(data stored in ACNUC7421 zone)

SWISSPROT: TTCA_STRM5

ID   TTCA_STRM5              Reviewed;         298 AA.
AC   B4SRP3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 62.
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};
GN   OrderedLocusNames=Smal_0058;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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
CC       atoms are provided by the cysteine/cysteine desulfurase (IscS)
CC       system. {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
CC       by three Cys residues, the fourth Fe has a free coordination site
CC       that may bind a sulfur atom transferred from the persulfide of
CC       IscS. {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
CC       steps: a first activation step by ATP to form an adenylated
CC       intermediate of the target base of tRNA, and a second nucleophilic
CC       substitution step of the sulfur (S) atom supplied by the
CC       hydrosulfide attached to the Fe-S cluster. {ECO:0000255|HAMAP-
CC       Rule:MF_01850}.
CC   -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01850}.
DR   EMBL; CP001111; ACF49763.1; -; Genomic_DNA.
DR   RefSeq; WP_012509638.1; NC_011071.1.
DR   SMR; B4SRP3; -.
DR   STRING; 391008.Smal_0058; -.
DR   EnsemblBacteria; ACF49763; ACF49763; Smal_0058.
DR   KEGG; smt:Smal_0058; -.
DR   eggNOG; ENOG4105CB3; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000013323; -.
DR   KO; K14058; -.
DR   OMA; PCKACVL; -.
DR   OrthoDB; 1051352at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00290-MONOMER; -.
DR   Proteomes; UP000001867; 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; B4SRP3.
DR   SWISS-2DPAGE; B4SRP3.
KW   4Fe-4S; ATP-binding; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Magnesium; Metal-binding; Nucleotide-binding; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN         1    298       tRNA-cytidine(32) 2-sulfurtransferase.
FT                                /FTId=PRO_1000188662.
FT   MOTIF        57     62       PP-loop motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_01850}.
FT   METAL       132    132       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01850}.
FT   METAL       135    135       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01850}.
FT   METAL       223    223       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01850}.
SQ   SEQUENCE   298 AA;  32895 MW;  E3FD8DED90B95066 CRC64;
     MTAVISLPDP PQRASRGPRV AGPGQDRLGK RLRRQVGQAI ADFGMIEAGD KVMVCLSGGK
     DSYTLLDLLL QLQKRAPVPF ELVAVNLDQK QPGFPEHVLP EYLAALGVPY QIIEQDTYSV
     VSRVIPEGRT MCSLCSRLRR GALYNHAKAH GFTRIALGHH CDDMVATLFM NLFHHAKLAA
     MPPKLLSDDG QHVVIRPLAY VREHDIAEYA QARRFPIIPC TLCGSQESLQ RRQVGLMLKQ
     WDQDHPGRIE QIARAMADVR PAQLADATLF DFRALGHSGH AAHADAWLAD AVPETPAD
//

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