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Conserved domains on  [gi|446402748|ref|WP_000480603|]
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MULTISPECIES: staphylobilin-forming heme oxygenase IsdI [Staphylococcus]

Protein Classification

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

Graphical summary

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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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
Cdd:PRK13313   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
                         90       100
                 ....*....|....*....|....*...
gi 446402748  81 LKSDDDGQQSPILSNKVFKYDIGYHYQK 108
Cdd:PRK13313  81 LKSDDDGQQSPILSNKVFKYDIGYHYQK 108
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
Cdd:PRK13313   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
                         90       100
                 ....*....|....*....|....*...
gi 446402748  81 LKSDDDGQQSPILSNKVFKYDIGYHYQK 108
Cdd:PRK13313  81 LKSDDDGQQSPILSNKVFKYDIGYHYQK 108
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQG-IETIEGFQQMFVTKtlNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNV 79
Cdd:COG2329    1 MIVVINRFRVKPGQEEEFEEAFAERRElLAEQPGFLGFELLR--SLEDPGEYLVVSYWESEEAFRAWFRSSEHRAAHAKG 78

                 .
gi 446402748  80 R 80
Cdd:COG2329   79 R 79
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446402748    2 FMAENRLQLQKGSAEETIERFYNR-QGIETIEGFQQMFVTKtlNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAH 76
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELvEATRNEPGCLSYELLR--SLEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
Cdd:PRK13313   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
                         90       100
                 ....*....|....*....|....*...
gi 446402748  81 LKSDDDGQQSPILSNKVFKYDIGYHYQK 108
Cdd:PRK13313  81 LKSDDDGQQSPILSNKVFKYDIGYHYQK 108
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   2 FMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRL 81
Cdd:PRK13312   3 FMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRS 82
                         90       100
                 ....*....|....*....|....*..
gi 446402748  82 KSDDdgQQSPILSNKVFKYDIGYHYQK 108
Cdd:PRK13312  83 KNED--ESSPIINNKVITYDIGYSYMK 107
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNvr 80
Cdd:PRK13315   1 MIVVTNRITVKKGFAAKMAPRFTKGGPLEELEGFHKVEVWLIDNDDEYDEMYVNMWWETEEDFEAWRNSDAFKEAHKR-- 78
                         90       100
                 ....*....|....*....|..
gi 446402748  81 lKSDDDGQQSPILSNKVFKYDI 102
Cdd:PRK13315  79 -PSKTESDDSPIIGSEIVKSEV 99
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHknvr 80
Cdd:PRK13314   1 MIIVTNTAKITKGNGHKLIDRFNKVGKVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAH---- 76
                         90       100
                 ....*....|....*....|..
gi 446402748  81 lkSDDDGQQSPILSNKVFKYDI 102
Cdd:PRK13314  77 --SHQGGMPDYILDNKISYYDV 96
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQG-IETIEGFQQMFVTKtlNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNV 79
Cdd:COG2329    1 MIVVINRFRVKPGQEEEFEEAFAERRElLAEQPGFLGFELLR--SLEDPGEYLVVSYWESEEAFRAWFRSSEHRAAHAKG 78

                 .
gi 446402748  80 R 80
Cdd:COG2329   79 R 79
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446402748    2 FMAENRLQLQKGSAEETIERFYNR-QGIETIEGFQQMFVTKtlNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAH 76
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELvEATRNEPGCLSYELLR--SLEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402748   1 MFMAENRLQLQKGSAEETIERFYNRQG-------IETIEGFQ--QMFVTKTlNTEDTDEVKILTIWESEDSFNNWLNSDV 71
Cdd:PRK13316   1 MIIVTNTIKVEKGAAEHVIRQFTGANGdghptkdIAEVEGFLgfELWHSKP-EDKDYEEVVVTSKWESEEAQRNWVKSDS 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446402748  72 FKEAHKNVRLKSDDDGQQSPILSNKVFKYDI 102
Cdd:PRK13316  80 FKKAHGRTKDTREQREDRKGIVGNAIARFEV 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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