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Database: UniProt
Entry: A0A0V0RLI4_9BILA
LinkDB: A0A0V0RLI4_9BILA
Original site: A0A0V0RLI4_9BILA 
ID   A0A0V0RLI4_9BILA        Unreviewed;       311 AA.
AC   A0A0V0RLI4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=tRNA-specific adenosine deaminase 2 {ECO:0000256|ARBA:ARBA00019216};
DE   AltName: Full=Deaminase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00033441};
DE   AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT2 {ECO:0000256|ARBA:ARBA00031817};
GN   Name=DEADC1 {ECO:0000313|EMBL:KRX15282.1};
GN   ORFNames=T07_2303 {ECO:0000313|EMBL:KRX15282.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX15282.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX15282.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX15282.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably participates in deamination of adenosine-34 to
CC       inosine in many tRNAs. {ECO:0000256|ARBA:ARBA00002255}.
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:KRX15282.1}.
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DR   EMBL; JYDL01000135; KRX15282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0RLI4; -.
DR   STRING; 6336.A0A0V0RLI4; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR   CDD; cd01285; nucleoside_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR028883; tRNA_aden_deaminase.
DR   PANTHER; PTHR12962; CALCIUM-REGULATED HEAT STABLE PROTEIN CRHSP-24-RELATED; 1.
DR   PANTHER; PTHR12962:SF1; COLD SHOCK DOMAIN-CONTAINING PROTEIN CG9705; 1.
DR   Pfam; PF14437; MafB19-deam; 1.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS51857; CSD_2; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          2..119
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   DOMAIN          215..284
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
SQ   SEQUENCE   311 AA;  35274 MW;  28E11033FEEBF990 CRC64;
     MFSEEKCFEE AFTLARKALS LGEVPVGCVL LYENVIIGRG HNRVNFYKNA CRHAEMEAFD
     EAFLWCKANC LSFNDVFLKT TLFVTCEPCM MCAALICKMQ LKRVVYGCPN DRFGGFGSVL
     DVKETFGHTF PSEIVANYRK DESVKLLQIF YESGAINKVL MDNEAVLNSV PEKDVLQCVS
     AMHDPHHRCM NPPSPLITKR ERRPSLCERA ASGPVHYGRV RYFCRERGHG YITPLDQHPA
     GEDIFVHISD VEGDYAPHDG DEVTYKLCPI PPKFEKMQAV HVVLRNLVAG VKHERWDQPI
     SHPCHTPDSH P
//
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