ID A0A067F1C6_CITSI Unreviewed; 611 AA.
AC A0A067F1C6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
GN ORFNames=CISIN_1g007250mg {ECO:0000313|EMBL:KDO57021.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO57021.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO57021.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes
CC the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs
CC by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
CC {ECO:0000256|RuleBase:RU367113}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU367113};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367113}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family.
CC {ECO:0000256|ARBA:ARBA00006562, ECO:0000256|RuleBase:RU367113}.
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DR EMBL; KK784967; KDO57021.1; -; Genomic_DNA.
DR RefSeq; XP_006477068.2; XM_006477005.2.
DR AlphaFoldDB; A0A067F1C6; -.
DR STRING; 2711.A0A067F1C6; -.
DR PaxDb; 2711-XP_006477068-1; -.
DR GeneID; 102622361; -.
DR KEGG; cit:102622361; -.
DR eggNOG; KOG1982; Eukaryota.
DR OrthoDB; 11691at2759; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034353; F:mRNA 5'-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0110155; P:NAD-cap decapping; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0090304; P:nucleic acid metabolic process; IBA:GO_Central.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395:SF9; DECAPPING AND EXORIBONUCLEASE PROTEIN; 1.
DR PANTHER; PTHR12395; DOM-3 RELATED; 1.
DR Pfam; PF08652; RAI1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU367113};
KW Metal-binding {ECO:0000256|RuleBase:RU367113};
KW Nuclease {ECO:0000256|RuleBase:RU367113};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367113};
KW Nucleus {ECO:0000256|RuleBase:RU367113};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT DOMAIN 470..532
FT /note="RAI1-like"
FT /evidence="ECO:0000259|Pfam:PF08652"
FT REGION 56..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 68319 MW; E4279C86BF83B06E CRC64;
MGTSHTILPR YIHIPNRIVL SESAYCFAIG INKARLDSGT RKFVKSKTQN NLSIVHPKTS
MDFPDQDVDV FGEEYGNNHE LEGGTHESSA SSSSSSSSTS SSRSSSSSAS SSSNGSGGGE
SSSASGSASS GGGAAGLGVE GGGEEESGEE VENTLNLNSK NYEDYNYNHT RDLFGDDDDD
DEVVVVEEDD KDLFGSDNEA YCRTSAISPY PIPVLPVVRN NNNHGGRGGF GRGRWPNDRG
GVGILPRPGY PPRQGGYGRG SRFSNGRQDE RFVSEFRLSR SEETLSRKVV AFQEPCELAQ
YSRVEGGDVY FDDRSLRLFK RLISEDVGAD LNEGFDTFIE KKELGSEGFG DLLSCIRNRN
IPLQNMHFVT FRNNLNKILA TAYIRNEPWA MGVHKRNGVV YLDVHKVQER PKSELDRRRC
YWGYCFESLA TEDPRRADGE GIHHIDANVE FCAVMKTKLG AHRLLMGAEM DCCDSTDDGR
RFYVELKTSR ELDYHTEERF EREKLLKFWI QSFLAGVPFI VVGFRDDAGR LVRTERLRTK
DITHRVKMKN YWQGGVCLAF ADEVLCWLYG TVKENEDYTL HFNPPSNRLE LLQASSCPES
ITCHVEQLQN I
//
