTPVAGR
     VEVPVGRDPN NRLRMTAVAG PLNPRKSRHA ASRYKVIEIL ARGGCALVEW KLETGRTHQI
     RAHAKYLGVP LLGDEVYGAT RSMVLSLLRP RTPSGLHSKI VQMVSRIDRP CLHALTLGFK
     HPHTGQEVHF SCEPPADFDE ILNQLRKISN EGAFFTKHSI S
//
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