TAD2_SCHPO
ID TAD2_SCHPO Reviewed; 389 AA.
AC O94642;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=tRNA-specific adenosine deaminase subunit tad2;
DE EC=3.5.4.33;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit tad2;
GN Name=tad2 {ECO:0000250|UniProtKB:P47058}; ORFNames=SPBC16D10.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Deaminates adenosine-34 to inosine in many tRNAs.
CC {ECO:0000250|UniProtKB:P47058}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O67050};
CC -!- SUBUNIT: Heterodimer with tad3. {ECO:0000250|UniProtKB:P47058}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000255}.
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DR EMBL; CU329671; CAB38514.2; -; Genomic_DNA.
DR PIR; T39574; T39574.
DR RefSeq; NP_596505.2; NM_001022426.2.
DR PDB; 7EEY; X-ray; 2.60 A; A/B/C/D=1-202.
DR PDBsum; 7EEY; -.
DR AlphaFoldDB; O94642; -.
DR SMR; O94642; -.
DR BioGRID; 276190; 1.
DR IntAct; O94642; 1.
DR STRING; 4896.SPBC16D10.10.1; -.
DR MaxQB; O94642; -.
DR PaxDb; O94642; -.
DR EnsemblFungi; SPBC16D10.10.1; SPBC16D10.10.1:pep; SPBC16D10.10.
DR GeneID; 2539634; -.
DR KEGG; spo:SPBC16D10.10; -.
DR PomBase; SPBC16D10.10; tad2.
DR VEuPathDB; FungiDB:SPBC16D10.10; -.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_710102_0_0_1; -.
DR InParanoid; O94642; -.
DR OMA; YMKLAHE; -.
DR PhylomeDB; O94642; -.
DR PRO; PR:O94642; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0052718; C:tRNA-specific adenosine-34 deaminase complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IDA:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..389
FT /note="tRNA-specific adenosine deaminase subunit tad2"
FT /id="PRO_0000310823"
FT DOMAIN 212..325
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 268
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 43603 MW; 0182DE8A2DC3606C CRC64;
MAGDSVKSAI IGIAGGPFSG KTQLCEQLLE RLKSSAPSTF SKLIHLTSFL YPNSVDRYAL
SSYDIEAFKK VLSLISQGAE KICLPDGSCI KLPVDQNRII LIEGYYLLLP ELLPYYTSKI
FVYEDADTRL ERCVLQRVKA EKGDLTKVLN DFVTLSKPAY DSSIHPTREN ADIILPQKEN
IDTALLFVSQ HLQDILAEMN KTSSSNTVKY DTQHETYMKL AHEILNLGPY FVIQPRSPGS
CVFVYKGEVI GRGFNETNCS LSGIRHAELI AIEKILEHYP ASVFKETTLY VTVEPCLMCA
AALKQLHIKA VYFGCGNDRF GGCGSVFSIN KDQSIDPSYP VYPGLFYSEA VMLMREFYVQ
ENVKAPVPQS KKQRVLKREV KSLDLSRFK
