CDAT8_METKA
ID CDAT8_METKA Reviewed; 278 AA.
AC Q8TWU6;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=tRNA(cytosine(8)) deaminase;
DE EC=3.5.4.35;
DE AltName: Full=Cytidine deaminase acting on tRNA base C8;
DE Short=CDAT8;
GN OrderedLocusNames=MK0935;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=19407206; DOI=10.1126/science.1170123;
RA Randau L., Stanley B.J., Kohlway A., Mechta S., Xiong Y., Soll D.;
RT "A cytidine deaminase edits C to U in transfer RNAs in Archaea.";
RL Science 324:657-659(2009).
CC -!- FUNCTION: Catalyzes the deamimation of cytosine to uracil at position 8
CC of tRNA in 30 different tRNAs. This editing guarantees the proper
CC folding and functionality of the tRNAs. {ECO:0000269|PubMed:19407206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(8) in tRNA + H(+) + H2O = NH4(+) + uridine(8) in
CC tRNA; Xref=Rhea:RHEA:50964, Rhea:RHEA-COMP:12853, Rhea:RHEA-
CC COMP:12854, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:82748; EC=3.5.4.35;
CC Evidence={ECO:0000269|PubMed:19407206};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19407206};
CC Note=Binds 1 zinc ion. {ECO:0000269|PubMed:19407206};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19407206}.
CC -!- INTERACTION:
CC Q8TWU6; Q8TWU6: MK0935; NbExp=2; IntAct=EBI-26895112, EBI-26895112;
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AE009439; AAM02148.1; -; Genomic_DNA.
DR PDB; 3G8Q; X-ray; 2.40 A; A/B/C/D=1-278.
DR PDBsum; 3G8Q; -.
DR AlphaFoldDB; Q8TWU6; -.
DR SMR; Q8TWU6; -.
DR STRING; 190192.MK0935; -.
DR EnsemblBacteria; AAM02148; AAM02148; MK0935.
DR KEGG; mka:MK0935; -.
DR HOGENOM; CLU_999699_0_0_2; -.
DR BRENDA; 3.5.4.35; 3274.
DR EvolutionaryTrace; Q8TWU6; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR004114; THUMP_dom.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF02926; THUMP; 1.
DR SMART; SM00981; THUMP; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; RNA-binding;
KW tRNA processing; tRNA-binding; Zinc.
FT CHAIN 1..278
FT /note="tRNA(cytosine(8)) deaminase"
FT /id="PRO_0000422595"
FT DOMAIN 1..102
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 175..277
FT /note="THUMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT ACT_SITE 46
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19407206"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19407206"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19407206"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:3G8Q"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:3G8Q"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:3G8Q"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:3G8Q"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:3G8Q"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3G8Q"
SQ SEQUENCE 278 AA; 30618 MW; 6F04884057684B4F CRC64;
MKVSLAGQTV DVKKILNEIP KRTVTAALLE GGEIVAVEEA DDEHAERKLV RRHDVEGKVV
FVTARPCLYC ARELAEAGVA GVVYLGRGRG LGPYYLARSG VEVVEVHPDE PLGYDPVDRL
DVLLTFGGNP YLTEEDVAAR VYCLLTGRGF DADIAPAPEN LSGRVEIMVT RGDPDEAVEL
LKEELPVFRI RRFLISGEFD RDELRERILE DIEPRILDPF AVRARIARAG AFSSSREAEV
FIGDVLTSVG REVNLNDPRT VVTVDVLGPR VSVGVEKR
