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Database: UniProt
Entry: K7B6Y4_PANTR
LinkDB: K7B6Y4_PANTR
Original site: K7B6Y4_PANTR 
ID   K7B6Y4_PANTR            Unreviewed;       396 AA.
AC   K7B6Y4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE            EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
GN   Name=DOM3Z {ECO:0000313|EMBL:JAA07785.1};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA07785.1};
RN   [1] {ECO:0000313|EMBL:JAA07785.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA07785.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA +
CC         a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:67496,
CC         Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57328, ChEBI:CHEBI:138282,
CC         ChEBI:CHEBI:172371; Evidence={ECO:0000256|ARBA:ARBA00024564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67497;
CC         Evidence={ECO:0000256|ARBA:ARBA00024564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end
CC         phospho-ribonucleoside in mRNA + FAD + H(+); Xref=Rhea:RHEA:67492,
CC         Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:138282,
CC         ChEBI:CHEBI:172372; Evidence={ECO:0000256|ARBA:ARBA00024458};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493;
CC         Evidence={ECO:0000256|ARBA:ARBA00024458};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in snoRNA + H2O = a 5'-
CC         end phospho-ribonucleoside in snoRNA + H(+) + NAD(+);
CC         Xref=Rhea:RHEA:60892, Rhea:RHEA-COMP:15699, Rhea:RHEA-COMP:15700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC         Evidence={ECO:0000256|ARBA:ARBA00023687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60893;
CC         Evidence={ECO:0000256|ARBA:ARBA00023687};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU367113};
CC       Note=Binds 2 magnesium ions. {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; GABC01003553; JAA07785.1; -; mRNA.
DR   AlphaFoldDB; K7B6Y4; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|RuleBase:RU367113};
KW   Magnesium {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   RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT   DOMAIN          235..301
FT                   /note="RAI1-like"
FT                   /evidence="ECO:0000259|Pfam:PF08652"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  44886 MW;  2E91110895726111 CRC64;
     MDPRGTKRGA EKTEVAEPRN KLPRPAPSLP TDPALYSGPF PFYRRPSELG CFSLDAQRQY
     HGDARALRYY SPPPTNGPGP NFDLRDGYPD RYQPRDEEVQ ERLDHLLCWL LEHRGRLEGG
     PGWLAEAIVT WRGHLTKLLT TPYERQEGWQ LAASRFQGTL YLSEVETPNA RAQRLARPPL
     LRELMYMGYK FEQYMCADKP GSSPDPSGEV NTNVAFCSVL RSRLGSHPLL FSGEVDCTDP
     QAPSTQPPTC YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPNVV VGFRNPDGFV
     SSLKTFPTMK MFEYVRNDGD GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV HLFSWEPGGP
     VTVSVHRDAP YAFLPIWYVE AMTQDLPSPP KTPSPK
//
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