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Conserved domains on  [gi|1369061829|ref|WP_106499484|]
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MULTISPECIES: ferredoxin:protochlorophyllide reductase (ATP-dependent) iron-sulfur ATP-binding protein [Synechococcus]

Protein Classification

ferredoxin:protochlorophyllide reductase (ATP-dependent) iron-sulfur ATP-binding protein( domain architecture ID 10793742)

ferredoxin:protochlorophyllide reductase (ATP-dependent) iron-sulfur ATP-binding protein is a light-independent component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 35-302 0e+00

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


:

Pssm-ID: 237293  Cd Length: 270  Bit Score: 561.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  35 GALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGY 114
Cdd:PRK13185    1 MALVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILEEVDFHSEELRPEDFVYEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 115 NGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNR 194
Cdd:PRK13185   81 NGVDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPLQYADYALIVTANDFDSIFAANR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEATPE-VEAVQKEYIA 273
Cdd:PRK13185  161 IAAAIQAKAKNYKVRLAGVIANRSAGTDLIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEETDPgLEEVQNEYLR 240

                         250       260
                  ....*....|....*....|....*....
gi 1369061829 274 LAQRMLDNVVPLEAESLKDREIFDLLGFD 302
Cdd:PRK13185  241 LAEQLLAGPEPLVPKPLKDREIFELLGFD 269
 
Name Accession Description Interval E-value
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 35-302 0e+00

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 561.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  35 GALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGY 114
Cdd:PRK13185    1 MALVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILEEVDFHSEELRPEDFVYEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 115 NGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNR 194
Cdd:PRK13185   81 NGVDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPLQYADYALIVTANDFDSIFAANR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEATPE-VEAVQKEYIA 273
Cdd:PRK13185  161 IAAAIQAKAKNYKVRLAGVIANRSAGTDLIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEETDPgLEEVQNEYLR 240

                         250       260
                  ....*....|....*....|....*....
gi 1369061829 274 LAQRMLDNVVPLEAESLKDREIFDLLGFD 302
Cdd:PRK13185  241 LAEQLLAGPEPLVPKPLKDREIFELLGFD 269
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 37-302 0e+00

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: 529.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  37 LVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGYNG 116
Cdd:cd02032     1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRII 196
Cdd:cd02032    81 VDCVEAGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTANDFDSLFAANRIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 197 AAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEM-EATPEVEAVQKEYIALA 275
Cdd:cd02032   161 AAVREKAKTYPVRLAGIIGNRTDKTDLIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMeESEPELNYVCDEYLNIA 240

                         250       260
                  ....*....|....*....|....*..
gi 1369061829 276 QRMLDNVVPLEAESLKDREIFDLLGFD 302
Cdd:cd02032   241 DQLLSDPEGVVPKPLPDREIFDLLGDF 267
DPOR_bchL TIGR01281
light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; The BchL ...
 37-300 2.54e-163

light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; The BchL peptide (ChlL in chloroplast and cyanobacteria) is an ATP-binding iron-sulfur protein of the dark form protochlorophyllide reductase, an enzyme similar to nitrogenase. This subunit resembles the nitrogenase NifH subunit. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 130348  Cd Length: 268  Bit Score: 454.65  E-value: 2.54e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  37 LVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGYNG 116
Cdd:TIGR01281   1 MILAVYGKGGIGKSTTSSNLSVAFAKLGKRVLQIGCDPKHDSTFTLTGRLIPTVIDVLQAVNYHYEDVRPEDVIYTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRII 196
Cdd:TIGR01281  81 VDCVEAGGPPAGSGCGGYVVGETVKLLKEHHILDDYDVILFDVLGDVVCGGFATPLQYADYALVVAANDFDALFAANRIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 197 AAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEAT-PEVEAVQKEYIALA 275
Cdd:TIGR01281 161 ASVQEKAKNYDVRLAGIIGNRSDATDLIERFNERVGMPVLGVVPDLEVIRRSRVKGKTLFEMEESgPELAAVTQEYLRMA 240

                         250       260
                  ....*....|....*....|....*
gi 1369061829 276 QRMLDNVVPLEAESLKDREIFDLLG 300
Cdd:TIGR01281 241 EYLLAGPEGVVPTPLIDREIFELLG 265
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 39-299 4.25e-105

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: 307.48  E-value: 4.25e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTK-KMVPTVIDILETVDfhtEELRPEDFVFEGYNGV 117
Cdd:COG1348     5 IAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGgKRIPTVLDTLREKG---EDVELEDIVFEGFGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLE-DTDVVIFDVLGDVVCGGFAAPLQ--HANYCLIVTANDFDSIFAMNR 194
Cdd:COG1348    82 KCVEAGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIRegYADEIYIVTSGEFMALYAANN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVANR---SKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEatPEVEAVQkEY 271
Cdd:COG1348   162 ICKGIKKYANRGGVRLGGIICNSrnvDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYA--PDSEQAD-EY 238

                         250       260
                  ....*....|....*....|....*...
gi 1369061829 272 IALAQRMLDNVVPLEAESLKDREIFDLL 299
Cdd:COG1348   239 RELAKKILENKKLVIPKPLSDEELEELL 266
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
39-299 2.13e-96

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 285.11  E-value: 2.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDST-FTLTKKMVPTVIDILETVDFHtEELRPEDFVFEGYNGV 117
Cdd:pfam00142   3 IAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrLLLGGKLQPTVLDTAREKGYV-EDVEVEDVVYKGYGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDSIFAMNRI 195
Cdd:pfam00142  82 KCVESGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIREgkAQEIYIVTSNEMMALYAANNI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 196 IAAIQAKAKNYKVRLGGVVANRSKDTDQ---IDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEATPEveaVQKEYI 272
Cdd:pfam00142 162 AKGIQKYAKSGGVRLGGIICNSRKVDDErelIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSE---QAQEYR 238

                         250       260
                  ....*....|....*....|....*..
gi 1369061829 273 ALAQRMLDNVVPLEAESLKDREIFDLL 299
Cdd:pfam00142 239 ELARKILENPKGTIPTPLSMDELEALL 265
 
Name Accession Description Interval E-value
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 35-302 0e+00

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 561.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  35 GALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGY 114
Cdd:PRK13185    1 MALVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILEEVDFHSEELRPEDFVYEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 115 NGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNR 194
Cdd:PRK13185   81 NGVDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPLQYADYALIVTANDFDSIFAANR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEATPE-VEAVQKEYIA 273
Cdd:PRK13185  161 IAAAIQAKAKNYKVRLAGVIANRSAGTDLIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEETDPgLEEVQNEYLR 240

                         250       260
                  ....*....|....*....|....*....
gi 1369061829 274 LAQRMLDNVVPLEAESLKDREIFDLLGFD 302
Cdd:PRK13185  241 LAEQLLAGPEPLVPKPLKDREIFELLGFD 269
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 37-302 0e+00

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: 529.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  37 LVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGYNG 116
Cdd:cd02032     1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRII 196
Cdd:cd02032    81 VDCVEAGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTANDFDSLFAANRIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 197 AAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEM-EATPEVEAVQKEYIALA 275
Cdd:cd02032   161 AAVREKAKTYPVRLAGIIGNRTDKTDLIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMeESEPELNYVCDEYLNIA 240

                         250       260
                  ....*....|....*....|....*..
gi 1369061829 276 QRMLDNVVPLEAESLKDREIFDLLGFD 302
Cdd:cd02032   241 DQLLSDPEGVVPKPLPDREIFDLLGDF 267
DPOR_bchL TIGR01281
light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; The BchL ...
 37-300 2.54e-163

light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; The BchL peptide (ChlL in chloroplast and cyanobacteria) is an ATP-binding iron-sulfur protein of the dark form protochlorophyllide reductase, an enzyme similar to nitrogenase. This subunit resembles the nitrogenase NifH subunit. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 130348  Cd Length: 268  Bit Score: 454.65  E-value: 2.54e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  37 LVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGYNG 116
Cdd:TIGR01281   1 MILAVYGKGGIGKSTTSSNLSVAFAKLGKRVLQIGCDPKHDSTFTLTGRLIPTVIDVLQAVNYHYEDVRPEDVIYTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRII 196
Cdd:TIGR01281  81 VDCVEAGGPPAGSGCGGYVVGETVKLLKEHHILDDYDVILFDVLGDVVCGGFATPLQYADYALVVAANDFDALFAANRIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 197 AAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEAT-PEVEAVQKEYIALA 275
Cdd:TIGR01281 161 ASVQEKAKNYDVRLAGIIGNRSDATDLIERFNERVGMPVLGVVPDLEVIRRSRVKGKTLFEMEESgPELAAVTQEYLRMA 240

                         250       260
                  ....*....|....*....|....*
gi 1369061829 276 QRMLDNVVPLEAESLKDREIFDLLG 300
Cdd:TIGR01281 241 EYLLAGPEGVVPTPLIDREIFELLG 265
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 38-300 6.90e-135

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: 382.87  E-value: 6.90e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGYNGV 117
Cdd:cd02117     2 SIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDLLFSGFNGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLED-TDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDSIFAMNR 194
Cdd:cd02117    82 DCVEAGGPEPGVGCGGRGIGTMLELLEEHGLLDDdYDVVIFDVLGDVVCGGFAAPLRRgfAQKVVIVVSEELMSLYAANN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNyKVRLGGVVANRS--KDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMeatPEVEAVQKEYI 272
Cdd:cd02117   162 IVKAVENYSKN-GVRLAGLVANLRdpAGTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEH---DPVSPAASEFA 237

                         250       260
                  ....*....|....*....|....*....
gi 1369061829 273 ALAQRMLDNVVPLEA-ESLKDREIFDLLG 300
Cdd:cd02117   238 RLAAKIADAVPPVPGpRPLSDRELFALLG 266
chlL CHL00072
photochlorophyllide reductase subunit L
 39-299 1.61e-119

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 344.80  E-value: 1.61e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILETVDFHTEELRPEDFVFEGYNGVM 118
Cdd:CHL00072    3 LAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 119 CVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIIAA 198
Cdd:CHL00072   83 CVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAAS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 199 IQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEM-EATPEVEAVQKEYIALAQR 277
Cdd:CHL00072  163 VREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMvESEPSLNYVCDYYLNIADQ 242

                         250       260
                  ....*....|....*....|....*
gi 1369061829 278 MLDN---VVPLEaesLKDREIFDLL 299
Cdd:CHL00072  243 LLSQpegVVPKE---VPDRELFSLL 264
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 39-299 4.25e-105

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: 307.48  E-value: 4.25e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTK-KMVPTVIDILETVDfhtEELRPEDFVFEGYNGV 117
Cdd:COG1348     5 IAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGgKRIPTVLDTLREKG---EDVELEDIVFEGFGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLE-DTDVVIFDVLGDVVCGGFAAPLQ--HANYCLIVTANDFDSIFAMNR 194
Cdd:COG1348    82 KCVEAGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIRegYADEIYIVTSGEFMALYAANN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVANR---SKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEatPEVEAVQkEY 271
Cdd:COG1348   162 ICKGIKKYANRGGVRLGGIICNSrnvDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYA--PDSEQAD-EY 238

                         250       260
                  ....*....|....*....|....*...
gi 1369061829 272 IALAQRMLDNVVPLEAESLKDREIFDLL 299
Cdd:COG1348   239 RELAKKILENKKLVIPKPLSDEELEELL 266
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
39-299 2.13e-96

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 285.11  E-value: 2.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDST-FTLTKKMVPTVIDILETVDFHtEELRPEDFVFEGYNGV 117
Cdd:pfam00142   3 IAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrLLLGGKLQPTVLDTAREKGYV-EDVEVEDVVYKGYGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDSIFAMNRI 195
Cdd:pfam00142  82 KCVESGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIREgkAQEIYIVTSNEMMALYAANNI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 196 IAAIQAKAKNYKVRLGGVVANRSKDTDQ---IDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIFEMEATPEveaVQKEYI 272
Cdd:pfam00142 162 AKGIQKYAKSGGVRLGGIICNSRKVDDErelIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSE---QAQEYR 238

                         250       260
                  ....*....|....*....|....*..
gi 1369061829 273 ALAQRMLDNVVPLEAESLKDREIFDLL 299
Cdd:pfam00142 239 ELARKILENPKGTIPTPLSMDELEALL 265
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 39-299 6.66e-86

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: 258.21  E-value: 6.66e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLT-KKMVPTVIDILETVDfhtEELRPEDFVFEGYNGV 117
Cdd:cd02040     3 IAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLgGKAIPTVLDTLREKG---EVEELEDVIKEGFNGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVESGGPPAGTGCGGYVTGQTVKLLKEHHLL-EDTDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDSIFAMNR 194
Cdd:cd02040    80 KCVESGGPEPGVGCAGRGIITAINLLEELGAYeEDLDVVFYDVLGDVVCGGFAMPIREgyADEVYIVTSGEMMALYAANN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVANRSK---DTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIfeMEATPEvEAVQKEY 271
Cdd:cd02040   160 IAKGIVKYAERGGVRLGGLICNSRNvdrEEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTV--IEYDPD-SEQADEY 236

                         250       260
                  ....*....|....*....|....*...
gi 1369061829 272 IALAQRMLDNVVPLEAESLKDREIFDLL 299
Cdd:cd02040   237 RELAKKILENKKLVIPKPLTMEELEELL 264
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 39-292 4.71e-67

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 210.78  E-value: 4.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILEtvDFHTEELRPEDFVFEGYNGVM 118
Cdd:PRK13230    4 FCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLR--EKGIDNLGLEDIIYEGFNGIY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 119 CVESGGPPAGTGCGGYVTGQTVKLLKEHHLLED--TDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDSIFAMNR 194
Cdd:PRK13230   82 CVESGGPEPGYGCAGRGVITAIDLLKKLGVFEElgPDVVIYDILGDVVCGGFAMPLQKglADDVYIVTTCDPMAIYAANN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 195 IIAAIQAKAKNYKVRLGGVVAN-RS--KDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIfeMEATPEVEaVQKEY 271
Cdd:PRK13230  162 ICKGIKRFAKRGKSALGGIIYNgRSviDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTV--IEYAPDSE-ISNIF 238

                         250       260
                  ....*....|....*....|....*.
gi 1369061829 272 IALAQRMLDN---VV--PLEAESLKD 292
Cdd:PRK13230  239 RELAEAIYENntgTIpnPLEEEEIDQ 264
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 39-294 3.27e-56

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 182.30  E-value: 3.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKlGKRVLQIGCDPKHDSTFTLTKKMVPTVIDILEtvdfhtEELRPE--DFVFEGYNG 116
Cdd:PRK13231    5 IAIYGKGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTRTLCGKRIPTVLDTLK------DNRKPEleDIIHEGFNG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLL-EDTDVVIFDVLGDVVCGGFAAPLQ--HANYCLIVTANDFDSIFAMN 193
Cdd:PRK13231   78 ILCVESGGPEPGVGCAGRGVIVAMNLLENLGVFdEDIDVVIYDVLGDVVCGGFSVPLRedYADEVYIVTSGEYMSLYAAN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 194 RIIAAIqakaKNYKVRLGGVVAN-RSKDTDQ--IDKFNERVGMRTMAHFPDLDAIRRSRLKKCTIfeMEATPEVEAvQKE 270
Cdd:PRK13231  158 NIARGI----KKLKGKLGGIICNcRGIDNEVeiVSEFASRIGSRIIGVIPRSNLVQESELDAKTV--VETFPESEQ-ASV 230

                         250       260
                  ....*....|....*....|....
gi 1369061829 271 YIALAQRMLDNVVPLEAESLKDRE 294
Cdd:PRK13231  231 YRKLANNIMNNTEFSTPEPMDDEE 254
nifH PRK13233
nitrogenase iron protein;
39-284 7.39e-49

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 163.84  E-value: 7.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKL-GKRVLQIGCDPKHDST-FTLTKKMVPTVIDILEtvDFHTEELRPEDFVFEGYNG 116
Cdd:PRK13233    5 IAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTrLILGGKPQTTMMDTLR--ELGEEKVTPDKVIKTGFKD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLL-EDTDVVIFDVLGDVVCGGFAAPLQ--HANYCLIVTANDFDSIFAMN 193
Cdd:PRK13233   83 IRCVESGGPEPGVGCAGRGVITAIDLMEENGAYtDDLDFVFFDVLGDVVCGGFAMPIRdgKAQEVYIVASGEMMAIYAAN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 194 RIIAAIQAKAKNYKVRLGGVVANrSKDTDQ----IDKFNERVGMRtMAHF-PDLDAIRRSRLKKCTIFEMEatPEVEAVQ 268
Cdd:PRK13233  163 NICKGLVKYAEQSGVRLGGIICN-SRNVDGelelLEEFTDAIGTQ-MIHFvPRDNIVQKAEFNKKTVVEFD--PDCNQAK 238

                         250
                  ....*....|....*....
gi 1369061829 269 kEYIALAQRMLDN---VVP 284
Cdd:PRK13233  239 -EYKELARKIIENkdfVIP 256
BchX TIGR02016
chlorophyllide reductase iron protein subunit X; This model represents the X subunit of the ...
 38-300 2.71e-47

chlorophyllide reductase iron protein subunit X; This model represents the X subunit of the three-subunit enzyme, (bacterio)chlorophyllide reductase. This enzyme is responsible for the reduction of the chlorin B-ring and is closely related to the protochlorophyllide reductase complex which reduces the D-ring. Both of these complexes in turn are homologous to nitrogenase. This subunit is homologous to the nitrogenase component II, or "iron" protein. [Energy metabolism, Photosynthesis]


Pssm-ID: 273929 [Multi-domain]  Cd Length: 296  Bit Score: 160.41  E-value: 2.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTL-TKKMVPTVIDILETVDFHTEELRPEDFVFE---- 112
Cdd:TIGR02016   2 IIAIYGKGGSGKSFTTTNLSHMMAEMGKRVLQLGCDPKHDSTSLLfGGISLPTIIEVATEKKLAGEEVKVGDVCFKttim 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 113 -GYNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLE-DTDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDS 188
Cdd:TIGR02016  82 nGSGGVYGMELGGPEVGRGCGGRGIIHGFDLLEKLGFHDwDFDFVLMDFLGDVVCGGFATPLARslAEEVIVIGSNDRQS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 189 IFAMNRIIAAIQAKAK-NYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRSRLKKcTIFEMEATPEVEAV 267
Cdd:TIGR02016 162 LYVANNICNAVEYFRKlGGRVGLLGLVVNRDDGSGEAQAFAREVGIPVLAAIPADEELRRKSLAY-QIVGSHATPRFGKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1369061829 268 QKEYIA-LAQRMLDNVVPL-------EAESLKDREIFDLLG 300
Cdd:TIGR02016 241 FEELAGnVADAPPLRPRPLspdallaLFETLPETRVVDLVG 281
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 38-265 2.91e-37

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: 134.96  E-value: 2.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTL-TKKMVPTVIDILETVDFHTEELRPEDFVFEgYNG 116
Cdd:cd02033    33 IIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLfGGKACPTIIETSTRKKLAGEEVKIGDVCFK-RGG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 117 VMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLE-DTDVVIFDVLGDVVCGGFAAPLQH--ANYCLIVTANDFDSIFAMN 193
Cdd:cd02033   112 VFAMELGGPEVGRGCGGRGIIHGFELLEKLGFHDwGFDYVLLDFLGDVVCGGFGLPIARdmCQKVIVVGSNDLQSLYVAN 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1369061829 194 RIIAAIQAKAK-NYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRsrlkKCTIFEMEATPEVE 265
Cdd:cd02033   192 NVCSAVEYFRKlGGNVGVAGIVINKDDGTGEAQAFAKAAGIPVLAAIPADEDIRR----KSANYQIVGRPETQ 260
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 36-280 2.63e-17

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: 79.52  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  36 ALVIAVY-GKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTL---TKKMVPTVIDILetvdfhTEELRPEDFVF 111
Cdd:COG1192     1 MKVIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLgldPDDLDPTLYDLL------LDDAPLEDAIV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 112 E-GYNGVMCVesggpPAGTGCGGY-----VTGQTVKLLKE--HHLLEDTDVVIFDV---LGDVVCGGFAAplqhANYCLI 180
Cdd:COG1192    75 PtEIPGLDLI-----PANIDLAGAeielvSRPGRELRLKRalAPLADDYDYILIDCppsLGLLTLNALAA----ADSVLI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 181 VTANDFDSIFAMNRIIAAIQA--KAKNYKVRLGGVVAN----RSKDTDQI-DKFNERVGMRTMAHF-PDLDAIRRSRLKK 252
Cdd:COG1192   146 PVQPEYLSLEGLAQLLETIEEvrEDLNPKLEILGILLTmvdpRTRLSREVlEELREEFGDKVLDTViPRSVALAEAPSAG 225

                         250       260
                  ....*....|....*....|....*...
gi 1369061829 253 CTIFEMEatPEVEAVQkEYIALAQRMLD 280
Cdd:COG1192   226 KPVFEYD--PKSKGAK-AYRALAEELLE 250
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 38-248 1.22e-15

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: 74.30  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPkhDSTFTLTKKMVPTVIDILET---VDFHTEELRPEDFVFEGY 114
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDP--QSNNSSVEGLEGDIAPALQAlaeGLKGRVNLDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 115 NGVMCVESGGPPAGTGCGGYVTGQTVKLLKE--HHLLEDTDVVIFD---------VLGDVVCGGFAAPLQhANYCLIVTA 183
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGPRKEERLREalEALKEDYDYVIIDgapglgellRNALIAADYVIIPLE-PEVILVEDA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1369061829 184 NDfdsifaMNRIIAAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNERVgMRTMAHFPDLDAIRRS 248
Cdd:pfam01656 158 KR------LGGVIAALVGGYALLGLKIIGVVLNKVDGDNHGKLLKEAL-EELLRGLPVLGVIPRD 215
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 38-80 8.79e-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: 8.79e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1369061829  38 VIAVYG-KGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTF 80
Cdd:pfam13614   3 VIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATS 46
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 38-82 4.25e-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: 56.78  E-value: 4.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1369061829  38 VIAVYG-KGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTL 82
Cdd:cd02042     2 VIAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 51-284 5.30e-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: 58.36  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  51 TTSSNLSAAFSKLGKRVL-------------QIGCDPKHdstftltkkmvpTVIDILEtvdfhtEELRPEDFVFEGYNGV 117
Cdd:COG0455     1 TVAVNLAAALARLGKRVLlvdadlglanldvLLGLEPKA------------TLADVLA------GEADLEDAIVQGPGGL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 118 MCVesggpPAGTGCGGYVT-GQTVKLLKEHHLLEDT-DVVIFDV---LGDVVcggfAAPLQHANYCLIVTANDFDSIFAM 192
Cdd:COG0455    63 DVL-----PGGSGPAELAElDPEERLIRVLEELERFyDVVLVDTgagISDSV----LLFLAAADEVVVVTTPEPTSITDA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 193 NRIIAAIqakAKNYKVRLGGVVANRSKDT-------DQIDKFNER---VGMRTMAHFPDLDAIRRSRLKKCTIFEMEATP 262
Cdd:COG0455   134 YALLKLL---RRRLGVRRAGVVVNRVRSEaeardvfERLEQVAERflgVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDS 210

                         250       260
                  ....*....|....*....|..
gi 1369061829 263 eveAVQKEYIALAQRMLDNVVP 284
Cdd:COG0455   211 ---PAARAIRELAARLAGWPVP 229
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 39-269 8.41e-10

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 57.87  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPkhDST------FTLTKKMVPTVIDILETVDFHTEELRPE----- 107
Cdd:COG3640     3 IAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADP--NANlaealgLEVEADLIKPLGEMRELIKERTGAPGGGmfkln 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 108 ---DFVFEGYngvmCVESG-------GPP--AGTGCGGYVtGQTVKLLKEHHLLEDTDVVIFD------VLGDVVCGGFa 169
Cdd:COG3640    81 pkvDDIPEEY----LVEGDgvdllvmGTIeeGGSGCYCPE-NALLRALLNHLVLGNYEYVVVDmeagieHLGRGTAEGV- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 170 aplqhaNYCLIVTANDFDSIFAMNRIiaaiqAK-AKNYKVRLGGVVANRSKDTDQIDKFNERVGMRTMAHFPDLDAIRRS 248
Cdd:COG3640   155 ------DLLLVVSEPSRRSIETARRI-----KElAEELGIKKIYLVGNKVREEEDEEFLRELLGLELLGFIPYDEEVREA 223

                         250       260
                  ....*....|....*....|.
gi 1369061829 249 RLKKCTIFEMEATPEVEAVQK 269
Cdd:COG3640   224 DLEGKPLLDLPDSPAVAAVEE 244
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 36-217 2.14e-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: 57.12  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  36 ALVIAVY-GKGGIGKSTTSSNLSAAFSKLGKRVLQIGCD---PKHDSTFTLTKKmvPTVIDILETVDFHTEELRPedfvF 111
Cdd:COG0489    92 LEVIAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgPSLHRMLGLENR--PGLSDVLAGEASLEDVIQP----T 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829 112 EGYN-GVMcveSGGPPAGTGCGGYVTGQTVKLLKEhhLLEDTDVVIFD---VLGDVVcggfAAPLQ-HANYCLIVTANDF 186
Cdd:COG0489   166 EVEGlDVL---PAGPLPPNPSELLASKRLKQLLEE--LRGRYDYVIIDtppGLGVAD----ATLLAsLVDGVLLVVRPGK 236

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1369061829 187 DSIFAMNRIIAAIqakaKNYKVRLGGVVANR 217
Cdd:COG0489   237 TALDDVRKALEML----EKAGVPVLGVVLNM 263
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 38-67 8.33e-08

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: 51.73  E-value: 8.33e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1369061829  38 VIAVY-GKGGIGKSTTSSNLSAAFSKLGKRV 67
Cdd:cd02037     2 IIAVLsGKGGVGKSTVAVNLALALAKKGYKV 32
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 38-67 9.87e-08

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: 52.07  E-value: 9.87e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1369061829  38 VIAVY-GKGGIGKSTTSSNLSAAFSKLGKRV 67
Cdd:pfam10609   5 VIAVAsGKGGVGKSTVAVNLALALARLGYKV 35
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 38-158 2.38e-07

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: 50.65  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVY-GKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDpkhdstftltkkMVPTVIDILETV-------DFHTEELRPEDF 109
Cdd:cd02038     2 IIAVTsGKGGVGKTNVSANLALALSKLGKRVLLLDAD------------LGLANLDILLGLapkktlgDVLKGRVSLEDI 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1369061829 110 VFEGYNGVMCVesggpPAGTGCGGYV---TGQTVKLLKE-HHLLEDTDVVIFD 158
Cdd:cd02038    70 IVEGPEGLDII-----PGGSGMEELAnldPEQKAKLIEElSSLESNYDYLLID 117
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 38-158 4.29e-07

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: 50.43  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKH---DStFTLTKKMVPTVID----ILEtVDFHTEELRPEDFV 110
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHslsDS-FNQKFGHEPTKVKenlsAME-IDPNMELEEYWQEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1369061829 111 FEGYN---------GVMCVESGGPPAGTGCGGYVtgQTVKLLKEhhllEDTDVVIFD 158
Cdd:pfam02374  81 QKYMNallglrmleGILAEELASLPGIDEAASFD--EFKKYMDE----GEYDVVVFD 131
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 43-73 2.22e-06

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: 47.97  E-value: 2.22e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1369061829  43 GKGGIGKSTTSSNLSAAFSKLGKRVLQIGCD 73
Cdd:cd02036     8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 38-241 5.17e-06

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: 47.42  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  38 VIAVYG-KGGIGKSTTSSNLSAAFSKL-GKRV------LQIGC-------DPKH------------DSTF---TLTKkmV 87
Cdd:COG4963   104 VIAVVGaKGGVGATTLAVNLAWALAREsGRRVllvdldLQFGDvalyldlEPRRgladalrnpdrlDETLldrALTR--H 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  88 PTVIDIL--ETVDFHTEELRPEDFvfegyngvmcvesggppagtgcggyvtGQTVKLLKEHHlledtDVVIFDvLGDVVC 165
Cdd:COG4963   182 SSGLSVLaaPADLERAEEVSPEAV---------------------------ERLLDLLRRHF-----DYVVVD-LPRGLN 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1369061829 166 GGFAAPLQHANYCLIVTANDFDSIFAMNRIIAAIQAKAKNY-KVRLggvVANR-SKDTD-QIDKFNERVGMRTMAHFPD 241
Cdd:COG4963   229 PWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDdKVRL---VLNRvPKRGEiSAKDIEEALGLPVAAVLPN 304
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 39-158 8.08e-06

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: 46.15  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369061829  39 IAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPkhDSTFTLTKKMVPTVIDILETVDFHTEEL-------------- 104
Cdd:cd02034     3 IAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADP--NSNLAETLGVEVEKLPLIKTIGDIRERTgakkgeppegmsln 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1369061829 105 -----RPEDFVFEGYNGVMCVESGGPPAGTGCGGYVTGQTVKLLKeHHLLEDTDVVIFD 158
Cdd:cd02034    81 pyvddIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLR-HLALKNYEYVVID 138
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 38-73 2.93e-05

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: 42.42  E-value: 2.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1369061829  38 VIAVYG-KGGIGKSTTSSNLSAAFSKLGKRVLQIGCD 73
Cdd:cd01983     2 VIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
minD CHL00175
septum-site determining protein; Validated
 43-95 4.67e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 43.99  E-value: 4.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1369061829  43 GKGGIGKSTTSSNLSAAFSKLGKRVLQIGCD---PKHDSTFTLTKKMVPTVIDILE 95
Cdd:CHL00175   23 GKGGVGKTTTTANLGMSIARLGYRVALIDADiglRNLDLLLGLENRVLYTAMDVLE 78
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 43-76 5.59e-05

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: 43.65  E-value: 5.59e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1369061829  43 GKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKH 76
Cdd:cd02035     7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAH 40
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 38-75 7.83e-05

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: 43.10  E-value: 7.83e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1369061829  38 VIAVYG-KGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPK 75
Cdd:TIGR03371   3 VIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 46-94 1.64e-04

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


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 41.79  E-value: 1.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1369061829  46 GIGKSTTSSNLSAAFSKLGKRVLQIGCD---PKHDSTFTLTKKmvPTVIDIL 94
Cdd:cd05387    30 GEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGLPNE--PGLSEVL 79
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
38-76 3.30e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.73  E-value: 3.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1369061829  38 VIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKH 76
Cdd:COG0003     5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAH 43
PHA02518 PHA02518
ParA-like protein; Provisional
 38-79 5.24e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.60  E-value: 5.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1369061829  38 VIAVYG-KGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDST 79
Cdd:PHA02518    2 IIAVLNqKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST 44
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
38-67 2.10e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 39.26  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1369061829  38 VIAVY-GKGGIGKSTTSSNLSAAFSKLGKRV 67
Cdd:PRK11670  109 IIAVSsGKGGVGKSSTAVNLALALAAEGAKV 139
 
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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