MULTISPECIES: staphylobilin-forming heme oxygenase IsdI [Staphylococcus]
antibiotic biosynthesis monooxygenase family protein( domain architecture ID 10014189)
antibiotic biosynthesis monooxygenase family protein may be involved in the biosynthesis of several antibiotics; similar to Streptomyces ambofaciens anthrone oxidase-like protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PRK13313 | PRK13313 | staphylobilin-forming heme oxygenase IsdI; |
1-108 | 7.37e-66 | |||
staphylobilin-forming heme oxygenase IsdI; : Pssm-ID: 183968 Cd Length: 108 Bit Score: 194.00 E-value: 7.37e-66
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Name | Accession | Description | Interval | E-value | |||
PRK13313 | PRK13313 | staphylobilin-forming heme oxygenase IsdI; |
1-108 | 7.37e-66 | |||
staphylobilin-forming heme oxygenase IsdI; Pssm-ID: 183968 Cd Length: 108 Bit Score: 194.00 E-value: 7.37e-66
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HmoA | COG2329 | Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ... |
1-80 | 2.54e-15 | |||
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism]; Pssm-ID: 441901 Cd Length: 98 Bit Score: 65.40 E-value: 2.54e-15
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ABM | pfam03992 | Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ... |
2-76 | 1.78e-14 | |||
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue. Pssm-ID: 427635 Cd Length: 74 Bit Score: 62.67 E-value: 1.78e-14
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Name | Accession | Description | Interval | E-value | |||
PRK13313 | PRK13313 | staphylobilin-forming heme oxygenase IsdI; |
1-108 | 7.37e-66 | |||
staphylobilin-forming heme oxygenase IsdI; Pssm-ID: 183968 Cd Length: 108 Bit Score: 194.00 E-value: 7.37e-66
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PRK13312 | PRK13312 | staphylobilin-forming heme oxygenase IsdG; |
2-108 | 1.37e-40 | |||
staphylobilin-forming heme oxygenase IsdG; Pssm-ID: 139480 Cd Length: 107 Bit Score: 129.85 E-value: 1.37e-40
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PRK13315 | PRK13315 | heme oxygenase; |
1-102 | 6.62e-25 | |||
heme oxygenase; Pssm-ID: 237345 Cd Length: 107 Bit Score: 90.24 E-value: 6.62e-25
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PRK13314 | PRK13314 | heme oxygenase; |
1-102 | 2.66e-16 | |||
heme oxygenase; Pssm-ID: 183969 Cd Length: 107 Bit Score: 68.37 E-value: 2.66e-16
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HmoA | COG2329 | Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ... |
1-80 | 2.54e-15 | |||
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism]; Pssm-ID: 441901 Cd Length: 98 Bit Score: 65.40 E-value: 2.54e-15
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ABM | pfam03992 | Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ... |
2-76 | 1.78e-14 | |||
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue. Pssm-ID: 427635 Cd Length: 74 Bit Score: 62.67 E-value: 1.78e-14
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PRK13316 | PRK13316 | heme oxygenase IsdG; |
1-102 | 3.88e-09 | |||
heme oxygenase IsdG; Pssm-ID: 183970 Cd Length: 121 Bit Score: 50.14 E-value: 3.88e-09
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Blast search parameters | ||||
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