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Conserved domains on  [gi|16131290|ref|NP_417873|]
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iron-sulfur cluster carrier protein NfuA [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

Fe/S biogenesis protein NfuA( domain architecture ID 11485261)

Fe/S biogenesis protein NfuA is an iron-sulphur carrier protein that may be involved in the maturation and/or repair of Fe/S proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11190 PRK11190
iron-sulfur cluster biogenesis protein NfuA;
1-191 2.15e-165

iron-sulfur cluster biogenesis protein NfuA;


:

Pssm-ID: 183027 [Multi-domain]  Cd Length: 192  Bit Score: 452.16  E-value: 2.15e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    1 MIRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDF 80
Cdd:PRK11190   1 MITISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTELKFDGFSAYVDELSAPFLEDAEIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290   81 VTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLK 160
Cdd:PRK11190  81 VTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYVLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLK 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 16131290  161 EGIEKQLLNEFP-ELKGVRDLTEHQRGEHSYY 191
Cdd:PRK11190 161 EGIEKQLLNEFPgELKGVRDLTEHQRGEHSYY 192
 
Name Accession Description Interval E-value
PRK11190 PRK11190
iron-sulfur cluster biogenesis protein NfuA;
1-191 2.15e-165

iron-sulfur cluster biogenesis protein NfuA;


Pssm-ID: 183027 [Multi-domain]  Cd Length: 192  Bit Score: 452.16  E-value: 2.15e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    1 MIRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDF 80
Cdd:PRK11190   1 MITISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTELKFDGFSAYVDELSAPFLEDAEIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290   81 VTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLK 160
Cdd:PRK11190  81 VTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYVLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLK 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 16131290  161 EGIEKQLLNEFP-ELKGVRDLTEHQRGEHSYY 191
Cdd:PRK11190 161 EGIEKQLLNEFPgELKGVRDLTEHQRGEHSYY 192
YhgI_GntY TIGR03341
IscR-regulated protein YhgI; IscR (TIGR02010) is an iron-sulfur cluster-binding ...
2-191 2.73e-142

IscR-regulated protein YhgI; IscR (TIGR02010) is an iron-sulfur cluster-binding transcriptional regulator (see Genome Property GenProp0138). Members of this protein family include YhgI, whose expression is under control of IscR, and show sequence similarity to IscA, a known protein of iron-sulfur cluster biosynthesis. These two lines of evidence strongly suggest a role as an iron-sulfur cluster biosynthesis protein. An older study designated this protein GntY and suggested a role for it and for the product of an adjacent gene, based on complementation studies, in gluconate utilization. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132384 [Multi-domain]  Cd Length: 190  Bit Score: 393.61  E-value: 2.73e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290     2 IRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFV 81
Cdd:TIGR03341   1 ITITEAAQAYLAKLLAKQNEGTGIRVFVVNPGTPYAECCVSYCPPDEVEPSDIKLEFNGFSAYVDALSAPFLEDAVIDFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    82 TDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLKE 161
Cdd:TIGR03341  81 TDRMGGQLTLKAPNAKMPKVADDAPLEERINYVLQSEINPQLASHGGKVTLVEITDDGVAVLQFGGGCNGCSMVDVTLKD 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 16131290   162 GIEKQLLNEFPELKGVRDLTEHQRGEHSYY 191
Cdd:TIGR03341 161 GVEKTLLERFPELKGVRDATDHTRGEHSYY 190
NifU COG0694
Fe-S cluster biogenesis protein NfuA, 4Fe-4S-binding domain [Posttranslational modification, ...
8-179 4.06e-50

Fe-S cluster biogenesis protein NfuA, 4Fe-4S-binding domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440458 [Multi-domain]  Cd Length: 176  Bit Score: 159.82  E-value: 4.06e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290   8 AQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFVTDQLGS 87
Cdd:COG0694   1 AQAAALKLLPEEPGGELIRGEVAAPGAPAAAALLLAEAPEVEEDDDVVVVAAVFVAVTDELSGPLLELAIIDAILAAAGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290  88 QLTLKAPNAKMRKVA-----DDAPLMERVEYMLQSQINPQLAGHGGRVSLMEItEDGYAILQFGGGCNGCSMVDVTLKEG 162
Cdd:COG0694  81 QLTLAAPDAAVAEVLsfhalTDAELEERIEEVLDEEIRPALASDGGDIELVDV-EDGVVYVRLGGACSGCPSSTMTLKNG 159
                       170
                ....*....|....*..
gi 16131290 163 IEKQLLNEFPELKGVRD 179
Cdd:COG0694 160 IERALKERVPEVKEVEA 176
NifU pfam01106
NifU-like domain; This is an alignment of the carboxy-terminal domain. This is the only common ...
111-177 8.44e-21

NifU-like domain; This is an alignment of the carboxy-terminal domain. This is the only common region between the NifU protein from nitrogen-fixing bacteria and rhodobacterial species. The biochemical function of NifU is unknown.


Pssm-ID: 460066 [Multi-domain]  Cd Length: 67  Bit Score: 81.33  E-value: 8.44e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131290   111 VEYMLQSQINPQLAGHGGRVSLMEItEDGYAILQFGGGCNGCSMVDVTLKEGIEKQLLNEFPELKGV 177
Cdd:pfam01106   1 IEEVLEEEIRPALQADGGDIELVDV-DDGVVYVRLQGACSGCPSSTMTLKNGIEQALKEKVPEVKRV 66
 
Name Accession Description Interval E-value
PRK11190 PRK11190
iron-sulfur cluster biogenesis protein NfuA;
1-191 2.15e-165

iron-sulfur cluster biogenesis protein NfuA;


Pssm-ID: 183027 [Multi-domain]  Cd Length: 192  Bit Score: 452.16  E-value: 2.15e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    1 MIRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDF 80
Cdd:PRK11190   1 MITISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTELKFDGFSAYVDELSAPFLEDAEIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290   81 VTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLK 160
Cdd:PRK11190  81 VTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYVLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLK 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 16131290  161 EGIEKQLLNEFP-ELKGVRDLTEHQRGEHSYY 191
Cdd:PRK11190 161 EGIEKQLLNEFPgELKGVRDLTEHQRGEHSYY 192
YhgI_GntY TIGR03341
IscR-regulated protein YhgI; IscR (TIGR02010) is an iron-sulfur cluster-binding ...
2-191 2.73e-142

IscR-regulated protein YhgI; IscR (TIGR02010) is an iron-sulfur cluster-binding transcriptional regulator (see Genome Property GenProp0138). Members of this protein family include YhgI, whose expression is under control of IscR, and show sequence similarity to IscA, a known protein of iron-sulfur cluster biosynthesis. These two lines of evidence strongly suggest a role as an iron-sulfur cluster biosynthesis protein. An older study designated this protein GntY and suggested a role for it and for the product of an adjacent gene, based on complementation studies, in gluconate utilization. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132384 [Multi-domain]  Cd Length: 190  Bit Score: 393.61  E-value: 2.73e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290     2 IRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFV 81
Cdd:TIGR03341   1 ITITEAAQAYLAKLLAKQNEGTGIRVFVVNPGTPYAECCVSYCPPDEVEPSDIKLEFNGFSAYVDALSAPFLEDAVIDFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    82 TDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLKE 161
Cdd:TIGR03341  81 TDRMGGQLTLKAPNAKMPKVADDAPLEERINYVLQSEINPQLASHGGKVTLVEITDDGVAVLQFGGGCNGCSMVDVTLKD 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 16131290   162 GIEKQLLNEFPELKGVRDLTEHQRGEHSYY 191
Cdd:TIGR03341 161 GVEKTLLERFPELKGVRDATDHTRGEHSYY 190
NifU COG0694
Fe-S cluster biogenesis protein NfuA, 4Fe-4S-binding domain [Posttranslational modification, ...
8-179 4.06e-50

Fe-S cluster biogenesis protein NfuA, 4Fe-4S-binding domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440458 [Multi-domain]  Cd Length: 176  Bit Score: 159.82  E-value: 4.06e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290   8 AQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFVTDQLGS 87
Cdd:COG0694   1 AQAAALKLLPEEPGGELIRGEVAAPGAPAAAALLLAEAPEVEEDDDVVVVAAVFVAVTDELSGPLLELAIIDAILAAAGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290  88 QLTLKAPNAKMRKVA-----DDAPLMERVEYMLQSQINPQLAGHGGRVSLMEItEDGYAILQFGGGCNGCSMVDVTLKEG 162
Cdd:COG0694  81 QLTLAAPDAAVAEVLsfhalTDAELEERIEEVLDEEIRPALASDGGDIELVDV-EDGVVYVRLGGACSGCPSSTMTLKNG 159
                       170
                ....*....|....*..
gi 16131290 163 IEKQLLNEFPELKGVRD 179
Cdd:COG0694 160 IERALKERVPEVKEVEA 176
NifU pfam01106
NifU-like domain; This is an alignment of the carboxy-terminal domain. This is the only common ...
111-177 8.44e-21

NifU-like domain; This is an alignment of the carboxy-terminal domain. This is the only common region between the NifU protein from nitrogen-fixing bacteria and rhodobacterial species. The biochemical function of NifU is unknown.


Pssm-ID: 460066 [Multi-domain]  Cd Length: 67  Bit Score: 81.33  E-value: 8.44e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131290   111 VEYMLQSQINPQLAGHGGRVSLMEItEDGYAILQFGGGCNGCSMVDVTLKEGIEKQLLNEFPELKGV 177
Cdd:pfam01106   1 IEEVLEEEIRPALQADGGDIELVDV-DDGVVYVRLQGACSGCPSSTMTLKNGIEQALKEKVPEVKRV 66
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
1-97 4.24e-16

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


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 70.18  E-value: 4.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290   1 MIRISDAAQAHFAKLLANQE-EGTQIRVFVINPGtpnaeC-GVSYcp--pDAVEATDTALKFDLLTAYVDELSAPYLEDA 76
Cdd:COG0316   1 PITLTDAAAKRIKRLLAKEGnPGLGLRVGVKGGG-----CsGFSYgldfdDEPNEDDLVFEQDGVKVVVDPKSLPYLDGT 75
                        90       100
                ....*....|....*....|.
gi 16131290  77 EIDFVTDQLGSQLTLKAPNAK 97
Cdd:COG0316  76 EIDYVEELLGSGFKFNNPNAK 96
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
2-99 5.90e-15

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: 67.67  E-value: 5.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290     2 IRISDAAQAHFAKLLANQEEgtQIRVFVINPGTPNAE--C--GVSYCP---PDAVEATDTALKFDLLTAYVDELSAPYLE 74
Cdd:pfam01521   3 ITITDAAAERLKKLLAGDKK--ELRLDVDDGGGPYSKggCsiGGKFSLvlvDEPDPDYDEVIESNGGPIYVDSYSLPFLD 80
                          90       100
                  ....*....|....*....|....*.
gi 16131290    75 D-AEIDFVTDQLGSQLTLKAPNAKMR 99
Cdd:pfam01521  81 EgLTLDFVEDLGTLGLKSDNGNLDGN 106
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
4-97 2.75e-11

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: 57.59  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290     4 ISDAAQAHFAKLLANQ-EEGTQIRVFVINPGtpnaeC-GVSYcppdAVEATDTALKFDLL------TAYVDELSAPYLED 75
Cdd:TIGR00049   2 LTDSAAKRIKALLAGEgEPNLGLRVGVKGGG-----CsGLQY----GLEFDDEPNEDDEVfeqdgvKVVVDPKSLPYLDG 72
                          90       100
                  ....*....|....*....|..
gi 16131290    76 AEIDFVTDQLGSQLTLKAPNAK 97
Cdd:TIGR00049  73 SEIDYVEELLGSGFTFTNPNAK 94
sufA_proteo TIGR01997
FeS assembly scaffold SufA; This model represents the SufA protein of the SUF system of ...
2-96 7.13e-07

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: 45.98  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290     2 IRISDAAQAHFAKLLANQEEGTQIRVFVINPGtpnaeC-GVSYCPpDAVE---ATDTALKFDLLTAYVDELSAPYLEDAE 77
Cdd:TIGR01997   3 ITLTDAAAIHIRELVAKRPEAVGIRLGVKKTG-----CaGMEYVL-DLVSepkKDDDLIEHDGAKVFVAPEAVLFILGTQ 76
                          90
                  ....*....|....*....
gi 16131290    78 IDFVTDQLGSQLTLKAPNA 96
Cdd:TIGR01997  77 VDFVRTTLRQGFKFNNPNA 95
PRK13623 PRK13623
iron-sulfur cluster insertion protein ErpA; Provisional
2-97 2.13e-06

iron-sulfur cluster insertion protein ErpA; Provisional


Pssm-ID: 184186  Cd Length: 115  Bit Score: 44.92  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    2 IRISDAAQAHFAKLLAnqEEGTQ---IRVFVINPGtpnaeC-GVSY--CPPDAVEATDTALKFDLLTAYVDELSAPYLED 75
Cdd:PRK13623  10 LVFTDAAAAKVKELIE--EEGNPdlkLRVYITGGG-----CsGFQYgfTFDEQVNEDDTTIEKQGVTLVVDPMSLQYLVG 82
                         90       100
                 ....*....|....*....|..
gi 16131290   76 AEIDFVTDQLGSQLTLKAPNAK 97
Cdd:PRK13623  83 AEVDYTEGLEGSRFVIKNPNAK 104
iscA PRK09502
iron-sulfur cluster assembly protein IscA;
2-97 2.20e-03

iron-sulfur cluster assembly protein IscA;


Pssm-ID: 181914 [Multi-domain]  Cd Length: 107  Bit Score: 36.39  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131290    2 IRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPnaecGVSYCPP--DAVEATDTALKFDLLTAYVDELSAPYLEDAEID 79
Cdd:PRK09502   3 ITLSDSAAARVNTFLANRGKGFGLRLGVRTSGCS----GMAYVLEfvDEPTPEDIVFEDKGVKVVVDGKSLQFLDGTQLD 78
                         90
                 ....*....|....*...
gi 16131290   80 FVTDQLGSQLTLKAPNAK 97
Cdd:PRK09502  79 FVKEGLNEGFKFTNPNVK 96
 
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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