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Database: UniProt
Entry: V5IF91_IXORI
LinkDB: V5IF91_IXORI
Original site: V5IF91_IXORI 
ID   V5IF91_IXORI            Unreviewed;       187 AA.
AC   V5IF91;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE            EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
DE   Flags: Fragment;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB75621.1};
RN   [1] {ECO:0000313|EMBL:JAB75621.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB75621.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
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; GANP01008847; JAB75621.1; -; mRNA.
DR   AlphaFoldDB; V5IF91; -.
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   2: Evidence at transcript level;
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   RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT   DOMAIN          37..105
FT                   /note="RAI1-like"
FT                   /evidence="ECO:0000259|Pfam:PF08652"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB75621.1"
SQ   SEQUENCE   187 AA;  21064 MW;  F01CB6C3331BE99D CRC64;
     RPGAPPDTNA PLRTGDQFYI VLKGRLESHS LLFSAEVDAI DDDVPHEPGS TAAYVEFKTS
     RIMTHPNQER NFFGKKLLSC WSQSFLAGVP RILFGFRTAD GEVQSVEEFS VEEMPSLAEG
     QWSDRVCLSF LDKMLSFVKE CVTKDDPNVV YLFTYDPKKD ARVVCKKLSD PGEYHILTSS
     YLDAFSH
//
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