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Conserved domains on  [gi|575523318|gb|AHG98010|]
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NifH [Cloning vector pCV_cistron14]

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 ...
 3-279 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: 546.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   3 MRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsvEDLELEDVLQIGYG 82
Cdd:COG1348    2 MRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  83 DVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 162
Cdd:COG1348   80 GVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 163 NNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYR 242
Cdd:COG1348  160 NNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYR 239

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 575523318 243 TLAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEED 279
Cdd:COG1348  240 ELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED 276
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 3-279 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: 546.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   3 MRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsvEDLELEDVLQIGYG 82
Cdd:COG1348    2 MRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  83 DVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 162
Cdd:COG1348   80 GVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 163 NNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYR 242
Cdd:COG1348  160 NNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYR 239

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 575523318 243 TLAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEED 279
Cdd:COG1348  240 ELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED 276
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 4-279 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: 541.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318    4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSvEDLELEDVLQIGYGD 83
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:TIGR01287  80 IRCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  164 NISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:TIGR01287 160 NICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 575523318  244 LAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEED 279
Cdd:TIGR01287 240 LAKKIYENTEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 4-270 1.15e-179

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: 1.15e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsvEDLELEDVLQIGYGD 83
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:cd02040   79 IKCVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAAN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 164 NISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:cd02040  159 NIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRE 238

                        250       260
                 ....*....|....*....|....*..
gi 575523318 244 LAQKIVNNTMKVVPTPCTMDELESLLM 270
Cdd:cd02040  239 LAKKILENKKLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
4-275 3.60e-158

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 441.50  E-value: 3.60e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318    4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQIGYGD 83
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAY-DDLDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  164 NISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:pfam00142 160 NIAKGIQKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 575523318  244 LAQKIVNNTMKVVPTPCTMDELESLLMEFGIM 275
Cdd:pfam00142 240 LARKILENPKGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
1-276 3.62e-151

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 423.85  E-value: 3.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   1 MTmRQCAIYGKGGIGKSTTTQNLVAALAEM-GKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSvEDLELEDVLQI 79
Cdd:PRK13233   1 MT-RKIAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  80 GYGDVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAM 159
Cdd:PRK13233  79 GFKDIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 160 YAANNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQAN 239
Cdd:PRK13233 159 YAANNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAK 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 575523318 240 EYRTLAQKIVNNTMKVVPTPCTMDELESLLMEFGIME 276
Cdd:PRK13233 239 EYKELARKIIENKDFVIPKPLTMDELEEMVVKYGLMD 275
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 4-268 6.67e-139

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: 392.32  E-value: 6.67e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsveDLELEDVLQIGYGD 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:NF033200  78 VRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 164 NISKGIVKYaksgKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:NF033200 158 NICKGIKKL----KGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRK 233

                        250       260
                 ....*....|....*....|....*
gi 575523318 244 LAQKIVNNTMKVVPTPCTMDELESL 268
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 ...
 3-279 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: 546.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   3 MRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsvEDLELEDVLQIGYG 82
Cdd:COG1348    2 MRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  83 DVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 162
Cdd:COG1348   80 GVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 163 NNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYR 242
Cdd:COG1348  160 NNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYR 239

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 575523318 243 TLAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEED 279
Cdd:COG1348  240 ELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED 276
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 4-279 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: 541.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318    4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSvEDLELEDVLQIGYGD 83
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:TIGR01287  80 IRCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  164 NISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:TIGR01287 160 NICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 575523318  244 LAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEED 279
Cdd:TIGR01287 240 LAKKIYENTEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 4-270 1.15e-179

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: 1.15e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsvEDLELEDVLQIGYGD 83
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:cd02040   79 IKCVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAAN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 164 NISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:cd02040  159 NIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRE 238

                        250       260
                 ....*....|....*....|....*..
gi 575523318 244 LAQKIVNNTMKVVPTPCTMDELESLLM 270
Cdd:cd02040  239 LAKKILENKKLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
4-275 3.60e-158

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 441.50  E-value: 3.60e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318    4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQIGYGD 83
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAY-DDLDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  164 NISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:pfam00142 160 NIAKGIQKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 575523318  244 LAQKIVNNTMKVVPTPCTMDELESLLMEFGIM 275
Cdd:pfam00142 240 LARKILENPKGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
1-276 3.62e-151

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 423.85  E-value: 3.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   1 MTmRQCAIYGKGGIGKSTTTQNLVAALAEM-GKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSvEDLELEDVLQI 79
Cdd:PRK13233   1 MT-RKIAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  80 GYGDVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAM 159
Cdd:PRK13233  79 GFKDIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 160 YAANNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQAN 239
Cdd:PRK13233 159 YAANNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAK 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 575523318 240 EYRTLAQKIVNNTMKVVPTPCTMDELESLLMEFGIME 276
Cdd:PRK13233 239 EYKELARKIIENKDFVIPKPLTMDELEEMVVKYGLMD 275
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 4-268 6.67e-139

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: 392.32  E-value: 6.67e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGsveDLELEDVLQIGYGD 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:NF033200  78 VRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 164 NISKGIVKYaksgKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:NF033200 158 NICKGIKKL----KGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRK 233

                        250       260
                 ....*....|....*....|....*
gi 575523318 244 LAQKIVNNTMKVVPTPCTMDELESL 268
Cdd:NF033200 234 LAKKIMENTDFVIPEPLEDEELEEL 258
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 4-270 4.88e-132

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: 375.16  E-value: 4.88e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   4 RQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQIGYGD 83
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDLLFSGFNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  84 VRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAAN 163
Cdd:cd02117   81 VDCVEAGGPEPGVGCGGRGIGTMLELLEEHGLLDDDYDVVIFDVLGDVVCGGFAAPLRRGFAQKVVIVVSEELMSLYAAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 164 NISKGIVKYAKSGkVRLGGLICNSRQTdREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRT 243
Cdd:cd02117  161 NIVKAVENYSKNG-VRLAGLVANLRDP-AGTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFAR 238

                        250       260
                 ....*....|....*....|....*...
gi 575523318 244 LAQKIVNNTMKVV-PTPCTMDELESLLM 270
Cdd:cd02117  239 LAAKIADAVPPVPgPRPLSDRELFALLG 266
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 3-268 5.54e-106

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 309.39  E-value: 5.54e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   3 MRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAqNTIMEMAAEVGsVEDLELEDVLQIGYG 82
Cdd:PRK13230   1 MRKFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKI-PTVLDVLREKG-IDNLGLEDIIYEGFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  83 DVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYED-DLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA 161
Cdd:PRK13230  79 GIYCVESGGPEPGYGCAGRGVITAIDLLKKLGVFEElGPDVVIYDILGDVVCGGFAMPLQKGLADDVYIVTTCDPMAIYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 162 ANNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEY 241
Cdd:PRK13230 159 ANNICKGIKRFAKRGKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPDSEISNIF 238

                        250       260
                 ....*....|....*....|....*..
gi 575523318 242 RTLAQKIVNNTMKVVPTPCTMDELESL 268
Cdd:PRK13230 239 RELAEAIYENNTGTIPNPLEEEEIDQI 265
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 3-272 1.65e-95

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 282.46  E-value: 1.65e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   3 MRQCAIYGKGGIGKSTTTQNLVAALAEmGKKVMIVGCDPKADSTRlILHAKAQNTIMEMAAEVgsvEDLELEDVLQIGYG 82
Cdd:PRK13231   2 MKKIAIYGKGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTR-TLCGKRIPTVLDTLKDN---RKPELEDIIHEGFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  83 DVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA 162
Cdd:PRK13231  77 GILCVESGGPEPGVGCAGRGVIVAMNLLENLGVFDEDIDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 163 NNISKGIVKYaksgKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYR 242
Cdd:PRK13231 157 NNIARGIKKL----KGKLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYR 232

                        250       260       270
                 ....*....|....*....|....*....|
gi 575523318 243 TLAQKIVNNTMKVVPTPCTMDELESLLMEF 272
Cdd:PRK13231 233 KLANNIMNNTEFSTPEPMDDEEFEEFFKSF 262
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 7-272 9.01e-68

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: 211.77  E-value: 9.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHaKAQNTIMEMAAEVG-SVEDLELEDVLQIGYGDVR 85
Cdd:cd02032    4 AVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTG-FLIPTVIDVLQSVDfHYEEVWPEDVIFTGYGGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  86 CAESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDVLGDVVCGGFAMPIreNKAQEIYIVCSGEMMAMYAANNI 165
Cdd:cd02032   83 CVEAGGPPAGTGCGGYVVGETVKLLKELNAF-DEYDVILFDVLGDVVCGGFAAPL--NYADYCLIVTANDFDSLFAANRI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 166 SKGIVKYAKSGKVRLGGLICN-SRQTDredeLIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQAN----E 240
Cdd:cd02032  160 AAAVREKAKTYPVRLAGIIGNrTDKTD----LIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPELNyvcdE 235

                        250       260       270
                 ....*....|....*....|....*....|..
gi 575523318 241 YRTLAQKIVNNTMKVVPTPCTMDELESLLMEF 272
Cdd:cd02032  236 YLNIADQLLSDPEGVVPKPLPDREIFDLLGDF 267
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 7-269 1.75e-67

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 211.36  E-value: 1.75e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTrLILHAKAQNTIMEMAAEVG-SVEDLELEDVLQIGYGDVR 85
Cdd:PRK13185   6 AVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST-FTLTGKLVPTVIDILEEVDfHSEELRPEDFVYEGYNGVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  86 CAESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDVLGDVVCGGFAMPIreNKAQEIYIVCSGEMMAMYAANNI 165
Cdd:PRK13185  85 CVEAGGPPAGTGCGGYVVGETVKLLKEHHLL-DDYDVILFDVLGDVVCGGFAAPL--QYADYALIVTANDFDSIFAANRI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 166 SKGIVKYAKSGKVRLGGLICN-SRQTDredeLIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDP------ACKQa 238
Cdd:PRK13185 162 AAAIQAKAKNYKVRLAGVIANrSAGTD----LIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEEtdpgleEVQN- 236

                        250       260       270
                 ....*....|....*....|....*....|.
gi 575523318 239 nEYRTLAQKIVNNTMKVVPTPCTMDELESLL 269
Cdd:PRK13185 237 -EYLRLAEQLLAGPEPLVPKPLKDREIFELL 266
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 7-280 5.44e-49

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: 165.39  E-value: 5.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSV-EDLELEDVLqIGYGDVR 85
Cdd:cd02033   35 AIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFGGKACPTIIETSTRKKLAgEEVKIGDVC-FKRGGVF 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  86 CAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAANNI 165
Cdd:cd02033  114 AMELGGPEVGRGCGGRGIIHGFELLEKLGFHDWGFDYVLLDFLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSLYVANNV 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 166 SKGIVKYAK-SGKVRLGGLICNSRQTDREDEliiALAEKLGTQMIHFVPRDNivqraEIRRMTViEYDPACKQANEYRTL 244
Cdd:cd02033  194 CSAVEYFRKlGGNVGVAGIVINKDDGTGEAQ---AFAKAAGIPVLAAIPADE-----DIRRKSA-NYQIVGRPETQWGPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 575523318 245 AQKIVNNTMK---VVPTPCTMDELesllmeFGIMEEEDT 280
Cdd:cd02033  265 FAELATNVAEappMRPTPLSQDEL------LGLFSSEET 297
chlL CHL00072
photochlorophyllide reductase subunit L
 7-272 1.03e-45

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 155.67  E-value: 1.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTrLILHAKAQNTIME-MAAEVGSVEDLELEDVLQIGYGDVR 85
Cdd:CHL00072   4 AVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDST-FTLTGFLIPTIIDtLQSKDYHYEDVWPEDVIYKGYGGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  86 CAESGGPEPGVGCAGRGVITAINFLEEEGAYeDDLDFVFYDVLGDVVCGGFAMPIreNKAQEIYIVCSGEMMAMYAANNI 165
Cdd:CHL00072  83 CVEAGGPPAGAGCGGYVVGETVKLLKELNAF-YEYDIILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAANRI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 166 SKGIVKYAKSGKVRLGGLICNsrQTDREDeLIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIE---YDPACKQANE-Y 241
Cdd:CHL00072 160 AASVREKARTHPLRLAGLVGN--RTSKRD-LIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEmveSEPSLNYVCDyY 236

                        250       260       270
                 ....*....|....*....|....*....|.
gi 575523318 242 RTLAQKIVNNTMKVVPTPCTMDELESLLMEF 272
Cdd:CHL00072 237 LNIADQLLSQPEGVVPKEVPDRELFSLLSDF 267
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-249 6.31e-18

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: 81.06  E-value: 6.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   3 MRQCAIY-GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRL--ILHAKAQNTIMEMAAEVGSVEDLELE----- 74
Cdd:COG1192    1 MKVIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGlgLDPDDLDPTLYDLLLDDAPLEDAIVPteipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  75 -DVLqIGYGDVRCAESggpePGVGCAGRGVITAiNFLEEegaYEDDLDFVFYDV---LGDVVCGGFAMpirenkAQEIYI 150
Cdd:COG1192   81 lDLI-PANIDLAGAEI----ELVSRPGRELRLK-RALAP---LADDYDYILIDCppsLGLLTLNALAA------ADSVLI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 151 VCSGEMMAMYAANNISKGIVKYAKSGKVRL---GGLICNSRQTDREDELIIA-LAEKLGTQMI-HFVPRDNIVQRAEIRR 225
Cdd:COG1192  146 PVQPEYLSLEGLAQLLETIEEVREDLNPKLeilGILLTMVDPRTRLSREVLEeLREEFGDKVLdTVIPRSVALAEAPSAG 225

                        250       260
                 ....*....|....*....|....
gi 575523318 226 MTVIEYDPACKQANEYRTLAQKIV 249
Cdd:COG1192  226 KPVFEYDPKSKGAKAYRALAEELL 249
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 11-49 2.82e-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: 2.82e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 575523318  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 8.32e-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: 59.52  E-value: 8.32e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575523318    3 MRQCAIYG-KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTR--LILHAKAQNTIMEMAAEVGSVEDLELEDVL 77
Cdd:pfam13614   1 GKVIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSglGIDKNNVEKTIYELLIGECNIEEAIIKTVI 78
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-250 3.45e-10

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: 58.75  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  18 TTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAevgsvEDLELEDVLQIGYGDVRcaesggpepgVG 97
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLA-----GEADLEDAIVQGPGGLD----------VL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  98 CAGRGVITAINFLEEEG------AYEDDLDFVFYDV---LGDVVCGGFAMpirenkAQEIYIVCSGEMMAMYAANNISKG 168
Cdd:COG0455   66 PGGSGPAELAELDPEERlirvleELERFYDVVLVDTgagISDSVLLFLAA------ADEVVVVTTPEPTSITDAYALLKL 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 169 IvkyAKSGKVRLGGLICNSRQTDRE-----DELIIALAEKLGTQM--IHFVPRDNIVQRAEIRRMTVIEYDPACKQANEY 241
Cdd:COG0455  140 L---RRRLGVRRAGVVVNRVRSEAEardvfERLEQVAERFLGVRLrvLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAI 216


                 ....*....
gi 575523318 242 RTLAQKIVN 250
Cdd:COG0455  217 RELAARLAG 225
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 10-236 5.15e-10

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: 58.35  E-value: 5.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTImemaaevGSV--EDLELEDVLQIGYGDVRC- 86
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTL-------GDVlkGRVSLEDIIVEGPEGLDIi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  87 -AESGGPEpgvgcagrgvITAIN------FLEEEGAYEDDLDFVFYDV---LGDVVCGGFAMpirenkAQEIYIVCSGE- 155
Cdd:cd02038   81 pGGSGMEE----------LANLDpeqkakLIEELSSLESNYDYLLIDTgagISRNVLDFLLA------ADEVIVVTTPEp 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318 156 --MMAMYAA--NNISKGIVKYAKsgkvrlggLICNSRQTDREDeliIALAEKLGT----------QMIHFVPRDNIVQRA 221
Cdd:cd02038  145 tsITDAYALikVLSRRGGKKNFR--------LIVNMARSPKEG---RATFERLKKvakrfldinlDFVGFIPYDQSVRRA 213

                        250
                 ....*....|....*
gi 575523318 222 EIRRMTVIEYDPACK 236
Cdd:cd02038  214 VRSQKPFVLLFPNSK 228
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 4-187 1.43e-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: 48.97  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   4 RQCAIYG-KGGIGKSTTTQNLVAALAEMGKKVMIVGCDpkadstrlilhakaqntimemaaevgsvedleledvlqigyg 82
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318  83 dvrcaesggpepgvgcagrgvitainfleeegayeddlDFVFYDVLGDVVCGGF----AMPIRENKAQEIYIVCSGEMMA 158
Cdd:cd01983   39 --------------------------------------DYVLIDGGGGLETGLLlgtiVALLALKKADEVIVVVDPELGS 80

                        170       180
                 ....*....|....*....|....*....
gi 575523318 159 MYAANNISKgiVKYAKSGKVRLGGLICNS 187
Cdd:cd01983   81 LLEAVKLLL--ALLLLGIGIRPDGIVLNK 107
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 10-78 3.05e-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: 50.57  E-value: 3.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDpkadstrliLHAKAQNTIMEMAAEVGSVEDL----ELEDVLQ 78
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDAD---------LRGPSLHRMLGLENRPGLSDVLageaSLEDVIQ 163
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 10-40 6.60e-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: 49.12  E-value: 6.60e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 10-40 6.99e-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: 49.04  E-value: 6.99e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 10-37 1.11e-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: 48.60  E-value: 1.11e-06
                          10        20
                  ....*....|....*....|....*...
gi 575523318   10 GKGGIGKSTTTQNLVAALAEMGKKVMIV 37
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYKVGLL 38
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 10-228 4.17e-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: 43.87  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEvGSVEDLELEDVLQIGYGDVR---- 85
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAE-GLKGRVNLDPILLKEKSDEGgldl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523318   86 --CAESGGPEPGVGCAGRGVITAINFLEeegAYEDDLDFVFYD---------VLGDVVCGGFAMPIRenkaQEIYIVCSG 154
Cdd:pfam01656  85 ipGNIDLEKFEKELLGPRKEERLREALE---ALKEDYDYVIIDgapglgellRNALIAADYVIIPLE----PEVILVEDA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523318  155 EMMAMYAANniskgIVKYAKSGKVRLGGLICN-SRQTDREDELIIALAE-KLGTQMIHFVPRDNIVQRAEIRRMTV 228
Cdd:pfam01656 158 KRLGGVIAA-----LVGGYALLGLKIIGVVLNkVDGDNHGKLLKEALEElLRGLPVLGVIPRDEAVAEAPARGLPV 228
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 13-40 9.82e-05

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: 9.82e-05
                         10        20
                 ....*....|....*....|....*...
gi 575523318  13 GIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDAD 57
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-41 1.19e-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: 1.19e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 575523318   10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:TIGR04291  10 GKGGVGKTSIACATAINLADQGKRVLLVSTDP 41
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
10-40 1.23e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.11  E-value: 1.23e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:PRK11670 115 GKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 7-41 1.41e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.46  E-value: 1.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 575523318   7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:COG3640    4 AVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
PHA02518 PHA02518
ParA-like protein; Provisional
 11-46 1.56e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 42.14  E-value: 1.56e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 575523318  11 KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADST 46
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST 44
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 1-43 3.98e-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: 41.61  E-value: 3.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 575523318    1 MTMrqcaiyGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKA 43
Cdd:TIGR04291 325 MTM------GKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAA 361
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 10-41 5.60e-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: 5.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 575523318   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 5.81e-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: 40.37  E-value: 5.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 575523318   7 AIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKA 43
Cdd:cd02034    4 AVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS 40
minD CHL00175
septum-site determining protein; Validated
 10-40 1.04e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 39.75  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCD 40
Cdd:CHL00175  23 GKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 7-78 1.08e-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: 40.10  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523318   7 AIYG-KGGIGKSTTTQNLVAALA-EMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQ 78
Cdd:COG4963  106 AVVGaKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALT 179
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 10-41 1.37e-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: 1.37e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 575523318  10 GKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP 41
Cdd:cd02035    7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-42 2.51e-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: 2.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 575523318    3 MRQCAIYG-KGGIGKSTTTQNLVAALAEMGKKVMIVGCDPK 42
Cdd:TIGR03371   1 MKVIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
10-41 3.65e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 38.26  E-value: 3.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 575523318  10 GKGGIGKSTttqnlVAA-----LAEMGKKVMIVGCDP 41
Cdd:COG0003   10 GKGGVGKTT-----VAAatalaLAERGKRTLLVSTDP 41
 
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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