ID A0A061G444_THECC Unreviewed; 436 AA.
AC A0A061G444;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
GN ORFNames=TCM_015822 {ECO:0000313|EMBL:EOY24148.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY24148.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY24148.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001881; EOY24148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061G444; -.
DR EnsemblPlants; EOY24148; EOY24148; TCM_015822.
DR Gramene; EOY24148; EOY24148; TCM_015822.
DR Proteomes; UP000026915; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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:UP000026915};
KW RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT DOMAIN 319..381
FT /note="RAI1-like"
FT /evidence="ECO:0000259|Pfam:PF08652"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 48801 MW; F78B5BEA1E02EB78 CRC64;
MDFSEQDVDV FAEDYNNNDS NNHDDSHESS SSHSSSSSSS ASSSSSASSS PNGSGGGESS
SASGSASSGE EETGEEVGNV NANNYDCNNN SEEGIYGDEE EDERDLFGSD NEDYCKTPAT
SPFSIPVLPV IRNPNNPGRG GFGRGRWQND RGAGILGRPG YPPRQGYGYG SKFANGRHDE
RFVSELKLSK SEETLSRKCI AFQEPCELAC YSRVEGGDVY FDDRSLIMAT AYIRNEPWEM
GVHKRNGVVY LDVHKLPERP RSELDRQRCY WGYCFESLAT EDPRRADGEE IHHIDANAEY
CSVIKTKLGA HRILMGAEMD CCDSTDEGRR FYVELKTSRE LDYHTEERYE REKLLKFWIQ
SFLAGVPYIV IGFRDDAGRL VRTERLRTKD ITHRVKMKNY WQGGVCLAFA DEVLCWLYGT
VKESKILTLI SPSTSA
//
