ID A0A0V1H3S2_9BILA Unreviewed; 311 AA.
AC A0A0V1H3S2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:KRZ05256.1};
GN ORFNames=T11_1924 {ECO:0000313|EMBL:KRZ05256.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ05256.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ05256.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ05256.1};
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:KRZ05256.1}.
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DR EMBL; JYDP01000143; KRZ05256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1H3S2; -.
DR STRING; 268475.A0A0V1H3S2; -.
DR Proteomes; UP000055024; 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; PF00313; CSD; 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:UP000055024};
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..283
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
SQ SEQUENCE 311 AA; 35182 MW; DF7A9242B9D30472 CRC64;
MLSEEKCFEE AFTLARKALS IGEVPVGCVL VYENVIIGRG HNRVNFYKNA CRHAEMEAFD
EAFLWCKANC HSFNDVFLKT TLFVTCEPCM MCAALICKMK LKRVVYGCPN DRFGGFGSVL
DVKETFGHTF PSEIVANYRK DESVKLLQIF YESGAINKVI MDNEAVLNSV PEKDVLQCVS
AMQDPDHRCM NPPSPLITKR DRRPSLCERA AMGPVHHGRV RYFCRERGHG YITPLDHQGG
EDIFVHISDV EGDYAPHDGD EVTYKLCPIP PKFEKMQAVH VVLRNLVPGV KHERWDQPIS
HPCHAADSTH P
//
