(data stored in ACNUC7421 zone)

SWISSPROT: TTCA_RHILO

ID   TTCA_RHILO              Reviewed;         295 AA.
AC   Q98NP4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=tRNA-cytidine(32) 2-sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_01850};
DE            EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_01850};
DE   AltName: Full=Two-thiocytidine biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01850};
DE   AltName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000255|HAMAP-Rule:MF_01850};
GN   Name=ttcA {ECO:0000255|HAMAP-Rule:MF_01850}; OrderedLocusNames=mlr0047;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Catalyzes the ATP-dependent 2-thiolation of cytidine in
CC       position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms
CC       are provided by the cysteine/cysteine desulfurase (IscS) system.
CC       {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by
CC       three Cys residues, the fourth Fe has a free coordination site that may
CC       bind a sulfur atom transferred from the persulfide of IscS.
CC       {ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- MISCELLANEOUS: The thiolation reaction likely consists of two steps: a
CC       first activation step by ATP to form an adenylated intermediate of the
CC       target base of tRNA, and a second nucleophilic substitution step of the
CC       sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S
CC       cluster. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01850}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47717.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; BA000012; BAB47717.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_032930041.1; NC_002678.2.
DR   SMR; Q98NP4; -.
DR   STRING; 266835.14021104; -.
DR   EnsemblBacteria; BAB47717; BAB47717; BAB47717.
DR   KEGG; mlo:mlr0047; -.
DR   eggNOG; ENOG4105CB3; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000013323; -.
DR   KO; K14058; -.
DR   OrthoDB; 1051352at2; -.
DR   BioCyc; MLOT266835:G1G20-36-MONOMER; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01850; TtcA; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012089; tRNA_Cyd_32_2_STrfase.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q98NP4.
DR   SWISS-2DPAGE; Q98NP4.
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Nucleotide-binding; RNA-binding; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..295
FT                   /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT                   /id="PRO_0000348816"
FT   MOTIF           63..68
FT                   /note="PP-loop motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           138
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           141
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           229
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ   SEQUENCE   295 AA;  33168 MW;  3AAA2F460E47FFA0 CRC64;
     MNMLPDIETL ETAAEGGSHP LFADVPSSVE FNKLRKRLLR LTRQAIEDFS MVEPGQRWLV
     ALSGGKDSYG LLALLLDLKW RGLLPVELLA CNLDQGQPNF PKHILPDYLN ANGIAHRIEY
     QDTYSVVTNK LPEGSTYCSL CSRLRRGHLY RIAREEGCSA LVLGHHREDI LETFFMNLFH
     GGRLAAMPPK LLNDEGDVMV LRPLSYCAEI DLEKFAAAMR FPIIPCDLCG SQEGLQRNAM
     KAMLEDIEKR MPGRKDTMIR ALSNTRPSHL LDRKLFDFAA LNQTLITGQD ASDDI
//

If you have problems or comments...

PBIL Back to PBIL home page