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Conserved domains on  [gi|1024306804|gb|KZX16449|]
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nitrogenase iron protein 1 [Methanobrevibacter cuticularis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 19-277 1.48e-180

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: 497.09  E-value: 1.48e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTKNPRLGDIVFGGFGDVLC 97
Cdd:NF033200    1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMgGRRIPTILDLLRENKNIKEEDVVFEGYGGVRC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  98 VESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANNI 177
Cdd:NF033200   81 VESGGPEPGVGCAGRGIIVAMQLLEKLGAFMED-LDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 178 SKGIKKLKGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKLAKNIF 257
Cdd:NF033200  160 CKGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKIM 239

                         250       260
                  ....*....|....*....|
gi 1024306804 258 ENNSYSIPNPMDDDEFEEFF 277
Cdd:NF033200  240 ENTDFVIPEPLEDEELEELF 259
 
Name Accession Description Interval E-value
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 19-277 1.48e-180

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: 497.09  E-value: 1.48e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTKNPRLGDIVFGGFGDVLC 97
Cdd:NF033200    1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMgGRRIPTILDLLRENKNIKEEDVVFEGYGGVRC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  98 VESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANNI 177
Cdd:NF033200   81 VESGGPEPGVGCAGRGIIVAMQLLEKLGAFMED-LDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 178 SKGIKKLKGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKLAKNIF 257
Cdd:NF033200  160 CKGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKIM 239

                         250       260
                  ....*....|....*....|
gi 1024306804 258 ENNSYSIPNPMDDDEFEEFF 277
Cdd:NF033200  240 ENTDFVIPEPLEDEELEELF 259
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 17-282 5.24e-163

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: 453.47  E-value: 5.24e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  17 KQKKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTK-NPRLGDIVFGGFGD 94
Cdd:COG1348     1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLgGKRIPTVLDTLREKGeDVELEDIVFEGFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAA 174
Cdd:COG1348    81 VKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEED-LDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGIKKL----KGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYE 250
Cdd:COG1348   160 NNICKGIKKYanrgGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYR 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024306804 251 KLAKNIFENNSYSIPNPMDDDEFEEFFINFSK 282
Cdd:COG1348   240 ELAKKILENKKLVIPKPLSDEELEELLLEYGI 271
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 18-280 2.73e-156

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 436.15  E-value: 2.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  18 QKKIAIYGKGGIGKSTTVANIAASFSQNHkNVMVIGCDPKADTTRTLFGKRLPTILNTIKNTKNPRLGDIVFGGFGDVLC 97
Cdd:PRK13231    2 MKKIAIYGKGGIGKSTTVSNMAAAYSNDH-RVLVIGCDPKADTTRTLCGKRIPTVLDTLKDNRKPELEDIIHEGFNGILC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  98 VESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANNI 177
Cdd:PRK13231   81 VESGGPEPGVGCAGRGVIVAMNLLENLGVFDED-IDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAANNI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 178 SKGIKKLKGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKLAKNIF 257
Cdd:PRK13231  160 ARGIKKLKGKLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYRKLANNIM 239

                         250       260
                  ....*....|....*....|...
gi 1024306804 258 ENNSYSIPNPMDDDEFEEFFINF 280
Cdd:PRK13231  240 NNTEFSTPEPMDDEEFEEFFKSF 262
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 19-276 5.99e-146

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: 409.98  E-value: 5.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIK-NTKNPRLGDIVFGGFGDVL 96
Cdd:cd02040     1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLgGKAIPTVLDTLReKGEVEELEDVIKEGFNGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  97 CVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANN 176
Cdd:cd02040    81 CVESGGPEPGVGCAGRGIITAINLLEELGAYEED-LDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAANN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 177 ISKGIKKLKGN----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKL 252
Cdd:cd02040   160 IAKGIVKYAERggvrLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYREL 239

                         250       260
                  ....*....|....*....|....
gi 1024306804 253 AKNIFENNSYSIPNPMDDDEFEEF 276
Cdd:cd02040   240 AKKILENKKLVIPKPLTMEELEEL 263
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 19-283 1.48e-142

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: 401.77  E-value: 1.48e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFG-KRLPTILNTI--KNTKNPRLGDIVFGGFGDV 95
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGgKAQPTVLDVLreKGAEDLELEDVIKEGFGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  96 LCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAAN 175
Cdd:TIGR01287  81 RCVESGGPEPGVGCAGRGVITAINLLEELGAYEDD-LDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 176 NISKGIKKLKGN----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEK 251
Cdd:TIGR01287 160 NICKGILKYAKSggvrLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024306804 252 LAKNIFENNSYSIPNPMDDDEFEEFFINFSKI 283
Cdd:TIGR01287 240 LAKKIYENTEFVIPTPLTMDELEEILMKFGIM 271
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
19-280 1.91e-113

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 327.86  E-value: 1.91e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTKNP---RLGDIVFGGFGD 94
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLgGKLQPTVLDTAREKGYVedvEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDdnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAA 174
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAYDD--LDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGIKKlKGN-----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKY 249
Cdd:pfam00142 159 NNIAKGIQK-YAKsggvrLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEY 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024306804 250 EKLAKNIFENNSYSIPNPMDDDEFEEFFINF 280
Cdd:pfam00142 238 RELARKILENPKGTIPTPLSMDELEALLEDF 268
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 17-62 8.18e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 8.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1024306804   17 KQKKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTR 62
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVL 46
 
Name Accession Description Interval E-value
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 19-277 1.48e-180

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: 497.09  E-value: 1.48e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTKNPRLGDIVFGGFGDVLC 97
Cdd:NF033200    1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMgGRRIPTILDLLRENKNIKEEDVVFEGYGGVRC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  98 VESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANNI 177
Cdd:NF033200   81 VESGGPEPGVGCAGRGIIVAMQLLEKLGAFMED-LDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 178 SKGIKKLKGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKLAKNIF 257
Cdd:NF033200  160 CKGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKIM 239

                         250       260
                  ....*....|....*....|
gi 1024306804 258 ENNSYSIPNPMDDDEFEEFF 277
Cdd:NF033200  240 ENTDFVIPEPLEDEELEELF 259
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 17-282 5.24e-163

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: 453.47  E-value: 5.24e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  17 KQKKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTK-NPRLGDIVFGGFGD 94
Cdd:COG1348     1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLgGKRIPTVLDTLREKGeDVELEDIVFEGFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAA 174
Cdd:COG1348    81 VKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEED-LDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGIKKL----KGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYE 250
Cdd:COG1348   160 NNICKGIKKYanrgGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYR 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024306804 251 KLAKNIFENNSYSIPNPMDDDEFEEFFINFSK 282
Cdd:COG1348   240 ELAKKILENKKLVIPKPLSDEELEELLLEYGI 271
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 18-280 2.73e-156

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 436.15  E-value: 2.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  18 QKKIAIYGKGGIGKSTTVANIAASFSQNHkNVMVIGCDPKADTTRTLFGKRLPTILNTIKNTKNPRLGDIVFGGFGDVLC 97
Cdd:PRK13231    2 MKKIAIYGKGGIGKSTTVSNMAAAYSNDH-RVLVIGCDPKADTTRTLCGKRIPTVLDTLKDNRKPELEDIIHEGFNGILC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  98 VESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANNI 177
Cdd:PRK13231   81 VESGGPEPGVGCAGRGVIVAMNLLENLGVFDED-IDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAANNI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 178 SKGIKKLKGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKLAKNIF 257
Cdd:PRK13231  160 ARGIKKLKGKLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYRKLANNIM 239

                         250       260
                  ....*....|....*....|...
gi 1024306804 258 ENNSYSIPNPMDDDEFEEFFINF 280
Cdd:PRK13231  240 NNTEFSTPEPMDDEEFEEFFKSF 262
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 19-276 5.99e-146

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: 409.98  E-value: 5.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIK-NTKNPRLGDIVFGGFGDVL 96
Cdd:cd02040     1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLgGKAIPTVLDTLReKGEVEELEDVIKEGFNGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  97 CVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANN 176
Cdd:cd02040    81 CVESGGPEPGVGCAGRGIITAINLLEELGAYEED-LDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAANN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 177 ISKGIKKLKGN----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKL 252
Cdd:cd02040   160 IAKGIVKYAERggvrLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYREL 239

                         250       260
                  ....*....|....*....|....
gi 1024306804 253 AKNIFENNSYSIPNPMDDDEFEEF 276
Cdd:cd02040   240 AKKILENKKLVIPKPLTMEELEEL 263
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 19-283 1.48e-142

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: 401.77  E-value: 1.48e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFG-KRLPTILNTI--KNTKNPRLGDIVFGGFGDV 95
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGgKAQPTVLDVLreKGAEDLELEDVIKEGFGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  96 LCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAAN 175
Cdd:TIGR01287  81 RCVESGGPEPGVGCAGRGVITAINLLEELGAYEDD-LDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 176 NISKGIKKLKGN----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEK 251
Cdd:TIGR01287 160 NICKGILKYAKSggvrLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024306804 252 LAKNIFENNSYSIPNPMDDDEFEEFFINFSKI 283
Cdd:TIGR01287 240 LAKKIYENTEFVIPTPLTMDELEEILMKFGIM 271
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 19-275 9.91e-117

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 336.36  E-value: 9.91e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGKRLPTILNTI--KNTKNPRLGDIVFGGFGDVL 96
Cdd:PRK13230    2 RKFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLreKGIDNLGLEDIIYEGFNGIY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  97 CVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDNLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANN 176
Cdd:PRK13230   82 CVESGGPEPGYGCAGRGVITAIDLLKKLGVFEELGPDVVIYDILGDVVCGGFAMPLQKGLADDVYIVTTCDPMAIYAANN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 177 ISKGIKKL----KGNLGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKL 252
Cdd:PRK13230  162 ICKGIKRFakrgKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPDSEISNIFREL 241

                         250       260
                  ....*....|....*....|...
gi 1024306804 253 AKNIFENNSYSIPNPMDDDEFEE 275
Cdd:PRK13230  242 AEAIYENNTGTIPNPLEEEEIDQ 264
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
19-280 1.91e-113

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 327.86  E-value: 1.91e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTKNP---RLGDIVFGGFGD 94
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLgGKLQPTVLDTAREKGYVedvEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDdnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAA 174
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAYDD--LDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGIKKlKGN-----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKY 249
Cdd:pfam00142 159 NNIAKGIQK-YAKsggvrLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEY 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024306804 250 EKLAKNIFENNSYSIPNPMDDDEFEEFFINF 280
Cdd:pfam00142 238 RELARKILENPKGTIPTPLSMDELEALLEDF 268
nifH PRK13233
nitrogenase iron protein;
19-280 1.31e-103

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 302.89  E-value: 1.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNH-KNVMVIGCDPKADTTR-TLFGKRLPTILNTIKNTKNPR--LGDIVFGGFGD 94
Cdd:PRK13233    3 RKIAIYGKGGIGKSTTTQNTAAAMAYFHdKKVFIHGCDPKADSTRlILGGKPQTTMMDTLRELGEEKvtPDKVIKTGFKD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDDnLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAA 174
Cdd:PRK13233   83 IRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDD-LDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGIKKLKGN----LGGIICNCKGIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYE 250
Cdd:PRK13233  162 NNICKGLVKYAEQsgvrLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYK 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 1024306804 251 KLAKNIFENNSYSIPNPMDDDEFEEFFINF 280
Cdd:PRK13233  242 ELARKIIENKDFVIPKPLTMDELEEMVVKY 271
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 21-277 4.75e-100

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: 293.50  E-value: 4.75e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  21 IAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFG-KRLPTILNTI---KNTKNPRLGDIVFGGFGDVL 96
Cdd:cd02117     3 IVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGgKVPPTIDEMLtedGTAEELRREDLLFSGFNGVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  97 CVESGGPEPGVGCAGRGVIVAMKLLEKLGaFEDDNLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAANN 176
Cdd:cd02117    83 CVEAGGPEPGVGCGGRGIGTMLELLEEHG-LLDDDYDVVIFDVLGDVVCGGFAAPLRRGFAQKVVIVVSEELMSLYAANN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 177 ISKGIKKLKGN---LGGIICNCKGiENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEKLA 253
Cdd:cd02117   162 IVKAVENYSKNgvrLAGLVANLRD-PAGTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLA 240

                         250       260
                  ....*....|....*....|....*
gi 1024306804 254 KNIFENNSYSI-PNPMDDDEFEEFF 277
Cdd:cd02117   241 AKIADAVPPVPgPRPLSDRELFALL 265
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 19-277 4.72e-77

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: 235.27  E-value: 4.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGKRLPTILNTIK----NTKNPRLGDIVFGGFGD 94
Cdd:cd02032     1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQsvdfHYEEVWPEDVIFTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDdnLDVILYDVLGDVVCGGFAVPLkeNYADEVFIVTSGEYMSLYAA 174
Cdd:cd02032    81 VDCVEAGGPPAGTGCGGYVVGETVKLLKELNAFDE--YDVILFDVLGDVVCGGFAAPL--NYADYCLIVTANDFDSLFAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGI----KKLKGNLGGIICNcKGIENEQIivESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKK-- 248
Cdd:cd02032   157 NRIAAAVrekaKTYPVRLAGIIGN-RTDKTDLI--DKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPELNYvc 233

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024306804 249 --YEKLAKNIFENNSYSIPNPMDDDEFEEFF 277
Cdd:cd02032   234 deYLNIADQLLSDPEGVVPKPLPDREIFDLL 264
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 19-277 1.97e-75

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 231.00  E-value: 1.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGKRLPTILNTIK----NTKNPRLGDIVFGGFGD 94
Cdd:PRK13185    3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILEevdfHSEELRPEDFVYEGYNG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFEDdnLDVILYDVLGDVVCGGFAVPLkeNYADEVFIVTSGEYMSLYAA 174
Cdd:PRK13185   83 VDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDD--YDVILFDVLGDVVCGGFAAPL--QYADYALIVTANDFDSIFAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 175 NNISKGI----KKLKGNLGGIICNcKGIENEQIivESFAKRIGTNVIGTIPRDELVQKSEIEAKTL--IEKYPDSNQA-- 246
Cdd:PRK13185  159 NRIAAAIqakaKNYKVRLAGVIAN-RSAGTDLI--DKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLfeMEETDPGLEEvq 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024306804 247 KKYEKLAKNIFENNSYSIPNPMDDDEFEEFF 277
Cdd:PRK13185  236 NEYLRLAEQLLAGPEPLVPKPLKDREIFELL 266
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 21-277 1.62e-55

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: 181.95  E-value: 1.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  21 IAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF-GKRLPTILNTIKNTK----NPRLGDIVFGGfGDV 95
Cdd:cd02033    34 IAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFgGKACPTIIETSTRKKlageEVKIGDVCFKR-GGV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  96 LCVESGGPEPGVGCAGRGVIVAMKLLEKLGaFEDDNLDVILYDVLGDVVCGGFAVPLKENYADEVFIVTSGEYMSLYAAN 175
Cdd:cd02033   113 FAMELGGPEVGRGCGGRGIIHGFELLEKLG-FHDWGFDYVLLDFLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSLYVAN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 176 NISKGI---KKLKGNLG--GIICNCKGIENEqiiVESFAKRIGTNVIGTIPRDELVQKSeiEAKTLIEKYPDSNQAKKYE 250
Cdd:cd02033   192 NVCSAVeyfRKLGGNVGvaGIVINKDDGTGE---AQAFAKAAGIPVLAAIPADEDIRRK--SANYQIVGRPETQWGPLFA 266

                         250       260
                  ....*....|....*....|....*..
gi 1024306804 251 KLAKNIFENNSYSiPNPMDDDEFEEFF 277
Cdd:cd02033   267 ELATNVAEAPPMR-PTPLSQDELLGLF 292
chlL CHL00072
photochlorophyllide reductase subunit L
 20-238 7.55e-54

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 176.47  E-value: 7.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  20 KIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGKRLPTILNTIKNT----KNPRLGDIVFGGFGDV 95
Cdd:CHL00072    2 KLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKdyhyEDVWPEDVIYKGYGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  96 LCVESGGPEPGVGCAGRGVIVAMKLLEKLGAFedDNLDVILYDVLGDVVCGGFAVPLkeNYADEVFIVTSGEYMSLYAAN 175
Cdd:CHL00072   82 DCVEAGGPPAGAGCGGYVVGETVKLLKELNAF--YEYDIILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAAN 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024306804 176 NISKGIKK------LKgnLGGIICNckgIENEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTLIE 238
Cdd:CHL00072  158 RIAASVREkarthpLR--LAGLVGN---RTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFE 221
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 19-258 2.21e-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: 87.61  E-value: 2.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIY-GKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTrTLFGKRLPTILNTIKN--TKNPRLGDIV----FGG 91
Cdd:COG1192     2 KVIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLT-SGLGLDPDDLDPTLYDllLDDAPLEDAIvpteIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  92 FgDVLC--VESGGPEPGVGCAGRGVIVAMKLLEKLgafeDDNLDVILYDvlgdvvCGGFAVPLKEN---YADEVFIVTSG 166
Cdd:COG1192    81 L-DLIPanIDLAGAEIELVSRPGRELRLKRALAPL----ADDYDYILID------CPPSLGLLTLNalaAADSVLIPVQP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 167 EYMSLYAANNISKGIKKLKGNLG------GIICNC--KGIENEQIIVESFAKRIGTNVIGT-IPRDELVQKSEIEAKTLI 237
Cdd:COG1192   150 EYLSLEGLAQLLETIEEVREDLNpkleilGILLTMvdPRTRLSREVLEELREEFGDKVLDTvIPRSVALAEAPSAGKPVF 229

                         250       260
                  ....*....|....*....|.
gi 1024306804 238 EKYPDSNQAKKYEKLAKNIFE 258
Cdd:COG1192   230 EYDPKSKGAKAYRALAEELLE 250
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 33-258 1.38e-13

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: 68.38  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  33 TTVANIAASFSQNHKNVMVIGCDPKADTTRTLFG-KRLPTILNTIKNTKNPRlgDIVF---GGFgDVLcveSGGPEPGVg 108
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGlEPKATLADVLAGEADLE--DAIVqgpGGL-DVL---PGGSGPAE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 109 cagrgvIVAMKLLEKLG-AFE--DDNLDVILYDV---LGDVVCGGFAVplkenyADEVFIVTSGEYMSLYAAnniSKGIK 182
Cdd:COG0455    74 ------LAELDPEERLIrVLEelERFYDVVLVDTgagISDSVLLFLAA------ADEVVVVTTPEPTSITDA---YALLK 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 183 KLKGNLG----GIICN-CKGIENEQIIVESFAK------RIGTNVIGTIPRDELVQKSEIEAKTLIEKYPDSNQAKKYEK 251
Cdd:COG0455   139 LLRRRLGvrraGVVVNrVRSEAEARDVFERLEQvaerflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRE 218


                  ....*..
gi 1024306804 252 LAKNIFE 258
Cdd:COG0455   219 LAARLAG 225
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 19-256 2.57e-12

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 65.19  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVI------------GCDPKADTTRTLfGKRLPTILNTIKNTK------ 80
Cdd:COG3640     1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVdadpnanlaealGLEVEADLIKPL-GEMRELIKERTGAPGggmfkl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  81 NPRLGDIVfggfgDVLCVESGG--------PE-PGVGCAGRGVIVAMKLLEKLgafEDDNLDVILYD------VLGDVVC 145
Cdd:COG3640    80 NPKVDDIP-----EEYLVEGDGvdllvmgtIEeGGSGCYCPENALLRALLNHL---VLGNYEYVVVDmeagieHLGRGTA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 146 GGFavplkenyaDEVFIVTSGEYMSLYAANNISK-----GIKKLK--GNlggiicncKGIENEQiiVESFAKRIGTNVIG 218
Cdd:COG3640   152 EGV---------DLLLVVSEPSRRSIETARRIKElaeelGIKKIYlvGN--------KVREEED--EEFLRELLGLELLG 212

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1024306804 219 TIPRDELVQKSEIEAKTLIEkYPDSNQAKKYEKLAKNI 256
Cdd:COG3640   213 FIPYDEEVREADLEGKPLLD-LPDSPAVAAVEEIAEKL 249
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 19-256 4.56e-11

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: 61.56  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTL--------FGKRLPTILNTIKN---------TKN 81
Cdd:cd02034     1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLgveveklpLIKTIGDIRERTGAkkgeppegmSLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  82 PRLGDIVFGGfgdvlCVESGG---------PEPGVGCAGRGVIVAMKLLEKLGafeDDNLDVILYDVLGDVVCGGFAVPl 152
Cdd:cd02034    81 PYVDDIIKEI-----IVEPDGidllvmgrpEGGGSGCYCPVNALLRELLRHLA---LKNYEYVVIDMEAGIEHLSRGTI- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 153 keNYADEVFIVTSGEYMSLYAANNISKGIKKLKGNLGGIICNCKGIENEQIIVESFAkrIGTNVIGTIPRDELVQKSEIE 232
Cdd:cd02034   152 --RAVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELL--IKLKLIGVIPYDEEIMEADLK 227

                         250       260
                  ....*....|....*....|....
gi 1024306804 233 AKTLIEKypDSNQAKKYEKLAKNI 256
Cdd:cd02034   228 GKPLFDL--DSAAVKAIEKIVEKL 249
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 16-256 1.96e-10

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: 59.77  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  16 VKqKKIAIY-GKGGIGKSTTVANIAASFSQNHKNVMVIgcDpkADttrtLFGKRLPTILNTikNTKNPRLGDivfggfGD 94
Cdd:pfam10609   2 VK-HVIAVAsGKGGVGKSTVAVNLALALARLGYKVGLL--D--AD----IYGPSIPRMLGL--EGERPEQSD------GG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 VLCVESGG----------PEPGVGCAGRGVIVaMKLLEKLgaFED---DNLDVILYDV---LGDV---VCGgfAVPLken 155
Cdd:pfam10609  65 IIPVEAHGikvmsigfllPDEDDAVIWRGPMK-SGAIKQF--LTDvdwGELDYLIIDLppgTGDEqltLAQ--LLPL--- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 156 yaDEVFIVTSGEYMSLYAAnniSKGI---KKLKGNLGGIICN-----CKGIENEQII-----VESFAKRIGTNVIGTIPR 222
Cdd:pfam10609 137 --TGAVIVTTPQDVALLDV---RKAIdmfKKVNVPVLGVVENmsyfvCPHCGEETYIfgkggGEKLAEELGVPFLGEIPL 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024306804 223 DELVQKSEIEAKTLIEKYPDSNQAKKYEKLAKNI 256
Cdd:pfam10609 212 DPDIREAGDEGKPFVLADPDSPAAKAFLKIADKV 245
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 19-65 5.22e-10

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: 56.39  E-value: 5.22e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1024306804  19 KKIAIYG-KGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF 65
Cdd:cd02042     1 KVIAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWLY 48
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 19-243 1.61e-09

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: 56.81  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIY-GKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGKRLP-TILNTIKNTKnpRLGDIVF---GGFg 93
Cdd:cd02038     1 RIIAVTsGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKkTLGDVLKGRV--SLEDIIVegpEGL- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  94 DVLCVESGGPEpgvgCAGRGVIVAMKLLEKLGAFEdDNLDVILYD----VLGDVVcgGFAVPlkenyADEVFIVTSGEYM 169
Cdd:cd02038    78 DIIPGGSGMEE----LANLDPEQKAKLIEELSSLE-SNYDYLLIDtgagISRNVL--DFLLA-----ADEVIVVTTPEPT 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 170 SL---YAA-NNISKgiKKLKGNLGGIICNCKGIENEQIIVESFAKRIGTNV------IGTIPRDELVQKSEIEAKTLIEK 239
Cdd:cd02038   146 SItdaYALiKVLSR--RGGKKNFRLIVNMARSPKEGRATFERLKKVAKRFLdinldfVGFIPYDQSVRRAVRSQKPFVLL 223


                  ....
gi 1024306804 240 YPDS 243
Cdd:cd02038   224 FPNS 227
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 21-236 1.68e-09

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: 56.59  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  21 IAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPkaDTTRTLFGKRLPTILNTIKN-----TKNPRLGDIVFGGFGDV 95
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDP--QSNNSSVEGLEGDIAPALQAlaeglKGRVNLDPILLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  96 --LCVESGGPEPGVGCAG-RGVIVAMKLLEKLGAFEdDNLDVILYDvlgdvvC-GGFAVPLKENY--ADEVFIVTSGEYM 169
Cdd:pfam01656  80 ggLDLIPGNIDLEKFEKElLGPRKEERLREALEALK-EDYDYVIID------GaPGLGELLRNALiaADYVIIPLEPEVI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024306804 170 SLYAANNISKGIKKLKG-------NLGGIICNCKGIENEQIIVESFAKRI--GTNVIGTIPRDELVQKSEIEAKTL 236
Cdd:pfam01656 153 LVEDAKRLGGVIAALVGgyallglKIIGVVLNKVDGDNHGKLLKEALEELlrGLPVLGVIPRDEAVAEAPARGLPV 228
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 21-194 6.90e-09

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: 55.58  E-value: 6.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  21 IAIY-GKGGIGKSTTVANIAASFSQNHKNVMVIGCDpkadttrtLFGKRLPTILNtIKNtkNPRLGDIVFGGFG------ 93
Cdd:COG0489    95 IAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDAD--------LRGPSLHRMLG-LEN--RPGLSDVLAGEASledviq 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  94 -------DVLCVESGGPEPgvgcagRGVIVAMKLLEKLGAFEDDnLDVILYD---VLGDVvcggfAVPLKENYADEVFIV 163
Cdd:COG0489   164 pteveglDVLPAGPLPPNP------SELLASKRLKQLLEELRGR-YDYVIIDtppGLGVA-----DATLLASLVDGVLLV 231

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1024306804 164 TSGEYMSLYAANNISKGIKKLKGNLGGIICN 194
Cdd:COG0489   232 VRPGKTALDDVRKALEMLEKAGVPVLGVVLN 262
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 19-81 1.22e-07

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


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 50.66  E-value: 1.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024306804  19 KKIAIYG-KGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLF---GKRLPTILNTIKNTKN 81
Cdd:pfam13614   2 KVIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGidkNNVEKTIYELLIGECN 68
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 19-228 1.47e-06

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: 47.88  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIY-GKGGIGKSTTVANIAASFSQNHKNVMVIGCDpkadttrtLFGKRLPTILNTIKN---TKNPRLGDIVFGGfgd 94
Cdd:cd02037     1 HIIAVLsGKGGVGKSTVAVNLALALAKKGYKVGLLDAD--------IYGPSIPRLLGVEGKplhQSEEGIVPVEVGG--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  95 vLCVESGG---PEpgvgcaGRGVI----VAMKLLEKLgaFED---DNLDVILYDV---LGDVvcggfAVPLKENY-ADEV 160
Cdd:cd02037    70 -IKVMSIGfllPE------DDAVIwrgpMKSGAIKQF--LKDvdwGELDYLIIDLppgTGDE-----HLSLVQLIpIDGA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 161 FIVTSGEYMSLYAANnisKGI---KKLKGNLGGIICNCKGIE----NEQI------IVESFAKRIGTNVIGTIPRDELVQ 227
Cdd:cd02037   136 VVVTTPQEVSLIDVR---KAIdmcKKLNIPVLGIVENMSGFVcphcGKKIyifgkgGGEKLAEELGVPFLGKIPLDPELA 212


                  .
gi 1024306804 228 K 228
Cdd:cd02037   213 K 213
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 21-253 1.82e-06

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 48.04  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  21 IAIYG-KGGIGKSTTVANIAASFSQNHK-NVMVIGCD-PKADTTRTLFGKRLPTILNTIKNTKnpRLgDIVF-------- 89
Cdd:cd03111     3 VAVVGaKGGVGASTLAVNLAQELAQRAKdKVLLIDLDlPFGDLGLYLNLRPDYDLADVIQNLD--RL-DRTLldsavtrh 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  90 -GGFgDVLCvesgGPEPGVGCAGRGVIVAMKLLEKLGAFeddnLDVILYDvlgdvvCGGFAVPLKE---NYADEVFIVTS 165
Cdd:cd03111    80 sSGL-SLLP----APQELEDLEALGAEQVDKLLQVLRAF----YDHIIVD------LGHFLDEVTLavlEAADEILLVTQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 166 GEYMSLYAANNISKGIKKLKGNLGG--IICNCKGiENEQIIVESFAKRIGTNVIGTIPRDE-LVQKSEIEAKTLIEKYPD 242
Cdd:cd03111   145 QDLPSLRNARRLLDSLRELEGSSDRlrLVLNRYD-KKSEISPKDIEEALGLEVFATLPNDYkAVSESANTGRPLVEVAPR 223

                         250
                  ....*....|.
gi 1024306804 243 SNQAKKYEKLA 253
Cdd:cd03111   224 SALVRALQDLA 234
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 25-256 2.81e-04

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


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 41.42  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  25 GKGGIGKSTTVANIAASFSQNHKNVMVIGCDPkadTTRTL---FG--KRLP-TILNTIKNtkNPRLGD-IVFGGFGDVLC 97
Cdd:cd02036     8 GKGGVGKTTTTANLGVALAKLGKKVLLIDADI---GLRNLdliLGleNRIVyTLVDVLEG--ECRLEQaLIKDKRWENLY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804  98 vesggpepgvgcagrgVIVAMKLLEKLGAFEDDNLDVI-----LYD-VLGDVVCG---GF---AVPlkenyADEVFIVTS 165
Cdd:cd02036    83 ----------------LLPASQTRDKDALTPEKLEELVkelkdSFDfILIDSPAGiesGFinaIAP-----ADEAIIVTN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804 166 GEYMSLYAANNI-----SKGIKKLkgnlgGIICNCKGIE----NEQIIVESFAKRIGTNVIGTIPRDELVQKSEIEAKTL 236
Cdd:cd02036   142 PEISSVRDADRViglleSKGIVNI-----GLIVNRYRPEmvksGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPL 216

                         250       260
                  ....*....|....*....|
gi 1024306804 237 IEKYPDSNQAKKYEKLAKNI 256
Cdd:cd02036   217 VLYKPNSLAAKAFENIARRL 236
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 17-52 3.25e-04

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 41.55  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1024306804  17 KQKKIAIYGKGGIGKSTTVANIAASFSQNHKN--VMVI 52
Cdd:TIGR03499 193 QGGVIALVGPTGVGKTTTLAKLAARFALEHGKkkVALI 230
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 19-57 3.43e-04

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: 41.18  E-value: 3.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1024306804  19 KKIAIYG-KGGIGKSTTVANIAASFSQNHKNVMVIGCDPK 57
Cdd:TIGR03371   2 KVIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 19-55 3.66e-04

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 3.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1024306804  19 KKIAIYG-KGGIGKSTTVANIAASFSQNHKNVMVIGCD 55
Cdd:cd01983     1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 17-62 8.18e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 8.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1024306804   17 KQKKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTR 62
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVL 46
PRK04195 PRK04195
replication factor C large subunit; Provisional
 9-82 2.64e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 39.13  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024306804   9 WLFGVlmvKQKKIAIYGKGGIGKSTTVANIAASFS----------QNHKNVM--VIGcdpKADTTRTLFGKR-------- 68
Cdd:PRK04195   33 WLKGK---PKKALLLYGPPGVGKTSLAHALANDYGwevielnasdQRTADVIerVAG---EAATSGSLFGARrklillde 106

                          90       100
                  ....*....|....*....|....*.
gi 1024306804  69 ------------LPTILNTIKNTKNP 82
Cdd:PRK04195  107 vdgihgnedrggARAILELIKKAKQP 132
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 28-76 2.83e-03

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: 37.93  E-value: 2.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1024306804  28 GIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGKRLPTILNTI 76
Cdd:cd05387    30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEV 78
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 19-74 3.15e-03

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: 38.48  E-value: 3.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPK---ADTTRTLFGKrLPTILN 74
Cdd:pfam02374   2 RWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAhslSDSFNQKFGH-EPTKVK 59
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 21-55 3.24e-03

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 37.74  E-value: 3.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1024306804  21 IAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCD 55
Cdd:cd03115     3 ILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAAD 37
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 19-55 3.88e-03

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 37.53  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1024306804  19 KKIAIYGKGGIGKSTTVANIAASFSQNH-KNVMVIGCD 55
Cdd:cd17873     1 RVIALVGPTGVGKTTTLAKLAARYVLKKgKKVALITTD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 17-67 3.93e-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: 38.53  E-value: 3.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024306804  17 KQKKIAIYGKGGIGKSTTVANIAASFSQNHKNVMVIGCDPKADTTRTLFGK 67
Cdd:TIGR04291 320 EKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGS 370
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
17-55 6.66e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 37.54  E-value: 6.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1024306804  17 KQKKIAIYGKGGIGKSTTVANIAASFSQNH-KNVMVIGCD 55
Cdd:COG1419   163 EGGVIALVGPTGVGKTTTIAKLAARFVLRGkKKVALITTD 202
 
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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