Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  ⌊ main SPASM domain-containing

  ⌊ thioether bond formation requiring one auxiliary iron-sulfur cluster

     ⌊ Family sporulation killing factor protein (SkfB-like)

  ⌊ FunctionalDomain sporulation killing factor maturation protein (SkfB) (ID 280459)

Superfamily Assignment Evidence Code(s) ISS PubMed:23282011
Family Assignment Evidence Code CFM PubMed:23282011
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus subtilis subsp. subtilis str. 168 Taxon ID: 224308 50812176 NP_388073.2 (RefSeq) PRP URP
Bacillus subtilis Taxon ID: 1423 489327611 WP_003234902.1 (RefSeq) URP
Bacillus subtilis Taxon ID: 1423 857327482 KMN95355.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Sporulation killing factor maturation protein SkfB O31423 SKFB_BACSU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 410 | Length of Functional Domain: 410

1       10        20        30        40        50        60

MSYDRVKDFDLPELAVHLQPHGAVMIDRKSMFYFRLSGRGAQLAFLLSKNKNLHKTARIW
EIMKKEEMSADQLKEELSAHPFTEAWTEGLLDQPLHVSGSLDSYLPISCTLQLTNACNLS
CSFCYASSGKPYPEELSSEQWILVMQKLAAHGVADITLTGGEAKLIKGFKELVVVASSLF
TNVNVFSNGLNWRDEEVELLSHLGNVSVQISIDGMDNTHDQLRGRKGGFKESMNTIKKLS
EANIPVIVAMTINESNADEVSDVVEQCANAGAFIFRAGKTLSVGRATEGFKALDIDFEEM
VQIQLREARHKWGDRLNIIDWEHEESSFTTDFCTPGYLAWYIRADGYVTPCQLEDLPLGH
ILEDSMADIGSPARLLQLKCEAKNCKCIGKIELSEPDLPFQKEVKAGIQE
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
117 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
121 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
124 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
117 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
121 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
124 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
380 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
385 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
387 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
117 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IMP PubMed:23282011
121 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IMP PubMed:23282011
124 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IMP PubMed:23282011
380 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IMP PubMed:23282011
385 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IMP PubMed:23282011
387 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IMP PubMed:23282011

Catalyzed Reaction

thioether cross-link between Cys and Met

+ + + +
cysteine residue
32460		 methionine residue
32648		 S-adenosyl-L-methionine zwitterion
59789		 Cys-Met thioether
132410		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:01 a.m. update curation agent holliday setDomainBoundaries.py
update domain start position 21 30
July 15, 2014, 4:54 a.m. update curation agent setDomainBoundaries.py holliday
Oct. 16, 2014, 7:38 a.m. update curation agent holliday setDomainBoundaries.py
Oct. 15, 2016, 7:36 a.m. update domain end position 391 410
update domain start position 30 1
EC number assigned by UniProtKB accession ID.