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Conserved domains on  [gi|568980533|ref|XP_006516359|]
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iron-sulfur cluster assembly 2 homolog, mitochondrial isoform X1 [Mus musculus]

Protein Classification

HesB/IscA family protein( domain architecture ID 10001059)

HesB/IscA family protein is a scaffold protein upon which 2Fe-2S clusters are assembled and subsequently transferred to acceptor proteins; similar to iron-sulfur assembly protein IscA that is involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway

Gene Ontology:  GO:0016226|GO:0051536
PubMed:  32108236

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 43-145 8.04e-44

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


:

Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 139.52  E-value: 8.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITEGSE----FLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQ 118
Cdd:COG0316    2 ITLTDAAAKRIKRLLAKEGnpglGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYVE 81

                         90       100
                 ....*....|....*....|....*..
gi 568980533 119 ELIRSSFQVlNNPQAQQGCSCGSSFSV 145
Cdd:COG0316   82 ELLGSGFKF-NNPNAKSSCGCGESFSV 107
 
Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 43-145 8.04e-44

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


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 139.52  E-value: 8.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITEGSE----FLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQ 118
Cdd:COG0316    2 ITLTDAAAKRIKRLLAKEGnpglGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYVE 81

                         90       100
                 ....*....|....*....|....*..
gi 568980533 119 ELIRSSFQVlNNPQAQQGCSCGSSFSV 145
Cdd:COG0316   82 ELLGSGFKF-NNPNAKSSCGCGESFSV 107
PLN03082 PLN03082
Iron-sulfur cluster assembly; Provisional
 33-146 2.56e-43

Iron-sulfur cluster assembly; Provisional


Pssm-ID: 215564  Cd Length: 163  Bit Score: 140.45  E-value: 2.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  33 SSIPEAGEGQ-IRLTDSCVQRLLEI--TEGS---EFLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSL 106
Cdd:PLN03082  44 SSPSSSASLDaVHMTDNCIRRLKELqtSEPSaedKMLRLSVETGGCSGFQYVFELDDKTNSDDRVFEKDGVKLVVDNISY 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568980533 107 AFVKGAQVDFSQELIRSSFQVLNNPQAQQGCSCGSSFSVK 146
Cdd:PLN03082 124 DFVKGATVDYVEELIRSAFVVSTNPSAVGGCSCKSSFMVK 163
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 45-145 2.36e-41

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: 133.47  E-value: 2.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533   45 LTDSCVQRLLEITEGSE----FLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQEL 120
Cdd:TIGR00049   2 LTDSAAKRIKALLAGEGepnlGLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVEEL 81

                          90       100
                  ....*....|....*....|....*
gi 568980533  121 IRSSFQVLnNPQAQQGCSCGSSFSV 145
Cdd:TIGR00049  82 LGSGFTFT-NPNAKGTCGCGKSFSV 105
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
 42-140 8.23e-12

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: 58.04  E-value: 8.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533   42 QIRLTDSCVQRLLE-ITEGSEFLRLQVEGGG-------CSGfQYKFSL---DTVINPDDRVFEQGGARVVVDSDSLAFV- 109
Cdd:pfam01521   2 KITITDAAAERLKKlLAGDKKELRLDVDDGGgpyskggCSI-GGKFSLvlvDEPDPDYDEVIESNGGPIYVDSYSLPFLd 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568980533  110 KGAQVDFSQELIRSSFQVlNNPQAQQGCSCG 140
Cdd:pfam01521  81 EGLTLDFVEDLGTLGLKS-DNGNLDGNVGCG 110
IscA_HesB_Se NF038090
IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, ...
 43-139 4.27e-04

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: 37.31  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITEGSEF---LRLQVEGGGCSGFQYKFSLDTViNPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQE 119
Cdd:NF038090   2 LEVTDLASRKLKEYFADKKIdspIRVFLNQGGUAGPSLGLALDEP-KENDEVFEQDGLTFVIDKELLEQCGPIKVDFIDC 80

                         90       100
                 ....*....|....*....|.
gi 568980533 120 liRSSFQVL-NNPQAQQGCSC 139
Cdd:NF038090  81 --RSGFSITsSMPLGGGGCGS 99
 
Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 43-145 8.04e-44

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


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 139.52  E-value: 8.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITEGSE----FLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQ 118
Cdd:COG0316    2 ITLTDAAAKRIKRLLAKEGnpglGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYVE 81

                         90       100
                 ....*....|....*....|....*..
gi 568980533 119 ELIRSSFQVlNNPQAQQGCSCGSSFSV 145
Cdd:COG0316   82 ELLGSGFKF-NNPNAKSSCGCGESFSV 107
PLN03082 PLN03082
Iron-sulfur cluster assembly; Provisional
 33-146 2.56e-43

Iron-sulfur cluster assembly; Provisional


Pssm-ID: 215564  Cd Length: 163  Bit Score: 140.45  E-value: 2.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  33 SSIPEAGEGQ-IRLTDSCVQRLLEI--TEGS---EFLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSL 106
Cdd:PLN03082  44 SSPSSSASLDaVHMTDNCIRRLKELqtSEPSaedKMLRLSVETGGCSGFQYVFELDDKTNSDDRVFEKDGVKLVVDNISY 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568980533 107 AFVKGAQVDFSQELIRSSFQVLNNPQAQQGCSCGSSFSVK 146
Cdd:PLN03082 124 DFVKGATVDYVEELIRSAFVVSTNPSAVGGCSCKSSFMVK 163
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 45-145 2.36e-41

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: 133.47  E-value: 2.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533   45 LTDSCVQRLLEITEGSE----FLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQEL 120
Cdd:TIGR00049   2 LTDSAAKRIKALLAGEGepnlGLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVEEL 81

                          90       100
                  ....*....|....*....|....*
gi 568980533  121 IRSSFQVLnNPQAQQGCSCGSSFSV 145
Cdd:TIGR00049  82 LGSGFTFT-NPNAKGTCGCGKSFSV 105
PRK13623 PRK13623
iron-sulfur cluster insertion protein ErpA; Provisional
 43-145 3.02e-31

iron-sulfur cluster insertion protein ErpA; Provisional


Pssm-ID: 184186  Cd Length: 115  Bit Score: 108.09  E-value: 3.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSC---VQRLLEITEGSEF-LRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQ 118
Cdd:PRK13623  10 LVFTDAAaakVKELIEEEGNPDLkLRVYITGGGCSGFQYGFTFDEQVNEDDTTIEKQGVTLVVDPMSLQYLVGAEVDYTE 89

                         90       100
                 ....*....|....*....|....*..
gi 568980533 119 ELIRSSFqVLNNPQAQQGCSCGSSFSV 145
Cdd:PRK13623  90 GLEGSRF-VIKNPNAKTTCGCGSSFSI 115
sufA_proteo TIGR01997
FeS assembly scaffold SufA; This model represents the SufA protein of the SUF system of ...
 43-145 3.74e-23

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: 87.19  E-value: 3.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533   43 IRLTDSC---VQRLLEITEGSEFLRLQVEGGGCSGFQYkfSLDTVINP--DDRVFEQGGARVVVDSDSLAFVKGAQVDFS 117
Cdd:TIGR01997   3 ITLTDAAaihIRELVAKRPEAVGIRLGVKKTGCAGMEY--VLDLVSEPkkDDDLIEHDGAKVFVAPEAVLFILGTQVDFV 80

                          90       100
                  ....*....|....*....|....*...
gi 568980533  118 QELIRSSFqVLNNPQAQQGCSCGSSFSV 145
Cdd:TIGR01997  81 RTTLRQGF-KFNNPNATSACGCGESFEL 107
sufA PRK09504
iron-sulfur cluster assembly scaffold protein; Provisional
 43-145 1.64e-21

iron-sulfur cluster assembly scaffold protein; Provisional


Pssm-ID: 181915  Cd Length: 122  Bit Score: 83.63  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITE---GSEFLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQE 119
Cdd:PRK09504  18 LTLTPAAAAHIRELMAkqpGMKGVRLGVKQTGCAGFGYVLDSVSEPDKDDLVFEHDGAKLFVPLQAMPFIDGTEVDYVRE 97

                         90       100
                 ....*....|....*....|....*.
gi 568980533 120 LIRSSFQvLNNPQAQQGCSCGSSFSV 145
Cdd:PRK09504  98 GLNQIFK-FHNPKAQNECGCGESFGV 122
IscA TIGR02011
iron-sulfur cluster assembly protein IscA; This model represents the IscA component of the ISC ...
 43-145 1.20e-19

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: 78.33  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533   43 IRLTDSCVQRLLEI--TEGSEF-LRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQE 119
Cdd:TIGR02011   1 ITLTDSAAARVNTFlaNRGKGFgLRLGVKTSGCSGMAYVLEFVDEPTPDDIVFEDKGVKIVIDGKSLQYLDGTQLDFVKE 80

                          90       100
                  ....*....|....*....|....*.
gi 568980533  120 LIRSSFQvLNNPQAQQGCSCGSSFSV 145
Cdd:TIGR02011  81 GLNEGFK-FTNPNVKDECGCGESFHV 105
iscA PRK09502
iron-sulfur cluster assembly protein IscA;
43-145 2.21e-19

iron-sulfur cluster assembly protein IscA;


Pssm-ID: 181914 [Multi-domain]  Cd Length: 107  Bit Score: 77.60  E-value: 2.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITE--GSEF-LRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQE 119
Cdd:PRK09502   3 ITLSDSAAARVNTFLAnrGKGFgLRLGVRTSGCSGMAYVLEFVDEPTPEDIVFEDKGVKVVVDGKSLQFLDGTQLDFVKE 82

                         90       100
                 ....*....|....*....|....*.
gi 568980533 120 LIRSSFQvLNNPQAQQGCSCGSSFSV 145
Cdd:PRK09502  83 GLNEGFK-FTNPNVKDECGCGESFHV 107
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
 42-140 8.23e-12

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: 58.04  E-value: 8.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533   42 QIRLTDSCVQRLLE-ITEGSEFLRLQVEGGG-------CSGfQYKFSL---DTVINPDDRVFEQGGARVVVDSDSLAFV- 109
Cdd:pfam01521   2 KITITDAAAERLKKlLAGDKKELRLDVDDGGgpyskggCSI-GGKFSLvlvDEPDPDYDEVIESNGGPIYVDSYSLPFLd 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568980533  110 KGAQVDFSQELIRSSFQVlNNPQAQQGCSCG 140
Cdd:pfam01521  81 EGLTLDFVEDLGTLGLKS-DNGNLDGNVGCG 110
IscA_HesB_Se NF038090
IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, ...
 43-139 4.27e-04

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: 37.31  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  43 IRLTDSCVQRLLEITEGSEF---LRLQVEGGGCSGFQYKFSLDTViNPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQE 119
Cdd:NF038090   2 LEVTDLASRKLKEYFADKKIdspIRVFLNQGGUAGPSLGLALDEP-KENDEVFEQDGLTFVIDKELLEQCGPIKVDFIDC 80

                         90       100
                 ....*....|....*....|.
gi 568980533 120 liRSSFQVL-NNPQAQQGCSC 139
Cdd:NF038090  81 --RSGFSITsSMPLGGGGCGS 99
YneR COG4841
Uncharacterized conserved protein YneR, related to HesB/YadR/YfhF family [Function unknown];
42-120 7.02e-04

Uncharacterized conserved protein YneR, related to HesB/YadR/YfhF family [Function unknown];


Pssm-ID: 443869  Cd Length: 95  Bit Score: 36.74  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980533  42 QIRLTDSCVQ---RLLEITEGsEFLRLQVEGGGCSGFQYKFSLD-TVINPDDR--VFEQGGARVVVDSDSLAFVKGA--Q 113
Cdd:COG4841    2 KITITDQALKwfkEELDLESG-DGIRFFVRYGGSSPVQEGFSLGvTVEEPDEPavETEVDGITFFVEEDDLWFFDGHdlT 80


                 ....*..
gi 568980533 114 VDFSQEL 120
Cdd:COG4841   81 VDYDEKT 87
 
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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