(data stored in ACNUC7421 zone)

SWISSPROT: TTCA_RUEPO

ID   TTCA_RUEPO              Reviewed;         294 AA.
AC   Q5LW09;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 78.
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=SPO0534;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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}.
DR   EMBL; CP000031; AAV93851.1; -; Genomic_DNA.
DR   RefSeq; WP_011046293.1; NC_003911.12.
DR   STRING; 246200.SPO0534; -.
DR   DNASU; 3195432; -.
DR   EnsemblBacteria; AAV93851; AAV93851; SPO0534.
DR   KEGG; sil:SPO0534; -.
DR   eggNOG; ENOG4105CB3; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000013323; -.
DR   KO; K14058; -.
DR   OMA; IGDEACP; -.
DR   OrthoDB; 1051352at2; -.
DR   BioCyc; RPOM246200:G1G48-541-MONOMER; -.
DR   Proteomes; UP000001023; 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; Q5LW09.
DR   SWISS-2DPAGE; Q5LW09.
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..294
FT                   /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT                   /id="PRO_0000348854"
FT   MOTIF           58..63
FT                   /note="PP-loop motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           133
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           136
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           224
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ   SEQUENCE   294 AA;  33530 MW;  788CED00D7592454 CRC64;
     MLDENEDIHP LFAGAPATTE FKKLRKRIVR YTREAIEQYG MVERRADGST PKWLVCLSGG
     KDSYTLLAVL YELKWRGLLP VDLLACNLDQ GQPGFPSTVL PEFLDRMGVP NRIEYQDTYS
     VVVDKVPQGR TYCALCSRLR RGNLYRIARE EGCSAVVLGH HRDDILETFF MNLFHGGRLA
     TMPPKLVNEE GDLFVFRPLA HVAEADCEKF ARAMNYPIIP CDLCGSQDGL QRQQVKQILD
     GWEKNRPGRR QVMFRALMNA RPSHLLDPKL FDFQGLELGS REKGENFGEI PLLR
//

If you have problems or comments...

PBIL Back to PBIL home page