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Conserved domains on  [gi|303306328|gb|ADM13684|]
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NifH, partial [Burkholderia sp. enrichment culture clone CACua-01]

Protein Classification

nitrogenase iron protein; nitrogenase iron protein; nitrogenase iron protein; nitrogenase iron protein NifH( domain architecture ID 10787575)

nitrogenase iron protein NifH is the component II (iron protein) of nitrogenase that catalyzes the ATP-dependent reduction of dinitrogen to ammonia, which is central to the process of biological nitrogen fixation; nitrogenase iron protein NifH is the component II of nitogenase, which is responsible for the biological nitrogen fixation (reduction of molecular nitrogen to ammonia) in an ATP-dependent process; nitrogenase iron protein NifH is the component II of nitogenase, which is responsible for the biological nitrogen fixation (reduction of molecular nitrogen to ammonia) in an ATP-dependent process; nitrogenase iron protein NifH is the component II of nitogenase, which is responsible for the biological nitrogen fixation (reduction of molecular nitrogen to ammonia) in an ATP-dependent process

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 1-267 0e+00

Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


:

Pssm-ID: 440959  Cd Length: 276  Bit Score: 500.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsvEDLELEDVMKIGYKDIRCVE 80
Cdd:COG1348    8 YGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGFGGVKCVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYD-GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:COG1348   86 AGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAANNICKG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:COG1348  166 IKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYRELAKKI 245

                        250       260
                 ....*....|....*....|....*...
gi 303306328 240 HNNaGNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:COG1348  246 LEN-KKLVIPKPLSDEELEELLLEYGIL 272
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 1-267 0e+00

Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440959  Cd Length: 276  Bit Score: 500.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsvEDLELEDVMKIGYKDIRCVE 80
Cdd:COG1348    8 YGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGFGGVKCVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYD-GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:COG1348   86 AGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAANNICKG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:COG1348  166 IKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYRELAKKI 245

                        250       260
                 ....*....|....*....|....*...
gi 303306328 240 HNNaGNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:COG1348  246 LEN-KKLVIPKPLSDEELEELLLEYGIL 272
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 1-271 2.67e-178

nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also called nitrogenase reductase or nitrogenase component II. This model includes molybdenum-iron nitrogenase reductase (nifH), vanadium-iron nitrogenase reductase (vnfH), and iron-iron nitrogenase reductase (anfH). The model excludes the homologous protein from the light-independent protochlorophyllide reductase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 273538  Cd Length: 275  Bit Score: 492.29  E-value: 2.67e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328    1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSvEDLELEDVMKIGYKDIRCVE 80
Cdd:TIGR01287   6 YGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGGIRCVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   81 SGGPEPGVGCAGRGVITSINFLEENGAY-DGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:TIGR01287  85 SGGPEPGVGCAGRGVITAINLLEELGAYeDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAANNICKG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:TIGR01287 165 ILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRELAKKI 244

                         250       260       270
                  ....*....|....*....|....*....|..
gi 303306328  240 HNNaGNGTIPTPITMDQLEDLLMEHGIMKSID 271
Cdd:TIGR01287 245 YEN-TEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 1-262 5.43e-165

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 458.13  E-value: 5.43e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsvEDLELEDVMKIGYKDIRCVE 80
Cdd:cd02040    6 YGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNGIKCVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYD-GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:cd02040   84 SGGPEPGVGCAGRGIITAINLLEELGAYEeDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAANNIAKG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:cd02040  164 IVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRELAKKI 243

                        250       260
                 ....*....|....*....|...
gi 303306328 240 HNNAgNGTIPTPITMDQLEDLLM 262
Cdd:cd02040  244 LENK-KLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
1-267 2.44e-156

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 436.49  E-value: 2.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328    1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSVEDLELEDVMKIGYKDIRCVE 80
Cdd:pfam00142   6 YGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGGVKCVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   81 SGGPEPGVGCAGRGVITSINFLEENGAYDGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKGI 160
Cdd:pfam00142  86 SGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAANNIAKGI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  161 LKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKVH 240
Cdd:pfam00142 166 QKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRELARKIL 245

                         250       260
                  ....*....|....*....|....*..
gi 303306328  241 NNAgNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:pfam00142 246 ENP-KGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
1-267 2.96e-138

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 390.72  E-value: 2.96e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTEL-GQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSvEDLELEDVMKIGYKDIRCV 79
Cdd:PRK13233   8 YGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKTGFKDIRCV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  80 ESGGPEPGVGCAGRGVITSINFLEENGAY-DGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISK 158
Cdd:PRK13233  87 ESGGPEPGVGCAGRGVITAIDLMEENGAYtDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAANNICK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 159 GILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKK 238
Cdd:PRK13233 167 GLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYKELARK 246

                        250       260
                 ....*....|....*....|....*....
gi 303306328 239 VHNNAgNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:PRK13233 247 IIENK-DFVIPKPLTMDELEEMVVKYGLM 274
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 1-260 1.68e-126

Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, very closely related to the nitrogenase iron protein, was identified as a subunit involved in biosynthesis of coenzyme F430 in archaeal methanogens and archaeal anaerobic methanotrophs.


Pssm-ID: 380202  Cd Length: 260  Bit Score: 360.35  E-value: 1.68e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsveDLELEDVMKIGYKDIRCVE 80
Cdd:NF033200   6 YGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGGVRCVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYDG-VDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:NF033200  83 SGGPEPGVGCAGRGIIVAMQLLEKLGAFMEdLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNICKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANsggvRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:NF033200 163 IKKLKG----RLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKI 238

                        250       260
                 ....*....|....*....|.
gi 303306328 240 HNNaGNGTIPTPITMDQLEDL 260
Cdd:NF033200 239 MEN-TDFVIPEPLEDEELEEL 258
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 1-267 0e+00

Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440959  Cd Length: 276  Bit Score: 500.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsvEDLELEDVMKIGYKDIRCVE 80
Cdd:COG1348    8 YGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGFGGVKCVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYD-GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:COG1348   86 AGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAANNICKG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:COG1348  166 IKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYRELAKKI 245

                        250       260
                 ....*....|....*....|....*...
gi 303306328 240 HNNaGNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:COG1348  246 LEN-KKLVIPKPLSDEELEELLLEYGIL 272
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 1-271 2.67e-178

nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also called nitrogenase reductase or nitrogenase component II. This model includes molybdenum-iron nitrogenase reductase (nifH), vanadium-iron nitrogenase reductase (vnfH), and iron-iron nitrogenase reductase (anfH). The model excludes the homologous protein from the light-independent protochlorophyllide reductase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 273538  Cd Length: 275  Bit Score: 492.29  E-value: 2.67e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328    1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSvEDLELEDVMKIGYKDIRCVE 80
Cdd:TIGR01287   6 YGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGGIRCVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   81 SGGPEPGVGCAGRGVITSINFLEENGAY-DGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:TIGR01287  85 SGGPEPGVGCAGRGVITAINLLEELGAYeDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAANNICKG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:TIGR01287 165 ILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRELAKKI 244

                         250       260       270
                  ....*....|....*....|....*....|..
gi 303306328  240 HNNaGNGTIPTPITMDQLEDLLMEHGIMKSID 271
Cdd:TIGR01287 245 YEN-TEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 1-262 5.43e-165

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 458.13  E-value: 5.43e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsvEDLELEDVMKIGYKDIRCVE 80
Cdd:cd02040    6 YGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNGIKCVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYD-GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:cd02040   84 SGGPEPGVGCAGRGIITAINLLEELGAYEeDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAANNIAKG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:cd02040  164 IVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRELAKKI 243

                        250       260
                 ....*....|....*....|...
gi 303306328 240 HNNAgNGTIPTPITMDQLEDLLM 262
Cdd:cd02040  244 LENK-KLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
1-267 2.44e-156

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 436.49  E-value: 2.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328    1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSVEDLELEDVMKIGYKDIRCVE 80
Cdd:pfam00142   6 YGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGGVKCVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   81 SGGPEPGVGCAGRGVITSINFLEENGAYDGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKGI 160
Cdd:pfam00142  86 SGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAANNIAKGI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  161 LKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKVH 240
Cdd:pfam00142 166 QKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRELARKIL 245

                         250       260
                  ....*....|....*....|....*..
gi 303306328  241 NNAgNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:pfam00142 246 ENP-KGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
1-267 2.96e-138

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 390.72  E-value: 2.96e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTEL-GQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSvEDLELEDVMKIGYKDIRCV 79
Cdd:PRK13233   8 YGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKTGFKDIRCV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  80 ESGGPEPGVGCAGRGVITSINFLEENGAY-DGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISK 158
Cdd:PRK13233  87 ESGGPEPGVGCAGRGVITAIDLMEENGAYtDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAANNICK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 159 GILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKK 238
Cdd:PRK13233 167 GLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYKELARK 246

                        250       260
                 ....*....|....*....|....*....
gi 303306328 239 VHNNAgNGTIPTPITMDQLEDLLMEHGIM 267
Cdd:PRK13233 247 IIENK-DFVIPKPLTMDELEEMVVKYGLM 274
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 1-260 1.68e-126

Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, very closely related to the nitrogenase iron protein, was identified as a subunit involved in biosynthesis of coenzyme F430 in archaeal methanogens and archaeal anaerobic methanotrophs.


Pssm-ID: 380202  Cd Length: 260  Bit Score: 360.35  E-value: 1.68e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGsveDLELEDVMKIGYKDIRCVE 80
Cdd:NF033200   6 YGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGGVRCVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYDG-VDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:NF033200  83 SGGPEPGVGCAGRGIIVAMQLLEKLGAFMEdLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNICKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANsggvRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:NF033200 163 IKKLKG----RLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKI 238

                        250       260
                 ....*....|....*....|.
gi 303306328 240 HNNaGNGTIPTPITMDQLEDL 260
Cdd:NF033200 239 MEN-TDFVIPEPLEDEELEEL 258
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 1-262 6.21e-113

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 326.24  E-value: 6.21e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSVEDLELEDVMKIGYKDIRCVE 80
Cdd:cd02117    6 YGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDLLFSGFNGVDCVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAY-DGVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:cd02117   86 AGGPEPGVGCGGRGIGTMLELLEEHGLLdDDYDVVIFDVLGDVVCGGFAAPLRRGFAQKVVIVVSEELMSLYAANNIVKA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANsGGVRLGGLVCNERQTDkELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:cd02117  166 VENYSK-NGVRLAGLVANLRDPA-GTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKI 243

                        250       260
                 ....*....|....*....|...
gi 303306328 240 HNNAGNGTIPTPITMDQLEDLLM 262
Cdd:cd02117  244 ADAVPPVPGPRPLSDRELFALLG 266
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 1-272 2.12e-99

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 292.45  E-value: 2.12e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAqDTILSLAAEAGsVEDLELEDVMKIGYKDIRCVE 80
Cdd:PRK13230   7 YGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKI-PTVLDVLREKG-IDNLGLEDIIYEGFNGIYCVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYD--GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISK 158
Cdd:PRK13230  85 SGGPEPGYGCAGRGVITAIDLLKKLGVFEelGPDVVIYDILGDVVCGGFAMPLQKGLADDVYIVTTCDPMAIYAANNICK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 159 GILKYANSGGVRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKK 238
Cdd:PRK13230 165 GIKRFAKRGKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPDSEISNIFRELAEA 244

                        250       260       270
                 ....*....|....*....|....*....|....
gi 303306328 239 VHNNaGNGTIPTPITMDQLEDllmehgIMKSIDE 272
Cdd:PRK13230 245 IYEN-NTGTIPNPLEEEEIDQ------IGEKIKE 271
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 1-259 6.72e-87

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 260.12  E-value: 6.72e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTElGQKILIVGCDPKADSTRlILHAKAQDTILSLAAEAgsvEDLELEDVMKIGYKDIRCVE 80
Cdd:PRK13231   8 YGKGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTR-TLCGKRIPTVLDTLKDN---RKPELEDIIHEGFNGILCVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYDG-VDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:PRK13231  83 SGGPEPGVGCAGRGVIVAMNLLENLGVFDEdIDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAANNIARG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANsggvRLGGLVCNERQTDKELELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKKV 239
Cdd:PRK13231 163 IKKLKG----KLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYRKLANNI 238

                        250       260
                 ....*....|....*....|
gi 303306328 240 HNNAgNGTIPTPITMDQLED 259
Cdd:PRK13231 239 MNNT-EFSTPEPMDDEEFEE 257
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-261 2.52e-56

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 182.11  E-value: 2.52e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSVEDLELEDVMKIGYKDIRCVE 80
Cdd:cd02032    6 YGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGGVDCVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYDGVDYVSYDVLGDVVCGGFAMPIreNKAQEIYIVMSGEMMAMYAANNISKGI 160
Cdd:cd02032   86 AGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPL--NYADYCLIVTANDFDSLFAANRIAAAV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 161 LKYANSGGVRLGGLVCNerQTDKeLELAEALAGMLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANV----YRQLA 236
Cdd:cd02032  164 REKAKTYPVRLAGIIGN--RTDK-TDLIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPELNYvcdeYLNIA 240

                        250       260
                 ....*....|....*....|....*
gi 303306328 237 KKVHNNAgNGTIPTPITMDQLEDLL 261
Cdd:cd02032  241 DQLLSDP-EGVVPKPLPDREIFDLL 264
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-261 1.12e-54

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 177.85  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTrLILHAKAQDTILSLAAEAG-SVEDLELEDVMKIGYKDIRCV 79
Cdd:PRK13185   8 YGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST-FTLTGKLVPTVIDILEEVDfHSEELRPEDFVYEGYNGVDCV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  80 ESGGPEPGVGCAGRGVITSINFLEENGAYDGVDYVSYDVLGDVVCGGFAMPIreNKAQEIYIVMSGEMMAMYAANNISKG 159
Cdd:PRK13185  87 EAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPL--QYADYALIVTANDFDSIFAANRIAAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 160 ILKYANSGGVRLGGLVCNE-RQTDKELELAEAlagmLGSKLIHFVPRDNIVQHAELRRMTVIEFAPESNQANV----YRQ 234
Cdd:PRK13185 165 IQAKAKNYKVRLAGVIANRsAGTDLIDKFNEA----VGLKVLAHVPDLDAIRRSRLKGKTLFEMEETDPGLEEvqneYLR 240

                        250       260
                 ....*....|....*....|....*..
gi 303306328 235 LAKKVHNNAgNGTIPTPITMDQLEDLL 261
Cdd:PRK13185 241 LAEQLLAGP-EPLVPKPLKDREIFELL 266
chlL CHL00072
photochlorophyllide reductase subunit L
 1-224 2.78e-42

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 146.42  E-value: 2.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSVEDLELEDVMKIGYKDIRCVE 80
Cdd:CHL00072   6 YGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEENGAYDGVDYVSYDVLGDVVCGGFAMPIreNKAQEIYIVMSGEMMAMYAANNISKGI 160
Cdd:CHL00072  86 AGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAANRIAASV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303306328 161 LKYANSGGVRLGGLVCNerQTDKelelaealagmlgsklihfvpRDNIVQHAELRRMTVIEFAP 224
Cdd:CHL00072 164 REKARTHPLRLAGLVGN--RTSK---------------------RDLIDKYVEACPMPVLEVLP 204
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 1-257 3.69e-42

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 147.29  E-value: 3.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   1 YGKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAE---AGsvEDLELEDV-MKIGykDI 76
Cdd:cd02033   37 YGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFGGKACPTIIETSTRkklAG--EEVKIGDVcFKRG--GV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  77 RCVESGGPEPGVGCAGRGVITSINFLEENGAYD-GVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANN 155
Cdd:cd02033  113 FAMELGGPEVGRGCGGRGIIHGFELLEKLGFHDwGFDYVLLDFLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSLYVANN 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 156 ISKGILKYANSGG-VRLGGLVCNERQTDKElelAEALAGMLGSKLIHFVPrdnivQHAELRRMTV---IEFAPESNQANV 231
Cdd:cd02033  193 VCSAVEYFRKLGGnVGVAGIVINKDDGTGE---AQAFAKAAGIPVLAAIP-----ADEDIRRKSAnyqIVGRPETQWGPL 264

                        250       260
                 ....*....|....*....|....*.
gi 303306328 232 YRQLAKKVHNNAGNGtiPTPITMDQL 257
Cdd:cd02033  265 FAELATNVAEAPPMR--PTPLSQDEL 288
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-239 2.23e-12

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 65.26  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328   3 KGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRL--ILHAKAQDTILSLAAEAGSVEDLeledVMKIGYKDIRCVE 80
Cdd:COG1192   10 KGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGlgLDPDDLDPTLYDLLLDDAPLEDA----IVPTEIPGLDLIP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  81 SGGPEPGVGCAGRGVITSINFLEE--NGAYDGVDYV------SYDVLGD--VVCggfampirenkAQEIYIVMSGEMMAM 150
Cdd:COG1192   86 ANIDLAGAEIELVSRPGRELRLKRalAPLADDYDYIlidcppSLGLLTLnaLAA-----------ADSVLIPVQPEYLSL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 151 YAANNIS---KGILKYANSgGVRLGGLVCN--ERQTDKELELAEALAGMLGSKLI-HFVPRDNIVQHAELRRMTVIEFAP 224
Cdd:COG1192  155 EGLAQLLetiEEVREDLNP-KLEILGILLTmvDPRTRLSREVLEELREEFGDKVLdTVIPRSVALAEAPSAGKPVFEYDP 233

                        250
                 ....*....|....*
gi 303306328 225 ESNQANVYRQLAKKV 239
Cdd:COG1192  234 KSKGAKAYRALAEEL 248
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 3-69 1.14e-07

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 50.66  E-value: 1.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303306328    3 KGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTR--LILHAKAQDTILSLAAEAGSVEDLELEDVM 69
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSglGIDKNNVEKTIYELLIGECNIEEAIIKTVI 78
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-41 1.93e-07

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 49.08  E-value: 1.93e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 303306328   3 KGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLI 41
Cdd:cd02042    9 KGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 17-239 4.19e-05

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 43.72  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  17 AALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEagsveDLELEDVMKIGYKDIRCVesggpePGvgcaGRGVI 96
Cdd:COG0455    8 AALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAG-----EADLEDAIVQGPGGLDVL------PG----GSGPA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328  97 TSINFLEENGAYDGVDYVS--YDV--------LGDVVCGGFAMpirenkAQEIYIVMSGEMMAMYAAnnisKGILKYANS 166
Cdd:COG0455   73 ELAELDPEERLIRVLEELErfYDVvlvdtgagISDSVLLFLAA------ADEVVVVTTPEPTSITDA----YALLKLLRR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303306328 167 -GGVRLGGLVCNERQTDKEL-----ELAEALAGMLGSKL--IHFVPRDNIVQHAELRRMTVIEFAPESNQANVYRQLAKK 238
Cdd:COG0455  143 rLGVRRAGVVVNRVRSEAEArdvfeRLEQVAERFLGVRLrvLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAAR 222


                 .
gi 303306328 239 V 239
Cdd:COG0455  223 L 223
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-32 5.22e-04

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 38.57  E-value: 5.22e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 303306328   2 GKGGIGKSTTSQNTLAALTELGQKILIVGCD 32
Cdd:cd01983    8 GKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 2-33 5.73e-04

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 40.80  E-value: 5.73e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 303306328    2 GKGGIGKSTTSQNTLAALTELGQKILIVGCDP 33
Cdd:pfam02374   8 GKGGVGKTTVSAATAVQLSELGKKVLLISTDP 39
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-32 5.84e-04

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 40.26  E-value: 5.84e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 303306328   2 GKGGIGKSTTSQNTLAALTELGQKILIVGCD 32
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 2-33 9.73e-04

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.46  E-value: 9.73e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 303306328    2 GKGGIGKSTTSQNTLAALTELGQKILIVGCDP 33
Cdd:TIGR04291  10 GKGGVGKTSIACATAINLADQGKRVLLVSTDP 41
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-70 2.39e-03

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 38.63  E-value: 2.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 303306328   2 GKGGIGKSTTSQNTLAALTELGQKILIVGCDpkadstrliLHAKAQDTILSLAAEAGSVEDL----ELEDVMK 70
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDAD---------LRGPSLHRMLGLENRPGLSDVLageaSLEDVIQ 163
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-32 3.16e-03

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 37.87  E-value: 3.16e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 303306328   2 GKGGIGKSTTSQNTLAALTELGQKILIVGCD 32
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 2-69 3.32e-03

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 38.10  E-value: 3.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303306328    2 GKGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEaGSVEDLELEDVM 69
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAE-GLKGRVNLDPIL 72
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-32 3.45e-03

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 37.93  E-value: 3.45e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 303306328   2 GKGGIGKSTTSQNTLAALTELGQKILIVGCD 32
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
PHA02518 PHA02518
ParA-like protein; Provisional
 3-60 3.92e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 37.91  E-value: 3.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 303306328   3 KGGIGKSTTSQNTLAALTELGQKILIVGCDPKADSTRLILHAKAQDTILSLAAEAGSV 60
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVRMGKSI 66
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 2-33 6.18e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 37.49  E-value: 6.18e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 303306328   2 GKGGIGKSTTSQNTLAALTELGQKILIVGCDP 33
Cdd:cd02035    7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
 
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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