MULTISPECIES: SPASM domain-containing protein [Bacillus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
AslB super family | cl33987 | Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ... |
2-222 | 2.14e-21 | ||||
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones]; The actual alignment was detected with superfamily member COG0641: Pssm-ID: 440406 [Multi-domain] Cd Length: 349 Bit Score: 91.20 E-value: 2.14e-21
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Name | Accession | Description | Interval | E-value | ||||
AslB | COG0641 | Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ... |
2-222 | 2.14e-21 | ||||
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440406 [Multi-domain] Cd Length: 349 Bit Score: 91.20 E-value: 2.14e-21
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SPASM_CteB-like | cd21124 | Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ... |
143-222 | 1.83e-13 | ||||
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar proteins; Clostridium thermocellum sactionine bond-forming enzyme CteB is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the formation of the requisite thioether bridge between a cysteine and the alpha-carbon of an opposing amino acid that is required in sactipeptide biosynthesis. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM (RS) enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. CteB contains two auxillary 4Fe-4S clusters in its SPASM domain; the auxillary cluster nearest the RS site, called AuxI, exhibits an open coordination site in the absence of peptide substrate, which is coordinated by a peptidyl-cysteine residue in the bound state. Pssm-ID: 410615 [Multi-domain] Cd Length: 96 Bit Score: 64.30 E-value: 1.83e-13
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rSAM_more_4Fe4S | TIGR04085 | radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ... |
137-223 | 1.21e-09 | ||||
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding additional 4Fe4S clusters found in various radical SAM proteins C-terminal to the domain described by model pfam04055. Radical SAM enzymes with this domain tend to be involved in protein modification, including anaerobic sulfatase maturation proteins, a quinohemoprotein amine dehydrogenase biogenesis protein, the Pep1357-cyclizing radical SAM enzyme, and various bacteriocin biosynthesis proteins. The motif CxxCxxxxxCxxxC is nearly invariant for members of this family, although PqqE has a variant form. We name this domain SPASM for Subtilosin, PQQ, Anaerobic Sulfatase, and Mycofactocin. Pssm-ID: 274968 [Multi-domain] Cd Length: 93 Bit Score: 53.73 E-value: 1.21e-09
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Name | Accession | Description | Interval | E-value | ||||
AslB | COG0641 | Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ... |
2-222 | 2.14e-21 | ||||
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440406 [Multi-domain] Cd Length: 349 Bit Score: 91.20 E-value: 2.14e-21
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SPASM_CteB-like | cd21124 | Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ... |
143-222 | 1.83e-13 | ||||
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar proteins; Clostridium thermocellum sactionine bond-forming enzyme CteB is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the formation of the requisite thioether bridge between a cysteine and the alpha-carbon of an opposing amino acid that is required in sactipeptide biosynthesis. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM (RS) enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. CteB contains two auxillary 4Fe-4S clusters in its SPASM domain; the auxillary cluster nearest the RS site, called AuxI, exhibits an open coordination site in the absence of peptide substrate, which is coordinated by a peptidyl-cysteine residue in the bound state. Pssm-ID: 410615 [Multi-domain] Cd Length: 96 Bit Score: 64.30 E-value: 1.83e-13
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rSAM_more_4Fe4S | TIGR04085 | radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ... |
137-223 | 1.21e-09 | ||||
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding additional 4Fe4S clusters found in various radical SAM proteins C-terminal to the domain described by model pfam04055. Radical SAM enzymes with this domain tend to be involved in protein modification, including anaerobic sulfatase maturation proteins, a quinohemoprotein amine dehydrogenase biogenesis protein, the Pep1357-cyclizing radical SAM enzyme, and various bacteriocin biosynthesis proteins. The motif CxxCxxxxxCxxxC is nearly invariant for members of this family, although PqqE has a variant form. We name this domain SPASM for Subtilosin, PQQ, Anaerobic Sulfatase, and Mycofactocin. Pssm-ID: 274968 [Multi-domain] Cd Length: 93 Bit Score: 53.73 E-value: 1.21e-09
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SPASM_AlbA-like | cd21125 | Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis ... |
148-224 | 3.03e-06 | ||||
Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis protein AlbA and similar proteins; Bacillus subtilis antilisterial bacteriocin subtilosin biosynthesis protein AlbA is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the formation of three thioether bonds in the post-translational modification of a linear peptide into the cyclic peptide subtilosin A. The thioether bonds formed are between the sulfur of three cysteine residues and the alpha-carbons of two phenylalanines and one threonine to produce a rigid cyclic peptide. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. AlbA appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN. Pssm-ID: 410616 [Multi-domain] Cd Length: 97 Bit Score: 44.40 E-value: 3.03e-06
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rSAM_pep_methan | TIGR04083 | putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ... |
145-209 | 2.93e-03 | ||||
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are radical SAM enzymes, homologous to a variety of other peptide-modifying radical SAM, and found primarily in methanogenic archaea. Pssm-ID: 274966 [Multi-domain] Cd Length: 376 Bit Score: 38.17 E-value: 2.93e-03
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Blast search parameters | ||||
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