(data stored in SCRATCH zone)

SWISSPROT: C7PXD4_CATAD

ID   C7PXD4_CATAD            Unreviewed;       474 AA.
AC   C7PXD4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   05-JUL-2017, entry version 56.
DE   RecName: Full=Ribosomal protein S12 methylthiotransferase RimO {ECO:0000256|HAMAP-Rule:MF_01865, ECO:0000256|SAAS:SAAS00766429};
DE            Short=S12 MTTase {ECO:0000256|HAMAP-Rule:MF_01865};
DE            Short=S12 methylthiotransferase {ECO:0000256|HAMAP-Rule:MF_01865};
DE            EC=2.8.4.4 {ECO:0000256|HAMAP-Rule:MF_01865, ECO:0000256|SAAS:SAAS00766432};
DE   AltName: Full=Ribosomal protein S12 (aspartate-C(3))-methylthiotransferase {ECO:0000256|HAMAP-Rule:MF_01865};
DE   AltName: Full=Ribosome maturation factor RimO {ECO:0000256|HAMAP-Rule:MF_01865};
GN   Name=rimO {ECO:0000256|HAMAP-Rule:MF_01865};
GN   OrderedLocusNames=Caci_0547 {ECO:0000313|EMBL:ACU69485.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69485.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69485.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid
CC       residue of ribosomal protein S12. {ECO:0000256|HAMAP-
CC       Rule:MF_01865}.
CC   -!- CATALYTIC ACTIVITY: L-aspartate-[ribosomal protein S12] + sulfur-
CC       (sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-
CC       aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine +
CC       (sulfur carrier) + L-methionine + 5'-deoxyadenosine.
CC       {ECO:0000256|HAMAP-Rule:MF_01865, ECO:0000256|SAAS:SAAS00766448}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01865};
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01865};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01865,
CC       ECO:0000256|SAAS:SAAS00766458}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. RimO
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01865,
CC       ECO:0000256|SAAS:SAAS00766451}.
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DR   EMBL; CP001700; ACU69485.1; -; Genomic_DNA.
DR   RefSeq; WP_012784780.1; NC_013131.1.
DR   ProteinModelPortal; C7PXD4; -.
DR   STRING; 479433.Caci_0547; -.
DR   EnsemblBacteria; ACU69485; ACU69485; Caci_0547.
DR   KEGG; cai:Caci_0547; -.
DR   eggNOG; ENOG4105CBM; Bacteria.
DR   eggNOG; COG0621; LUCA.
DR   HOGENOM; HOG000224766; -.
DR   OrthoDB; POG091H006S; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01865; MTTase_RimO; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR005840; Ribosomal_S12_MeSTrfase_RimO.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   PANTHER; PTHR43837; PTHR43837; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDF00274; ribosomal_protein_S12_methylth; 1.
DR   SFLD; SFLDG01061; methylthiotransferase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR01125; TIGR01125; 1.
DR   PROSITE; PS51449; MTTASE_N; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS50926; TRAM; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7PXD4.
DR   SWISS-2DPAGE; C7PXD4.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01865,
KW   ECO:0000256|SAAS:SAAS00766439};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01865,
KW   ECO:0000256|SAAS:SAAS00766435};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01865, ECO:0000256|SAAS:SAAS00766413};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01865,
KW   ECO:0000256|SAAS:SAAS00766434};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01865,
KW   ECO:0000256|SAAS:SAAS00766449};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01865,
KW   ECO:0000256|SAAS:SAAS00766438};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01865,
KW   ECO:0000256|SAAS:SAAS00766426}.
FT   DOMAIN        6    120       MTTase N-terminal. {ECO:0000259|PROSITE:
FT                                PS51449}.
FT   DOMAIN      412    473       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   METAL        15     15       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        54     54       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL       195    195       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01865}.
FT   METAL       199    199       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01865}.
FT   METAL       202    202       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01865}.
SQ   SEQUENCE   474 AA;  50806 MW;  C9FE687D171F8D8A CRC64;
     MAASRGTVSL VTLGCGRNEV DSEELAARLE SAGWELADPD SVPGESDIIV VNTCGFIESA
     KKTSLETLVA ASNAEAKVVA VGCVAERYGK RLAEALPEVD AVLSFDDYPD ISQRLDDVVR
     GKKHESHTPR DRRRLLPIAP VDRANNSSVV APGHGIVRQD SEAGLGGSIF LRKRLGGGGP
     LGDGVVAPLK LASGCDRRCS FCAIPSFRGA FISRTPDDIV AEAEWLADAG VRELILVSEN
     STSYGKDFGD LQALEKLLPR LTSLVSRVRI SYLQPAELRP TLIEAIGGIP GVASYFDLSF
     QHASGPVLRR MRRFGDRERF LELLDKIRVI APEAGMRSNF IVGFPGETED DYGEVERFVS
     EARLDAVGVF GYSDEEGTEA LGLPDKVEQS QIADRVARLT VISRKAMDDR AAERVGSEIE
     VIVKHPGRGW AAHQAPAVDG FVTLTGSSSE AGDVLRARVT GQDGANLIAE ALAK
//

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