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Conserved domains on  [gi|497571784|ref|WP_009885968|]
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iron-sulfur cluster assembly scaffold protein [Mycoplasmoides genitalium]

Protein Classification

iron-sulfur cluster assembly scaffold protein( domain architecture ID 10160048)

iron-sulfur cluster assembly scaffold protein, similar to Escherichia coli IscU, on which IscS assembles Fe-S clusters

Gene Ontology:  GO:0016226|GO:0051536
PubMed:  15952888|15379587
SCOP:  4001402

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IscU_like cd06664
Iron-sulfur cluster scaffold-like proteins; IscU_like and NifU_like proteins. IscU and NifU ...
 6-134 1.20e-19

Iron-sulfur cluster scaffold-like proteins; IscU_like and NifU_like proteins. IscU and NifU function as a scaffold for the assembly of [2Fe-2S] clusters before they are transferred to apo target proteins. They are highly conserved and play vital roles in the ISC and NIF systems of Fe-S protein maturation. NIF genes participate in nitrogen fixation in several isolated bacterial species. The NifU domain, however, is also found in bacteria that do not fix nitrogen, so it may have wider significance in the cell. Human IscU interacts with frataxin, the Friedreich ataxia gene product, and incorrectly spliced IscU has been shown to disrupt iron homeostasis in skeletal muscle and cause myopathy.


:

Pssm-ID: 143480  Cd Length: 123  Bit Score: 78.45  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784   6 RTKIIDIYSNLKYKKPLKSFQKILTTsDSDNCEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAK 85
Cdd:cd06664    3 SEIILDHYRNPRNVGRLEDADGTGEV-GNPLCGDEITLYLKVEDGRITDAKFQGFGCAISIASASLLTELIKGKTLDEAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 497571784  86 KILSDLIATYKDKnsanqvvEELKLLIEMNVTEKRLQCLLLTPSNLLQW 134
Cdd:cd06664   82 KLLNKDIAMLDGK-------EELAALAGVGLPPARIHCALLAWKALKAA 123
 
Name Accession Description Interval E-value
IscU_like cd06664
Iron-sulfur cluster scaffold-like proteins; IscU_like and NifU_like proteins. IscU and NifU ...
 6-134 1.20e-19

Iron-sulfur cluster scaffold-like proteins; IscU_like and NifU_like proteins. IscU and NifU function as a scaffold for the assembly of [2Fe-2S] clusters before they are transferred to apo target proteins. They are highly conserved and play vital roles in the ISC and NIF systems of Fe-S protein maturation. NIF genes participate in nitrogen fixation in several isolated bacterial species. The NifU domain, however, is also found in bacteria that do not fix nitrogen, so it may have wider significance in the cell. Human IscU interacts with frataxin, the Friedreich ataxia gene product, and incorrectly spliced IscU has been shown to disrupt iron homeostasis in skeletal muscle and cause myopathy.


Pssm-ID: 143480  Cd Length: 123  Bit Score: 78.45  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784   6 RTKIIDIYSNLKYKKPLKSFQKILTTsDSDNCEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAK 85
Cdd:cd06664    3 SEIILDHYRNPRNVGRLEDADGTGEV-GNPLCGDEITLYLKVEDGRITDAKFQGFGCAISIASASLLTELIKGKTLDEAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 497571784  86 KILSDLIATYKDKnsanqvvEELKLLIEMNVTEKRLQCLLLTPSNLLQW 134
Cdd:cd06664   82 KLLNKDIAMLDGK-------EELAALAGVGLPPARIHCALLAWKALKAA 123
IscU COG0822
Fe-S cluster assembly scaffold protein IscU, NifU family [Posttranslational modification, ...
 1-138 6.83e-15

Fe-S cluster assembly scaffold protein IscU, NifU family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440584  Cd Length: 128  Bit Score: 66.01  E-value: 6.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784   1 MDIRARTKIIDIYSNLKYKKPLKSFQkILTTSDSDNCEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKT 80
Cdd:COG0822    2 LDDLYSEKILDHAKNPRNVGELEDAD-GSGEGGNPLCGDTVTLYLKVDDGRIEDAKFEGFGCAISQASASMLTELVKGKT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497571784  81 INQAKKILSDLiatykdknsanqvvEELKLLIEMNVTEKRLQCLLLTPSNLLQWFKNF 138
Cdd:COG0822   81 LEEALALTDEF--------------GDLAALGGLPKFPARVKCALLAWDALKAALADY 124
SUF_scaf_2 TIGR01994
SUF system FeS assembly protein, NifU family; Three iron-sulfur cluster assembly systems are ...
 9-87 1.95e-07

SUF system FeS assembly protein, NifU family; Three iron-sulfur cluster assembly systems are known so far. ISC is broadly distributed while NIF tends to be associated with nitrogenase in nitrogen-fixing bacteria. The most recently described is SUF, believed to be important to maintain the function during aerobic stress of enzymes with labile Fe-S clusters. It is fairly widely distributed. This family represents one of two different proteins proposed to act as a scaffold on which the Fe-S cluster is built and from which it is transferred. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273918  Cd Length: 137  Bit Score: 46.94  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784    9 IIDIYSNLKYKKPLKSFQKILttsDSDN--CEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAKK 86
Cdd:TIGR01994   9 ILDHYKNPRHRGKLEDATVQE---RGHNptCGDEITLTVKLEGDRIEDIAFEGEGCSISQASASMMTELIKGKTVEEALS 85


                  .
gi 497571784   87 I 87
Cdd:TIGR01994  86 L 86
NifU_N pfam01592
NifU-like N terminal domain; This domain is found in NifU in combination with pfam01106. This ...
 8-95 1.59e-04

NifU-like N terminal domain; This domain is found in NifU in combination with pfam01106. This domain is found on isolated in several bacterial species. The nif genes are responsible for nitrogen fixation. However this domain is found in bacteria that do not fix nitrogen, so it may have a broader significance in the cell than nitrogen fixation. These proteins appear to be scaffold proteins for iron-sulfur clusters.


Pssm-ID: 426336  Cd Length: 127  Bit Score: 38.93  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784    8 KIIDIYSNLKYKKPLKSFQKILTTSDSDNCEDF--FNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAK 85
Cdd:pfam01592   5 KVLDHYKNPRNVGVLEDADAGVGDVGNPACGDAmrLQIKVDESTDRIEDAKFKTFGCGSAIASSSMLTELVKGKTIEEAL 84

                          90
                  ....*....|
gi 497571784   86 KILSDLIATY 95
Cdd:pfam01592  85 KITNTDIAEE 94
 
Name Accession Description Interval E-value
IscU_like cd06664
Iron-sulfur cluster scaffold-like proteins; IscU_like and NifU_like proteins. IscU and NifU ...
 6-134 1.20e-19

Iron-sulfur cluster scaffold-like proteins; IscU_like and NifU_like proteins. IscU and NifU function as a scaffold for the assembly of [2Fe-2S] clusters before they are transferred to apo target proteins. They are highly conserved and play vital roles in the ISC and NIF systems of Fe-S protein maturation. NIF genes participate in nitrogen fixation in several isolated bacterial species. The NifU domain, however, is also found in bacteria that do not fix nitrogen, so it may have wider significance in the cell. Human IscU interacts with frataxin, the Friedreich ataxia gene product, and incorrectly spliced IscU has been shown to disrupt iron homeostasis in skeletal muscle and cause myopathy.


Pssm-ID: 143480  Cd Length: 123  Bit Score: 78.45  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784   6 RTKIIDIYSNLKYKKPLKSFQKILTTsDSDNCEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAK 85
Cdd:cd06664    3 SEIILDHYRNPRNVGRLEDADGTGEV-GNPLCGDEITLYLKVEDGRITDAKFQGFGCAISIASASLLTELIKGKTLDEAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 497571784  86 KILSDLIATYKDKnsanqvvEELKLLIEMNVTEKRLQCLLLTPSNLLQW 134
Cdd:cd06664   82 KLLNKDIAMLDGK-------EELAALAGVGLPPARIHCALLAWKALKAA 123
IscU COG0822
Fe-S cluster assembly scaffold protein IscU, NifU family [Posttranslational modification, ...
 1-138 6.83e-15

Fe-S cluster assembly scaffold protein IscU, NifU family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440584  Cd Length: 128  Bit Score: 66.01  E-value: 6.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784   1 MDIRARTKIIDIYSNLKYKKPLKSFQkILTTSDSDNCEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKT 80
Cdd:COG0822    2 LDDLYSEKILDHAKNPRNVGELEDAD-GSGEGGNPLCGDTVTLYLKVDDGRIEDAKFEGFGCAISQASASMLTELVKGKT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497571784  81 INQAKKILSDLiatykdknsanqvvEELKLLIEMNVTEKRLQCLLLTPSNLLQWFKNF 138
Cdd:COG0822   81 LEEALALTDEF--------------GDLAALGGLPKFPARVKCALLAWDALKAALADY 124
SUF_scaf_2 TIGR01994
SUF system FeS assembly protein, NifU family; Three iron-sulfur cluster assembly systems are ...
 9-87 1.95e-07

SUF system FeS assembly protein, NifU family; Three iron-sulfur cluster assembly systems are known so far. ISC is broadly distributed while NIF tends to be associated with nitrogenase in nitrogen-fixing bacteria. The most recently described is SUF, believed to be important to maintain the function during aerobic stress of enzymes with labile Fe-S clusters. It is fairly widely distributed. This family represents one of two different proteins proposed to act as a scaffold on which the Fe-S cluster is built and from which it is transferred. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273918  Cd Length: 137  Bit Score: 46.94  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784    9 IIDIYSNLKYKKPLKSFQKILttsDSDN--CEDFFNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAKK 86
Cdd:TIGR01994   9 ILDHYKNPRHRGKLEDATVQE---RGHNptCGDEITLTVKLEGDRIEDIAFEGEGCSISQASASMMTELIKGKTVEEALS 85


                  .
gi 497571784   87 I 87
Cdd:TIGR01994  86 L 86
NifU_N pfam01592
NifU-like N terminal domain; This domain is found in NifU in combination with pfam01106. This ...
 8-95 1.59e-04

NifU-like N terminal domain; This domain is found in NifU in combination with pfam01106. This domain is found on isolated in several bacterial species. The nif genes are responsible for nitrogen fixation. However this domain is found in bacteria that do not fix nitrogen, so it may have a broader significance in the cell than nitrogen fixation. These proteins appear to be scaffold proteins for iron-sulfur clusters.


Pssm-ID: 426336  Cd Length: 127  Bit Score: 38.93  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571784    8 KIIDIYSNLKYKKPLKSFQKILTTSDSDNCEDF--FNIGLNIDKNKITAIGFDGDGCIISTIATELSIKAIENKTINQAK 85
Cdd:pfam01592   5 KVLDHYKNPRNVGVLEDADAGVGDVGNPACGDAmrLQIKVDESTDRIEDAKFKTFGCGSAIASSSMLTELVKGKTIEEAL 84

                          90
                  ....*....|
gi 497571784   86 KILSDLIATY 95
Cdd:pfam01592  85 KITNTDIAEE 94
 
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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