NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13096254|pdb|1G20|F]
View 

Chain F, NITROGENASE IRON PROTEIN

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 2-278 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: 545.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        2 AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtvEDLELEDVLKAGY 81
Cdd:COG1348   1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       82 GGVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA 160
Cdd:COG1348  79 GGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVlGDVVCGGFAMPIREGYADEIYIVTSGEFMALYA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      161 ANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEY 240
Cdd:COG1348 159 ANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEY 238

                       250       260       270
                ....*....|....*....|....*....|....*...
1G20_F      241 RALARKVVDNKLLVIPNPITMDELEELLMEFGIMEVED 278
Cdd:COG1348 239 RELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED 276
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 2-278 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: 545.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        2 AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtvEDLELEDVLKAGY 81
Cdd:COG1348   1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       82 GGVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA 160
Cdd:COG1348  79 GGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVlGDVVCGGFAMPIREGYADEIYIVTSGEFMALYA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      161 ANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEY 240
Cdd:COG1348 159 ANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEY 238

                       250       260       270
                ....*....|....*....|....*....|....*...
1G20_F      241 RALARKVVDNKLLVIPNPITMDELEELLMEFGIMEVED 278
Cdd:COG1348 239 RELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED 276
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 4-278 0e+00

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: 529.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F          4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTvEDLELEDVLKAGYGG 83
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:TIGR01287  80 IRCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVlGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        163 NISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:TIGR01287 160 NICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
1G20_F        243 LARKVVDNKLLVIPNPITMDELEELLMEFGIMEVED 278
Cdd:TIGR01287 240 LAKKIYENTEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 4-269 8.85e-180

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: 495.49  E-value: 8.85e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtvEDLELEDVLKAGYGG 83
Cdd:cd02040   1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:cd02040  79 IKCVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVlGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAAN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      163 NISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:cd02040 159 NIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRE 238

                       250       260
                ....*....|....*....|....*..
1G20_F      243 LARKVVDNKLLVIPNPITMDELEELLM 269
Cdd:cd02040 239 LAKKILENKKLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
4-274 9.93e-158

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 440.34  E-value: 9.93e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F          4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGYGG 83
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAY-DDLDFVLYDVlGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        163 NISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:pfam00142 160 NIAKGIQKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|..
1G20_F        243 LARKVVDNKLLVIPNPITMDELEELLMEFGIM 274
Cdd:pfam00142 240 LARKILENPKGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
4-275 1.09e-149

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 419.99  E-value: 1.09e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         4 RQCAIYGKGGIGKSTTTQNLVAALAEM-GKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTvEDLELEDVLKAGYG 82
Cdd:PRK13233   3 RKIAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKTGFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        83 GVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 161
Cdd:PRK13233  82 DIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDDLDFVFFDVlGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       162 NNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYR 241
Cdd:PRK13233 162 NNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYK 241

                        250       260       270
                 ....*....|....*....|....*....|....
1G20_F       242 ALARKVVDNKLLVIPNPITMDELEELLMEFGIME 275
Cdd:PRK13233 242 ELARKIIENKDFVIPKPLTMDELEEMVVKYGLMD 275
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 4-267 5.76e-138

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: 389.62  E-value: 5.76e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtveDLELEDVLKAGYGG 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:NF033200  78 VRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVlGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       163 NISKGIVKYANsgsvRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:NF033200 158 NICKGIKKLKG----RLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRK 233

                        250       260
                 ....*....|....*....|....*
1G20_F       243 LARKVVDNKLLVIPNPITMDELEEL 267
Cdd:NF033200 234 LAKKIMENTDFVIPEPLEDEELEEL 258
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 2-278 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: 545.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        2 AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtvEDLELEDVLKAGY 81
Cdd:COG1348   1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       82 GGVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA 160
Cdd:COG1348  79 GGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVlGDVVCGGFAMPIREGYADEIYIVTSGEFMALYA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      161 ANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEY 240
Cdd:COG1348 159 ANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEY 238

                       250       260       270
                ....*....|....*....|....*....|....*...
1G20_F      241 RALARKVVDNKLLVIPNPITMDELEELLMEFGIMEVED 278
Cdd:COG1348 239 RELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED 276
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 4-278 0e+00

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: 529.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F          4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTvEDLELEDVLKAGYGG 83
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:TIGR01287  80 IRCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVlGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        163 NISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:TIGR01287 160 NICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
1G20_F        243 LARKVVDNKLLVIPNPITMDELEELLMEFGIMEVED 278
Cdd:TIGR01287 240 LAKKIYENTEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 4-269 8.85e-180

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: 495.49  E-value: 8.85e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtvEDLELEDVLKAGYGG 83
Cdd:cd02040   1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:cd02040  79 IKCVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVlGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAAN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      163 NISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:cd02040 159 NIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRE 238

                       250       260
                ....*....|....*....|....*..
1G20_F      243 LARKVVDNKLLVIPNPITMDELEELLM 269
Cdd:cd02040 239 LAKKILENKKLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
4-274 9.93e-158

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 440.34  E-value: 9.93e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F          4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGYGG 83
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAY-DDLDFVLYDVlGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        163 NISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:pfam00142 160 NIAKGIQKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|..
1G20_F        243 LARKVVDNKLLVIPNPITMDELEELLMEFGIM 274
Cdd:pfam00142 240 LARKILENPKGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
4-275 1.09e-149

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 419.99  E-value: 1.09e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         4 RQCAIYGKGGIGKSTTTQNLVAALAEM-GKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTvEDLELEDVLKAGYG 82
Cdd:PRK13233   3 RKIAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKTGFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        83 GVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 161
Cdd:PRK13233  82 DIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDDLDFVFFDVlGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       162 NNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYR 241
Cdd:PRK13233 162 NNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYK 241

                        250       260       270
                 ....*....|....*....|....*....|....
1G20_F       242 ALARKVVDNKLLVIPNPITMDELEELLMEFGIME 275
Cdd:PRK13233 242 ELARKIIENKDFVIPKPLTMDELEEMVVKYGLMD 275
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 4-269 4.27e-140

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: 395.20  E-value: 4.27e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGYGG 83
Cdd:cd02117   1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDLLFSGFNG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:cd02117  81 VDCVEAGGPEPGVGCGGRGIGTMLELLEEHGLLDDDYDVVIFDVlGDVVCGGFAAPLRRGFAQKVVIVVSEELMSLYAAN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      163 NISKGIVKYANSGsVRLGGLICNSRNTdREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:cd02117 161 NIVKAVENYSKNG-VRLAGLVANLRDP-AGTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFAR 238

                       250       260
                ....*....|....*....|....*...
1G20_F      243 LARKVVDNKLLVI-PNPITMDELEELLM 269
Cdd:cd02117 239 LAAKIADAVPPVPgPRPLSDRELFALLG 266
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 4-267 5.76e-138

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: 389.62  E-value: 5.76e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGtveDLELEDVLKAGYGG 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:NF033200  78 VRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVlGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       163 NISKGIVKYANsgsvRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRA 242
Cdd:NF033200 158 NICKGIKKLKG----RLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRK 233

                        250       260
                 ....*....|....*....|....*
1G20_F       243 LARKVVDNKLLVIPNPITMDELEEL 267
Cdd:NF033200 234 LAKKIMENTDFVIPEPLEDEELEEL 258
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 3-267 1.83e-105

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 308.24  E-value: 1.83e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         3 MRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAqNTIMEMAAEAGtVEDLELEDVLKAGYG 82
Cdd:PRK13230   1 MRKFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKI-PTVLDVLREKG-IDNLGLEDIIYEGFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        83 GVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYED-DLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA 160
Cdd:PRK13230  79 GIYCVESGGPEPGYGCAGRGVITAIDLLKKLGVFEElGPDVVIYDIlGDVVCGGFAMPLQKGLADDVYIVTTCDPMAIYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       161 ANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEY 240
Cdd:PRK13230 159 ANNICKGIKRFAKRGKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPDSEISNIF 238

                        250       260
                 ....*....|....*....|....*..
1G20_F       241 RALARKVVDNKLLVIPNPITMDELEEL 267
Cdd:PRK13230 239 RELAEAIYENNTGTIPNPLEEEEIDQI 265
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 3-271 1.38e-94

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 279.76  E-value: 1.38e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         3 MRQCAIYGKGGIGKSTTTQNLVAALAEmGKKVMIVGCDPKADSTRlILHSKAQNTIMEMAAEAgtvEDLELEDVLKAGYG 82
Cdd:PRK13231   2 MKKIAIYGKGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTR-TLCGKRIPTVLDTLKDN---RKPELEDIIHEGFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        83 GVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDV-GDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 161
Cdd:PRK13231  77 GILCVESGGPEPGVGCAGRGVIVAMNLLENLGVFDEDIDVVIYDVlGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       162 NNISKGIVKYANsgsvRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYR 241
Cdd:PRK13231 157 NNIARGIKKLKG----KLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYR 232

                        250       260       270
                 ....*....|....*....|....*....|
1G20_F       242 ALARKVVDNKLLVIPNPITMDELEELLMEF 271
Cdd:PRK13231 233 KLANNIMNNTEFSTPEPMDDEEFEEFFKSF 262
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 7-271 1.33e-65

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: 205.99  E-value: 1.33e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGYGGVKC 86
Cdd:cd02032   4 AVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGGVDC 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       87 VESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDV-GDVVCGGFAMPIreNKAQEIYIVCSGEMMAMYAANNIS 165
Cdd:cd02032  84 VEAGGPPAGTGCGGYVVGETVKLLKELNAF-DEYDVILFDVlGDVVCGGFAAPL--NYADYCLIVTANDFDSLFAANRIA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      166 KGIVKYANSGSVRLGGLICN-SRNTDredeLIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDP----KAKQADEY 240
Cdd:cd02032 161 AAVREKAKTYPVRLAGIIGNrTDKTD----LIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEEsepeLNYVCDEY 236

                       250       260       270
                ....*....|....*....|....*....|.
1G20_F      241 RALARKVVDNKLLVIPNPITMDELEELLMEF 271
Cdd:cd02032 237 LNIADQLLSDPEGVVPKPLPDREIFDLLGDF 267
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 7-268 6.03e-63

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 199.42  E-value: 6.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTrLILHSKAQNTIMEMAAEAG-TVEDLELEDVLKAGYGGVK 85
Cdd:PRK13185   6 AVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST-FTLTGKLVPTVIDILEEVDfHSEELRPEDFVYEGYNGVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        86 CVESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDV-GDVVCGGFAMPIreNKAQEIYIVCSGEMMAMYAANNI 164
Cdd:PRK13185  85 CVEAGGPPAGTGCGGYVVGETVKLLKEHHLL-DDYDVILFDVlGDVVCGGFAAPL--QYADYALIVTANDFDSIFAANRI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       165 SKGIVKYANSGSVRLGGLICN-SRNTDredeLIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDP----KAKQADE 239
Cdd:PRK13185 162 AAAIQAKAKNYKVRLAGVIANrSAGTD----LIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEEtdpgLEEVQNE 237

                        250       260
                 ....*....|....*....|....*....
1G20_F       240 YRALARKVVDNKLLVIPNPITMDELEELL 268
Cdd:PRK13185 238 YLRLAEQLLAGPEPLVPKPLKDREIFELL 266
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 7-286 1.91e-46

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: 158.84  E-value: 1.91e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAE---AGtvEDLELEDVLkAGYGG 83
Cdd:cd02033  35 AIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFGGKACPTIIETSTRkklAG--EEVKIGDVC-FKRGG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       84 VKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYD-VGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 162
Cdd:cd02033 112 VFAMELGGPEVGRGCGGRGIIHGFELLEKLGFHDWGFDYVLLDfLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSLYVAN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      163 NISKGIVKYAN-SGSVRLGGLICNSRNTDREDEliiALANKLGTQMIHFVPRDNvvqraEIRRMTV---IEYDPKAKQAD 238
Cdd:cd02033 192 NVCSAVEYFRKlGGNVGVAGIVINKDDGTGEAQ---AFAKAAGIPVLAAIPADE-----DIRRKSAnyqIVGRPETQWGP 263

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
1G20_F      239 EYRALARKVVDNKLLViPNPITMDEL------EELLMEFGIMEVEDESIVGKTA 286
Cdd:cd02033 264 LFAELATNVAEAPPMR-PTPLSQDELlglfssEETGRDVVLVPATDEDMRGKDA 316
chlL CHL00072
photochlorophyllide reductase subunit L
 7-192 5.71e-44

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 151.04  E-value: 5.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F         7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGYGGVKC 86
Cdd:CHL00072   4 AVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        87 VESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDV-GDVVCGGFAMPIreNKAQEIYIVCSGEMMAMYAANNIS 165
Cdd:CHL00072  84 VEAGGPPAGAGCGGYVVGETVKLLKELNAF-YEYDIILFDVlGDVVCGGFAAPL--NYADYCIIITDNGFDALFAANRIA 160

                        170       180
                 ....*....|....*....|....*..
1G20_F       166 KGIVKYANSGSVRLGGLICNsRNTDRE 192
Cdd:CHL00072 161 ASVREKARTHPLRLAGLVGN-RTSKRD 186
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-249 8.44e-20

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: 86.07  E-value: 8.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        3 MRQCAIY-GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRL--ILHSKAQNTIMEMAAEAGTVEDLeledVLKA 79
Cdd:COG1192   1 MKVIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGlgLDPDDLDPTLYDLLLDDAPLEDA----IVPT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       80 GYGGVKCVESG----GPEPGVGCAGRGVITAINFLEEegaYEDDLDFVFYDvgdvvCGG----------FAmpirenkAQ 145
Cdd:COG1192  77 EIPGLDLIPANidlaGAEIELVSRPGRELRLKRALAP---LADDYDYILID-----CPPslglltlnalAA-------AD 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      146 EIYIVCSGEMMAMYAANNIS---KGIVKYANSGSVRLGGLICNSRNTDREDELIIA-LANKLGTQMI-HFVPRDNVVQRA 220
Cdd:COG1192 142 SVLIPVQPEYLSLEGLAQLLetiEEVREDLNPKLEILGILLTMVDPRTRLSREVLEeLREEFGDKVLdTVIPRSVALAEA 221

                       250       260
                ....*....|....*....|....*....
1G20_F      221 EIRRMTVIEYDPKAKQADEYRALARKVVD 249
Cdd:COG1192 222 PSAGKPVFEYDPKSKGAKAYRALAEELLE 250
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 10-235 2.01e-11

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: 62.20  E-value: 2.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTImemaaeaGTV--EDLELEDVLKAGYGGVkCV 87
Cdd:cd02038   8 GKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTL-------GDVlkGRVSLEDIIVEGPEGL-DI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       88 ESGGpepgvgcAGRGVITAIN------FLEEEGAYEDDLDFVFYDVG----DVVCGGFAMpirenkAQEIYIVCSGE--- 154
Cdd:cd02038  80 IPGG-------SGMEELANLDpeqkakLIEELSSLESNYDYLLIDTGagisRNVLDFLLA------ADEVIVVTTPEpts 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      155 MMAMYAA--NNISKGIVKYAnsgsvrlgGLICNSRNTDREDE-----LIIALANKLGT--QMIHFVPRDNVVQRAEIRRM 225
Cdd:cd02038 147 ITDAYALikVLSRRGGKKNF--------RLIVNMARSPKEGRatferLKKVAKRFLDInlDFVGFIPYDQSVRRAVRSQK 218

                       250
                ....*....|
1G20_F      226 TVIEYDPKAK 235
Cdd:cd02038 219 PFVLLFPNSK 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-249 3.02e-11

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: 61.83  E-value: 3.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       18 TTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEagtveDLELEDVLKAGYGGVKCVeSGGPEPgvg 97
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAG-----EADLEDAIVQGPGGLDVL-PGGSGP--- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       98 cAGRGVITAINFLEEE-GAYEDDLDFVFYDVG----DVVCGGFAMpirenkAQEIYIVCSGEMMAMYAANNISKGIvkyA 172
Cdd:COG0455  72 -AELAELDPEERLIRVlEELERFYDVVLVDTGagisDSVLLFLAA------ADEVVVVTTPEPTSITDAYALLKLL---R 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F      173 NSGSVRLGGLICNSRNTDRE-----DELIIALANKLGTQM--IHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRALAR 245
Cdd:COG0455 142 RRLGVRRAGVVVNRVRSEAEardvfERLEQVAERFLGVRLrvLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAA 221


                ....
1G20_F      246 KVVD 249
Cdd:COG0455 222 RLAG 225
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 11-49 3.13e-11

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: 59.86  E-value: 3.13e-11
                        10        20        30
                ....*....|....*....|....*....|....*....
1G20_F       11 KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLI 49
Cdd:cd02042   9 KGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 3-77 7.42e-11

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: 59.90  E-value: 7.42e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1G20_F          3 MRQCAIYG-KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTR--LILHSKAQNTIMEMAAEAGTVEDLELEDVL 77
Cdd:pfam13614   1 GKVIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSglGIDKNNVEKTIYELLIGECNIEEAIIKTVI 78
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 4-82 2.44e-07

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: 48.20  E-value: 2.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F        4 RQCAIYG-KGGIGKSTTTQNLVAALAEMGKKVMIVGCDpkadstrlilhskaQNTIMEMAAEAGTVEDLELEDVLKAGYG 82
Cdd:cd01983   1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD--------------DYVLIDGGGGLETGLLLGTIVALLALKK 66
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 10-126 4.47e-07

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: 50.19  E-value: 4.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G20_F       10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDpkadstrliLHSKAQNTIMEMAAEAGTVEDL----ELEDVLKA-GYGGV 84
Cdd:COG0489 100 GKGGEGKSTVAANLALALAQSGKRVLLIDAD---------LRGPSLHRMLGLENRPGLSDVLageaSLEDVIQPtEVEGL 170

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1G20_F       85 KCVESGG-PEPGVGCAGRGVITAinFLEEegaYEDDLDFVFYD 126
Cdd:COG0489 171 DVLPAGPlPPNPSELLASKRLKQ--LLEE---LRGRYDYVIID 208
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 10-40 9.02e-07

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: 48.65  E-value: 9.02e-07
                        10        20        30
                ....*....|....*....|....*....|.
1G20_F       10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:cd02037   8 GKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 10-40 9.15e-07

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: 48.74  E-value: 9.15e-07
                        10        20        30
                ....*....|....*....|....*....|.
1G20_F       10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:cd02036   8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 10-37 1.46e-06

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 48.22  E-value: 1.46e-06
                          10        20
                  ....*....|....*....|....*...
1G20_F         10 GKGGIGKSTTTQNLVAALAEMGKKVMIV 37
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYKVGLL 38
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 10-41 8.14e-05

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: 43.10  E-value: 8.14e-05
                          10        20        30
                  ....*....|....*....|....*....|..
1G20_F         10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDP 37
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-41 1.15e-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: 43.54  E-value: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|..
1G20_F         10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:TIGR04291  10 GKGGVGKTSIACATAINLADQGKRVLLVSTDP 41
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
10-40 1.16e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.11  E-value: 1.16e-04
                         10        20        30
                 ....*....|....*....|....*....|.
1G20_F        10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:PRK11670 115 GKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 13-40 1.25e-04

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 42.17  E-value: 1.25e-04
                        10        20
                ....*....|....*....|....*...
1G20_F       13 GIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:cd05387  30 GEGKSTVAANLAVALAQSGKRVLLIDAD 57
PHA02518 PHA02518
ParA-like protein; Provisional
 11-46 1.69e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 41.76  E-value: 1.69e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
1G20_F        11 KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADST 46
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST 44
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 7-41 2.04e-04

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 41.69  E-value: 2.04e-04
                        10        20        30
                ....*....|....*....|....*....|....*
1G20_F        7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:COG3640   4 AVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 10-41 6.25e-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: 6.25e-04
                          10        20        30
                  ....*....|....*....|....*....|..
1G20_F         10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:pfam02374   8 GKGGVGKTTVSAATAVQLSELGKKVLLISTDP 39
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 7-43 7.81e-04

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 39.99  E-value: 7.81e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
1G20_F        7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKA 43
Cdd:cd02034   4 AVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS 40
minD CHL00175
septum-site determining protein; Validated
 10-40 1.23e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 39.75  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
1G20_F        10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:CHL00175  23 GKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 10-41 1.43e-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: 39.41  E-value: 1.43e-03
                        10        20        30
                ....*....|....*....|....*....|..
1G20_F       10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:cd02035   7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-43 1.93e-03

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: 39.69  E-value: 1.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....
1G20_F         10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKA 43
Cdd:TIGR04291 328 GKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAA 361
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-42 2.46e-03

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 38.48  E-value: 2.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
1G20_F          3 MRQCAIYG-KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPK 42
Cdd:TIGR03371   1 MKVIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
10-41 4.54e-03

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 37.88  E-value: 4.54e-03
                        10        20        30
                ....*....|....*....|....*....|..
1G20_F       10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:COG0003  10 GKGGVGKTTVAAATALALAERGKRTLLVSTDP 41
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 7-77 8.42e-03

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 37.40  E-value: 8.42e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1G20_F        7 AIYG-KGGIGKSTTTQNLVAALA-EMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVL 77
Cdd:COG4963 106 AVVGaKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRAL 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH