Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup methylthiotransferase

  ⌊ FunctionalDomain uncharacterized Radical SAM superfamily sequence (ID 403587)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermotoga maritima MSB8 Taxon ID: 243274 152149505 PRP URP
Thermotoga maritima MSB8 Taxon ID: 243274 152149504 PRP URP
Thermotoga maritima MSB8 Taxon ID: 243274 152149503 PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
Ribosomal protein S12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865} Q9X2H6 RIMO_THEMA (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 304 | Length of Functional Domain: 299

1       10        20        30        40        50        60

EERPYAYVKISDGCDRGCTFCSIPSFKGSLRSRSIEDITREVEDLLKEGKKEIILVAQDT
TSYGIDLYRKQALPDLLRRLNSLNGEFWIRVXYLHPDHLTEEIISAXLELDKVVKYFDVP
VQHGSDKILKLXGRTKSSEELKKXLSSIRERFPDAVLRTSIIVGFPGETEEDFEELKQFV
EEIQFDKLGAFVYSDEEGTVAFNLKEKVDPEXAKRRQEELLLLQAEISNSRLDRFVGKKL
KFLVEGKEGKFLVGRTWTEAPEVDGVVFVRGKGKIGDFLEVVIKEHDEYDXWGSVILEHH
HHHH
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
14 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
18 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
21 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
14 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
18 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
21 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2QGQ Crystal Structure Of Tm_1862 From Thermotoga Maritima. Northeast Structural Genomics Consortium Target Vr77 Protein Tm_1862 7 2.0 Selenomethionine • 3-Cyclohexyl-1-Propylsulfonic Acid CSA • PDB • PDBSum
4JC0 Crystal Structure Of Thermotoga Maritima Holo Rimo In Complex With Pentasulfide, Northeast Structural Genomics Consortium Target Vr77 Ribosomal Protein S12 Methylthiotransferase Rimo 7 3.3 Iron/Sulfur Penta-Sulfide Connected Clusters CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Oct. 16, 2014, 5:17 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.