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Conserved domains on  [gi|489348402|ref|WP_003255511|]
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MULTISPECIES: iron-sulfur cluster insertion protein ErpA [Pseudomonas]

Protein Classification

iron-sulfur cluster insertion protein ErpA( domain architecture ID 10014301)

iron-sulfur cluster insertion protein ErpA is essential for growth and may play a role in isoprenoid biosynthesis

CATH:  2.60.300.12
Gene Ontology:  GO:0005506|GO:0016226|GO:0051537
SCOP:  4003950

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13623 PRK13623
iron-sulfur cluster insertion protein ErpA; Provisional
 1-116 2.33e-78

iron-sulfur cluster insertion protein ErpA; Provisional


:

Pssm-ID: 184186  Cd Length: 115  Bit Score: 225.96  E-value: 2.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   1 MSVETFtPTGLEFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQY 80
Cdd:PRK13623   1 MMSDDV-PLPLVFTDAAAAKVKELIEEEGNPDLKLRVYITGGGCSGFQYGFTFDEQVNEDDTTIEKQGVTLVVDPMSLQY 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489348402  81 LAGAEVDYQEGLEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:PRK13623  80 LVGAEVDYTEGLEGSRFVIKNPNAKTTCGCGSSFSI 115
 
Name Accession Description Interval E-value
PRK13623 PRK13623
iron-sulfur cluster insertion protein ErpA; Provisional
 1-116 2.33e-78

iron-sulfur cluster insertion protein ErpA; Provisional


Pssm-ID: 184186  Cd Length: 115  Bit Score: 225.96  E-value: 2.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   1 MSVETFtPTGLEFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQY 80
Cdd:PRK13623   1 MMSDDV-PLPLVFTDAAAAKVKELIEEEGNPDLKLRVYITGGGCSGFQYGFTFDEQVNEDDTTIEKQGVTLVVDPMSLQY 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489348402  81 LAGAEVDYQEGLEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:PRK13623  80 LVGAEVDYTEGLEGSRFVIKNPNAKTTCGCGSSFSI 115
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 10-116 1.96e-58

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 175.34  E-value: 1.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402  10 GLEFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQ 89
Cdd:COG0316    1 PITLTDAAAKRIKRLLAKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYV 80

                         90       100
                 ....*....|....*....|....*..
gi 489348402  90 EGLEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:COG0316   81 EELLGSGFKFNNPNAKSSCGCGESFSV 107
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 12-116 1.80e-47

Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 272875 [Multi-domain]  Cd Length: 105  Bit Score: 147.73  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   12 EFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQEG 91
Cdd:TIGR00049   1 TLTDSAAKRIKALLAGEGEPNLGLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVEE 80

                          90       100
                  ....*....|....*....|....*
gi 489348402   92 LEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:TIGR00049  81 LLGSGFTFTNPNAKGTCGCGKSFSV 105
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
 11-111 7.26e-17

Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster biosynthesis. Its members include proteins that are involved in nitrogen fixation such as the HesB and HesB-like proteins.


Pssm-ID: 426304  Cd Length: 111  Bit Score: 69.98  E-value: 7.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   11 LEFTHGAAQKVKNLVNEEGNErlkLRVFVTGGG-------CS-GFQYGFTF-DEDVAEDDTIVEREGVSLVVDPMSFQYL 81
Cdd:pfam01521   3 ITITDAAAERLKKLLAGDKKE---LRLDVDDGGgpyskggCSiGGKFSLVLvDEPDPDYDEVIESNGGPIYVDSYSLPFL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 489348402   82 -AGAEVDYQEGLEGSRFVIKNPNAATTCGCG 111
Cdd:pfam01521  80 dEGLTLDFVEDLGTLGLKSDNGNLDGNVGCG 110
IscA_HesB_Se NF038090
IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, ...
 11-112 1.38e-06

IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, are homologous to proteins of iron-sulfur cluster biosynthesis such as IscA, and belong to the broader set of HesB-related proteins.


Pssm-ID: 411672  Cd Length: 99  Bit Score: 43.09  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402  11 LEFTHGAAQKVKNLVnEEGNERLKLRVFVTGGGCSGFQYGFTFDEDvAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQE 90
Cdd:NF038090   2 LEVTDLASRKLKEYF-ADKKIDSPIRVFLNQGGUAGPSLGLALDEP-KENDEVFEQDGLTFVIDKELLEQCGPIKVDFID 79

                         90       100
                 ....*....|....*....|..
gi 489348402  91 GLEGsrFVIKNPNAATTCGCGS 112
Cdd:NF038090  80 CRSG--FSITSSMPLGGGGCGS 99
 
Name Accession Description Interval E-value
PRK13623 PRK13623
iron-sulfur cluster insertion protein ErpA; Provisional
 1-116 2.33e-78

iron-sulfur cluster insertion protein ErpA; Provisional


Pssm-ID: 184186  Cd Length: 115  Bit Score: 225.96  E-value: 2.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   1 MSVETFtPTGLEFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQY 80
Cdd:PRK13623   1 MMSDDV-PLPLVFTDAAAAKVKELIEEEGNPDLKLRVYITGGGCSGFQYGFTFDEQVNEDDTTIEKQGVTLVVDPMSLQY 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489348402  81 LAGAEVDYQEGLEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:PRK13623  80 LVGAEVDYTEGLEGSRFVIKNPNAKTTCGCGSSFSI 115
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 10-116 1.96e-58

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 175.34  E-value: 1.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402  10 GLEFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQ 89
Cdd:COG0316    1 PITLTDAAAKRIKRLLAKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYV 80

                         90       100
                 ....*....|....*....|....*..
gi 489348402  90 EGLEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:COG0316   81 EELLGSGFKFNNPNAKSSCGCGESFSV 107
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 12-116 1.80e-47

Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 272875 [Multi-domain]  Cd Length: 105  Bit Score: 147.73  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   12 EFTHGAAQKVKNLVNEEGNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQEG 91
Cdd:TIGR00049   1 TLTDSAAKRIKALLAGEGEPNLGLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVEE 80

                          90       100
                  ....*....|....*....|....*
gi 489348402   92 LEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:TIGR00049  81 LLGSGFTFTNPNAKGTCGCGKSFSV 105
PLN03082 PLN03082
Iron-sulfur cluster assembly; Provisional
 4-116 4.46e-28

Iron-sulfur cluster assembly; Provisional


Pssm-ID: 215564  Cd Length: 163  Bit Score: 100.39  E-value: 4.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   4 ETFTPTGLEFTHGAAQKVKNLVNEEGNERLK-LRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLA 82
Cdd:PLN03082  48 SSASLDAVHMTDNCIRRLKELQTSEPSAEDKmLRLSVETGGCSGFQYVFELDDKTNSDDRVFEKDGVKLVVDNISYDFVK 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489348402  83 GAEVDYQEGLEGSRFVIK-NPNAATTCGCGSSFSI 116
Cdd:PLN03082 128 GATVDYVEELIRSAFVVStNPSAVGGCSCKSSFMV 162
sufA_proteo TIGR01997
FeS assembly scaffold SufA; This model represents the SufA protein of the SUF system of ...
 9-116 1.59e-21

FeS assembly scaffold SufA; This model represents the SufA protein of the SUF system of iron-sulfur cluster biosynthesis. This system performs FeS biosynthesis even during oxidative stress and tends to be absent in obligate anaerobic and microaerophilic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 131052  Cd Length: 107  Bit Score: 81.80  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402    9 TGLEFTHGAAQKVKNLVNEEGnERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDY 88
Cdd:TIGR01997   1 AVITLTDAAAIHIRELVAKRP-EAVGIRLGVKKTGCAGMEYVLDLVSEPKKDDDLIEHDGAKVFVAPEAVLFILGTQVDF 79

                          90       100
                  ....*....|....*....|....*...
gi 489348402   89 QEGLEGSRFVIKNPNAATTCGCGSSFSI 116
Cdd:TIGR01997  80 VRTTLRQGFKFNNPNATSACGCGESFEL 107
iscA PRK09502
iron-sulfur cluster assembly protein IscA;
11-116 1.26e-19

iron-sulfur cluster assembly protein IscA;


Pssm-ID: 181914 [Multi-domain]  Cd Length: 107  Bit Score: 77.22  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402  11 LEFTHGAAQKVKNLVNEEGnERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDY-Q 89
Cdd:PRK09502   3 ITLSDSAAARVNTFLANRG-KGFGLRLGVRTSGCSGMAYVLEFVDEPTPEDIVFEDKGVKVVVDGKSLQFLDGTQLDFvK 81

                         90       100
                 ....*....|....*....|....*...
gi 489348402  90 EGL-EGSRFviKNPNAATTCGCGSSFSI 116
Cdd:PRK09502  82 EGLnEGFKF--TNPNVKDECGCGESFHV 107
sufA PRK09504
iron-sulfur cluster assembly scaffold protein; Provisional
 1-116 2.90e-18

iron-sulfur cluster assembly scaffold protein; Provisional


Pssm-ID: 181915  Cd Length: 122  Bit Score: 74.00  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   1 MSVETFTPT-----GLEFTHGAAQKVKNLVNEEgNERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDP 75
Cdd:PRK09504   3 MHSGTFNPDdfawqGLTLTPAAAAHIRELMAKQ-PGMKGVRLGVKQTGCAGFGYVLDSVSEPDKDDLVFEHDGAKLFVPL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489348402  76 MSFQYLAGAEVDY-QEGLEgSRFVIKNPNAATTCGCGSSFSI 116
Cdd:PRK09504  82 QAMPFIDGTEVDYvREGLN-QIFKFHNPKAQNECGCGESFGV 122
IscA TIGR02011
iron-sulfur cluster assembly protein IscA; This model represents the IscA component of the ISC ...
 14-116 3.02e-18

iron-sulfur cluster assembly protein IscA; This model represents the IscA component of the ISC system for iron-sulfur cluster assembly. The ISC system consists of IscRASU, HscAB and an Isc-specific ferredoxin. IscA previously was believed to act as a scaffold and now is seen as an iron donor protein. This clade is limited to the proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213674  Cd Length: 105  Bit Score: 73.32  E-value: 3.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   14 THGAAQKVKNLVNEEGnERLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDY-QEGL 92
Cdd:TIGR02011   4 TDSAAARVNTFLANRG-KGFGLRLGVKTSGCSGMAYVLEFVDEPTPDDIVFEDKGVKIVIDGKSLQYLDGTQLDFvKEGL 82

                          90       100
                  ....*....|....*....|....*
gi 489348402   93 -EGSRFviKNPNAATTCGCGSSFSI 116
Cdd:TIGR02011  83 nEGFKF--TNPNVKDECGCGESFHV 105
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
 11-111 7.26e-17

Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster biosynthesis. Its members include proteins that are involved in nitrogen fixation such as the HesB and HesB-like proteins.


Pssm-ID: 426304  Cd Length: 111  Bit Score: 69.98  E-value: 7.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402   11 LEFTHGAAQKVKNLVNEEGNErlkLRVFVTGGG-------CS-GFQYGFTF-DEDVAEDDTIVEREGVSLVVDPMSFQYL 81
Cdd:pfam01521   3 ITITDAAAERLKKLLAGDKKE---LRLDVDDGGgpyskggCSiGGKFSLVLvDEPDPDYDEVIESNGGPIYVDSYSLPFL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 489348402   82 -AGAEVDYQEGLEGSRFVIKNPNAATTCGCG 111
Cdd:pfam01521  80 dEGLTLDFVEDLGTLGLKSDNGNLDGNVGCG 110
PRK11190 PRK11190
iron-sulfur cluster biogenesis protein NfuA;
17-104 1.06e-07

iron-sulfur cluster biogenesis protein NfuA;


Pssm-ID: 183027 [Multi-domain]  Cd Length: 192  Bit Score: 47.70  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402  17 AAQK--VKNLVNEEgnERLKLRVFVTGGGCSGFQYGFTF--DEDVAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQEGL 92
Cdd:PRK11190   7 AAQAhfAKLLANQE--EGTQIRVFVINPGTPNAECGVSYcpPDAVEATDTELKFDGFSAYVDELSAPFLEDAEIDFVTDQ 84

                         90
                 ....*....|..
gi 489348402  93 EGSRFVIKNPNA 104
Cdd:PRK11190  85 LGSQLTLKAPNA 96
IscA_HesB_Se NF038090
IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, ...
 11-112 1.38e-06

IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, are homologous to proteins of iron-sulfur cluster biosynthesis such as IscA, and belong to the broader set of HesB-related proteins.


Pssm-ID: 411672  Cd Length: 99  Bit Score: 43.09  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489348402  11 LEFTHGAAQKVKNLVnEEGNERLKLRVFVTGGGCSGFQYGFTFDEDvAEDDTIVEREGVSLVVDPMSFQYLAGAEVDYQE 90
Cdd:NF038090   2 LEVTDLASRKLKEYF-ADKKIDSPIRVFLNQGGUAGPSLGLALDEP-KENDEVFEQDGLTFVIDKELLEQCGPIKVDFID 79

                         90       100
                 ....*....|....*....|..
gi 489348402  91 GLEGsrFVIKNPNAATTCGCGS 112
Cdd:NF038090  80 CRSG--FSITSSMPLGGGGCGS 99
 
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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