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Protein

Ribosomal protein S12 methylthiotransferase RimO

Gene

rimO

Organism
Clostridium botulinum (strain Kyoto / Type A2)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.UniRule annotation

Catalytic activityi

L-aspartate-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine.UniRule annotationSAAS annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi48 – 481Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi82 – 821Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi156 – 1561Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi160 – 1601Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotation

Keywords - Ligandi

4Fe-4SUniRule annotationSAAS annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciCBOT536232:GCO3-2619-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S12 methylthiotransferase RimOUniRule annotationSAAS annotation (EC:2.8.4.4UniRule annotationSAAS annotation)
Short name:
S12 MTTaseUniRule annotation
Short name:
S12 methylthiotransferaseUniRule annotation
Alternative name(s):
Ribosomal protein S12 (aspartate-C(3))-methylthiotransferaseUniRule annotation
Ribosome maturation factor RimOUniRule annotation
Gene namesi
Name:rimOUniRule annotation
Ordered Locus Names:CLM_2699Imported
OrganismiClostridium botulinum (strain Kyoto / Type A2)Imported
Taxonomic identifieri536232 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001374 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliC1FS47.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 119116MTTase N-terminalUniRule annotationAdd
BLAST
Domaini375 – 44167TRAMUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the methylthiotransferase family. RimO subfamily.UniRule annotation
Contains 1 MTTase N-terminal domain.UniRule annotation
Contains 1 TRAM domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0621.
HOGENOMiHOG000224766.
KOiK14441.
OMAiCAIPSFK.
OrthoDBiEOG6P5ZD8.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.80.30.20. 1 hit.
HAMAPiMF_01865. MTTase_RimO.
InterProiIPR006638. Elp3/MiaB/NifB.
IPR023970. MeThioTfrase/rSAM.
IPR005839. Methylthiotransferase.
IPR020612. Methylthiotransferase_CS.
IPR013848. Methylthiotransferase_N.
IPR012340. NA-bd_OB-fold.
IPR005840. Ribosomal_S12_MeSTrfase_RimO.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
IPR002792. TRAM_dom.
[Graphical view]
PANTHERiPTHR11918. PTHR11918. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
PF00919. UPF0004. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00089. TIGR00089. 1 hit.
TIGR01125. TIGR01125. 1 hit.
PROSITEiPS51449. MTTASE_N. 1 hit.
PS01278. MTTASE_RADICAL. 1 hit.
PS50926. TRAM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C1FS47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKIKVALVS LGCDKNRIDS ELMLYKLNEE AELVKNPKEA QVIIVNTCGF
60 70 80 90 100
IETAKEESIN TILQMASYKK THNCKVLVVT GCLTQRYKGE LKELIPEMDI
110 120 130 140 150
MLGVNDYDKL LESIKVFLKS GEKSFYHKYS DTKINEGNRI LTTPTYTAYV
160 170 180 190 200
RIAEGCNNFC TYCAIPRIRG KYRSRKKENI LKEVENLAKQ GVKEIILIAQ
210 220 230 240 250
DTTMYGIDIY GKKVLHELLR DISKVEGVKW IRLLYCYPEE ITKELIEEIK
260 270 280 290 300
NNDKVCKYLD LPIQQISNSV LKRMGRKTTK ETIINIIKKL RKEIEGITLR
310 320 330 340 350
TSLIVGFPGE TEGEFSELKE FVSDVKLDKL GVFKYSKEEG TSAALMKEQI
360 370 380 390 400
DEEIKEKREE EIMILQQSIS KDINKEKIGK IYEVIVEGTK EDMYYGRNYE
410 420 430 440
MSPEIDGEIY FEKDENVKIG DIIKVKVTHS LEYDLIGVVY NELSK
Length:445
Mass (Da):51,361
Last modified:May 26, 2009 - v1
Checksum:iF3A5018A43591715
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001581 Genomic DNA. Translation: ACO86397.1.
RefSeqiWP_004440536.1. NC_012563.1.

Genome annotation databases

EnsemblBacteriaiACO86397; ACO86397; CLM_2699.
KEGGicby:CLM_2699.
PATRICi19381855. VBICloBot91161_2553.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001581 Genomic DNA. Translation: ACO86397.1.
RefSeqiWP_004440536.1. NC_012563.1.

3D structure databases

ProteinModelPortaliC1FS47.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACO86397; ACO86397; CLM_2699.
KEGGicby:CLM_2699.
PATRICi19381855. VBICloBot91161_2553.

Phylogenomic databases

eggNOGiCOG0621.
HOGENOMiHOG000224766.
KOiK14441.
OMAiCAIPSFK.
OrthoDBiEOG6P5ZD8.

Enzyme and pathway databases

BioCyciCBOT536232:GCO3-2619-MONOMER.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.80.30.20. 1 hit.
HAMAPiMF_01865. MTTase_RimO.
InterProiIPR006638. Elp3/MiaB/NifB.
IPR023970. MeThioTfrase/rSAM.
IPR005839. Methylthiotransferase.
IPR020612. Methylthiotransferase_CS.
IPR013848. Methylthiotransferase_N.
IPR012340. NA-bd_OB-fold.
IPR005840. Ribosomal_S12_MeSTrfase_RimO.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
IPR002792. TRAM_dom.
[Graphical view]
PANTHERiPTHR11918. PTHR11918. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
PF00919. UPF0004. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00089. TIGR00089. 1 hit.
TIGR01125. TIGR01125. 1 hit.
PROSITEiPS51449. MTTASE_N. 1 hit.
PS01278. MTTASE_RADICAL. 1 hit.
PS50926. TRAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Clostridium botulinum A2 Kyoto."
    Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Kyoto / Type A2Imported.

Entry informationi

Entry nameiC1FS47_CLOBJ
AccessioniPrimary (citable) accession number: C1FS47
Entry historyi
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: July 22, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.