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Conserved domains on  [gi|502999844|ref|WP_013234820|]
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MULTISPECIES: nitrogenase iron protein [Herbaspirillum]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 3-280 0e+00

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


:

Pssm-ID: 440959  Cd Length: 276  Bit Score: 517.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   3 SLRQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsvEDLELEDVMKIGY 82
Cdd:COG1348    1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  83 QNIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYA 161
Cdd:COG1348   79 GGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 162 ANNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEY 241
Cdd:COG1348  159 ANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEY 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 502999844 242 RTLANKIHENaGNGTIPTPITMDELEDLLMQHGLMPVVD 280
Cdd:COG1348  239 RELAKKILEN-KKLVIPKPLSDEELEELLLEYGILEKED 276
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 3-280 0e+00

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


Pssm-ID: 440959  Cd Length: 276  Bit Score: 517.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   3 SLRQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsvEDLELEDVMKIGY 82
Cdd:COG1348    1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  83 QNIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYA 161
Cdd:COG1348   79 GGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 162 ANNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEY 241
Cdd:COG1348  159 ANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEY 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 502999844 242 RTLANKIHENaGNGTIPTPITMDELEDLLMQHGLMPVVD 280
Cdd:COG1348  239 RELAKKILEN-KKLVIPKPLSDEELEELLLEYGILEKED 276
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 5-280 0e+00

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


Pssm-ID: 273538  Cd Length: 275  Bit Score: 505.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844    5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSvEDLELEDVMKIGYQN 84
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:TIGR01287  80 IRCVESGGPEPGVGCAGRGVITAINLLEELGAYeDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  164 NISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:TIGR01287 160 NICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 502999844  244 LANKIHENaGNGTIPTPITMDELEDLLMQHGLMPVVD 280
Cdd:TIGR01287 240 LAKKIYEN-TEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 5-271 1.17e-171

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: 475.08  E-value: 1.17e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsvEDLELEDVMKIGYQN 84
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:cd02040   79 IKCVESGGPEPGVGCAGRGIITAINLLEELGAYEeDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAAN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 164 NISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:cd02040  159 NIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRE 238

                        250       260
                 ....*....|....*....|....*...
gi 502999844 244 LANKIHENAgNGTIPTPITMDELEDLLM 271
Cdd:cd02040  239 LAKKILENK-KLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
5-276 1.14e-163

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 455.36  E-value: 1.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844    5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVMKIGYQN 84
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAYDDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANN 164
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAANN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  165 ISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRTL 244
Cdd:pfam00142 161 IAKGIQKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYREL 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 502999844  245 ANKIHENAgNGTIPTPITMDELEDLLMQHGLM 276
Cdd:pfam00142 241 ARKILENP-KGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
5-276 5.72e-141

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 398.04  E-value: 5.72e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQM-GQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSvEDLELEDVMKIGYQ 83
Cdd:PRK13233   3 RKIAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKTGFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  84 NIRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAA 162
Cdd:PRK13233  82 DIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYtDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 163 NNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYR 242
Cdd:PRK13233 162 NNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYK 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 502999844 243 TLANKIHENAgNGTIPTPITMDELEDLLMQHGLM 276
Cdd:PRK13233 242 ELARKIIENK-DFVIPKPLTMDELEEMVVKYGLM 274
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 5-269 2.31e-132

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: 375.75  E-value: 2.31e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsveDLELEDVMKIGYQN 84
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:NF033200  78 VRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFmEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 164 NISKGILKYANsggvRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:NF033200 158 NICKGIKKLKG----RLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRK 233

                        250       260
                 ....*....|....*....|....*.
gi 502999844 244 LANKIHENaGNGTIPTPITMDELEDL 269
Cdd:NF033200 234 LAKKIMEN-TDFVIPEPLEDEELEEL 258
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 5-44 3.81e-04

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 41.79  E-value: 3.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKA 44
Cdd:NF041417 334 RYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPAS 373
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 7-42 2.26e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.48  E-value: 2.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:NF041417  15 VFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDP 50
 
Name Accession Description Interval E-value
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 3-280 0e+00

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


Pssm-ID: 440959  Cd Length: 276  Bit Score: 517.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   3 SLRQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsvEDLELEDVMKIGY 82
Cdd:COG1348    1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKG--EDVELEDIVFEGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  83 QNIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYA 161
Cdd:COG1348   79 GGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEeDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 162 ANNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEY 241
Cdd:COG1348  159 ANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEY 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 502999844 242 RTLANKIHENaGNGTIPTPITMDELEDLLMQHGLMPVVD 280
Cdd:COG1348  239 RELAKKILEN-KKLVIPKPLSDEELEELLLEYGILEKED 276
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 5-280 0e+00

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


Pssm-ID: 273538  Cd Length: 275  Bit Score: 505.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844    5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSvEDLELEDVMKIGYQN 84
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGA-EDLELEDVIKEGFGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:TIGR01287  80 IRCVESGGPEPGVGCAGRGVITAINLLEELGAYeDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  164 NISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:TIGR01287 160 NICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYRE 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 502999844  244 LANKIHENaGNGTIPTPITMDELEDLLMQHGLMPVVD 280
Cdd:TIGR01287 240 LAKKIYEN-TEFVIPTPLTMDELEEILMKFGIMLKED 275
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 5-271 1.17e-171

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: 475.08  E-value: 1.17e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsvEDLELEDVMKIGYQN 84
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKG--EVEELEDVIKEGFNG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:cd02040   79 IKCVESGGPEPGVGCAGRGIITAINLLEELGAYEeDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAAN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 164 NISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:cd02040  159 NIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRE 238

                        250       260
                 ....*....|....*....|....*...
gi 502999844 244 LANKIHENAgNGTIPTPITMDELEDLLM 271
Cdd:cd02040  239 LAKKILENK-KLVIPKPLTMEELEELLM 265
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
5-276 1.14e-163

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 455.36  E-value: 1.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844    5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVMKIGYQN 84
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAYDDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANN 164
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAANN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  165 ISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRTL 244
Cdd:pfam00142 161 IAKGIQKYAKSGGVRLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYREL 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 502999844  245 ANKIHENAgNGTIPTPITMDELEDLLMQHGLM 276
Cdd:pfam00142 241 ARKILENP-KGTIPTPLSMDELEALLEDFGLM 271
nifH PRK13233
nitrogenase iron protein;
5-276 5.72e-141

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 398.04  E-value: 5.72e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQM-GQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSvEDLELEDVMKIGYQ 83
Cdd:PRK13233   3 RKIAIYGKGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGE-EKVTPDKVIKTGFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  84 NIRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAA 162
Cdd:PRK13233  82 DIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYtDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 163 NNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYR 242
Cdd:PRK13233 162 NNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYK 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 502999844 243 TLANKIHENAgNGTIPTPITMDELEDLLMQHGLM 276
Cdd:PRK13233 242 ELARKIIENK-DFVIPKPLTMDELEEMVVKYGLM 274
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 5-269 2.31e-132

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: 375.75  E-value: 2.31e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGsveDLELEDVMKIGYQN 84
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENK---NIKEEDVVFEGYGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:NF033200  78 VRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFmEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 164 NISKGILKYANsggvRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:NF033200 158 NICKGIKKLKG----RLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRK 233

                        250       260
                 ....*....|....*....|....*.
gi 502999844 244 LANKIHENaGNGTIPTPITMDELEDL 269
Cdd:NF033200 234 LAKKIMEN-TDFVIPEPLEDEELEEL 258
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 5-271 2.54e-119

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: 342.81  E-value: 2.54e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVMKIGYQN 84
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDLLFSGFNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  85 IRCVESGGPEPGVGCAGRGVITSINFLEEEGAY-DDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAAN 163
Cdd:cd02117   81 VDCVEAGGPEPGVGCGGRGIGTMLELLEEHGLLdDDYDVVIFDVLGDVVCGGFAAPLRRGFAQKVVIVVSEELMSLYAAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 164 NISKGILKYANsGGVRLGGLICNERKTDkELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRT 243
Cdd:cd02117  161 NIVKAVENYSK-NGVRLAGLVANLRDPA-GTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFAR 238

                        250       260
                 ....*....|....*....|....*...
gi 502999844 244 LANKIHENAGNGTIPTPITMDELEDLLM 271
Cdd:cd02117  239 LAAKIADAVPPVPGPRPLSDRELFALLG 266
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 4-269 2.12e-103

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 302.85  E-value: 2.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   4 LRQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAqDTILSLAADAGsVEDLELEDVMKIGYQ 83
Cdd:PRK13230   1 MRKFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKI-PTVLDVLREKG-IDNLGLEDIIYEGFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  84 NIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYDD--TDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYA 161
Cdd:PRK13230  79 GIYCVESGGPEPGYGCAGRGVITAIDLLKKLGVFEElgPDVVIYDILGDVVCGGFAMPLQKGLADDVYIVTTCDPMAIYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 162 ANNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEY 241
Cdd:PRK13230 159 ANNICKGIKRFAKRGKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPDSEISNIF 238

                        250       260
                 ....*....|....*....|....*...
gi 502999844 242 RTLANKIHENAgNGTIPTPITMDELEDL 269
Cdd:PRK13230 239 RELAEAIYENN-TGTIPNPLEEEEIDQI 265
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 4-268 2.15e-92

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 274.37  E-value: 2.15e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   4 LRQIAFYGKGGIGKSTTSQNTLAALAQmGQRILIVGCDPKADSTRlILHAKAQDTILSLAADAgsvEDLELEDVMKIGYQ 83
Cdd:PRK13231   2 MKKIAIYGKGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTR-TLCGKRIPTVLDTLKDN---RKPELEDIIHEGFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  84 NIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAA 162
Cdd:PRK13231  77 GILCVESGGPEPGVGCAGRGVIVAMNLLENLGVFDeDIDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 163 NNISKGILKYANsggvRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYR 242
Cdd:PRK13231 157 NNIARGIKKLKG----KLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYR 232

                        250       260
                 ....*....|....*....|....*.
gi 502999844 243 TLANKIHENAgNGTIPTPITMDELED 268
Cdd:PRK13231 233 KLANNIMNNT-EFSTPEPMDDEEFEE 257
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 7-270 1.39e-60

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 193.64  E-value: 1.39e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTrLILHAKAQDTIL-SLAADAGSVEDLELEDVMKIGYQNI 85
Cdd:PRK13185   5 LAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST-FTLTGKLVPTVIdILEEVDFHSEELRPEDFVYEGYNGV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  86 RCVESGGPEPGVGCAGRGVITSINFLEEEGAYDDTDYVSYDVLGDVVCGGFAMPIreNKAQEIYIVMSGEMMAMYAANNI 165
Cdd:PRK13185  84 DCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPL--QYADYALIVTANDFDSIFAANRI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 166 SKGILKYANSGGVRLGGLICNE-RKTDkELElatALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYA--PDSKQA--GE 240
Cdd:PRK13185 162 AAAIQAKAKNYKVRLAGVIANRsAGTD-LID---KFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEetDPGLEEvqNE 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 502999844 241 YRTLANKIHENAgNGTIPTPITMDELEDLL 270
Cdd:PRK13185 238 YLRLAEQLLAGP-EPLVPKPLKDREIFELL 266
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 7-270 2.41e-60

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: 192.90  E-value: 2.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVMKIGYQNIR 86
Cdd:cd02032    3 IAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  87 CVESGGPEPGVGCAGRGVITSINFLEEEGAYDDTDYVSYDVLGDVVCGGFAMPIreNKAQEIYIVMSGEMMAMYAANNIS 166
Cdd:cd02032   83 CVEAGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPL--NYADYCLIVTANDFDSLFAANRIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 167 KGILKYANSGGVRLGGLICNE-RKTDkeleLATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAG----EY 241
Cdd:cd02032  161 AAVREKAKTYPVRLAGIIGNRtDKTD----LIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPELNyvcdEY 236

                        250       260
                 ....*....|....*....|....*....
gi 502999844 242 RTLANKIHENAgNGTIPTPITMDELEDLL 270
Cdd:cd02032  237 LNIADQLLSDP-EGVVPKPLPDREIFDLL 264
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 7-290 1.32e-46

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


Pssm-ID: 349753  Cd Length: 329  Bit Score: 159.23  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAAD---AGsvEDLELEDV-MKIGy 82
Cdd:cd02033   34 IAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFGGKACPTIIETSTRkklAG--EEVKIGDVcFKRG- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  83 qNIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYD-DTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYA 161
Cdd:cd02033  111 -GVFAMELGGPEVGRGCGGRGIIHGFELLEKLGFHDwGFDYVLLDFLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSLYV 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 162 ANNISKGILKYANSGG-VRLGGLICNerKTDKELElATALAAKLNSKLIHFVPrdnivQHAELRRMTVlEYAPDSKQAGE 240
Cdd:cd02033  190 ANNVCSAVEYFRKLGGnVGVAGIVIN--KDDGTGE-AQAFAKAAGIPVLAAIP-----ADEDIRRKSA-NYQIVGRPETQ 260

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502999844 241 YRTLANKIHENAGNGTI--PTPITMDEL------EDLLMQHGLMPVVDESMVGKSAEV 290
Cdd:cd02033  261 WGPLFAELATNVAEAPPmrPTPLSQDELlglfssEETGRDVVLVPATDEDMRGKDAVP 318
chlL CHL00072
photochlorophyllide reductase subunit L
 6-233 7.35e-46

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 156.05  E-value: 7.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   6 QIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVMKIGYQNI 85
Cdd:CHL00072   2 KLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  86 RCVESGGPEPGVGCAGRGVITSINFLEEEGAYDDTDYVSYDVLGDVVCGGFAMPIreNKAQEIYIVMSGEMMAMYAANNI 165
Cdd:CHL00072  82 DCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAANRI 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502999844 166 SKGILKYANSGGVRLGGLICNerKTDKelelatalaaklnsklihfvpRDNIVQHAELRRMTVLEYAP 233
Cdd:CHL00072 160 AASVREKARTHPLRLAGLVGN--RTSK---------------------RDLIDKYVEACPMPVLEVLP 204
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 7-250 1.88e-14

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: 71.43  E-value: 1.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   7 IAFY-GKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRL--ILHAKAQDTILSLAADAGSVEDLeledVMKIGYQ 83
Cdd:COG1192    4 IAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGlgLDPDDLDPTLYDLLLDDAPLEDA----IVPTEIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  84 NIRCVESGGPEPGVGCAGRGVITSINFLEE--EGAYDDTDYV------SYDVLGD--VVCggfampirenkAQEIYIVMS 153
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRalAPLADDYDYIlidcppSLGLLTLnaLAA-----------ADSVLIPVQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 154 GEMMAMYAANNIS---KGILKYANSgGVRLGGLICN--ERKTDKELELATALAAKLNSKLI-HFVPRDNIVQHAELRRMT 227
Cdd:COG1192  149 PEYLSLEGLAQLLetiEEVREDLNP-KLEILGILLTmvDPRTRLSREVLEELREEFGDKVLdTVIPRSVALAEAPSAGKP 227

                        250       260
                 ....*....|....*....|...
gi 502999844 228 VLEYAPDSKQAGEYRTLANKIHE 250
Cdd:COG1192  228 VFEYDPKSKGAKAYRALAEELLE 250
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 7-50 1.29e-08

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: 52.54  E-value: 1.29e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 502999844   7 IAFYG-KGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLI 50
Cdd:cd02042    3 IAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 7-85 1.56e-08

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: 53.36  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844    7 IAFYG-KGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTR--LILHAKAQDTILSLAADAGSVEDLeledVMKIGYQ 83
Cdd:pfam13614   4 IAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSglGIDKNNVEKTIYELLIGECNIEEA----IIKTVIE 79


                  ..
gi 502999844   84 NI 85
Cdd:pfam13614  80 NL 81
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 26-248 3.00e-07

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: 50.27  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  26 AALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADagsveDLELEDVMKIGYQNIRCVesggpePGvgcaGRGVI 105
Cdd:COG0455    8 AALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAG-----EADLEDAIVQGPGGLDVL------PG----GSGPA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 106 TSINFLEEEGAYDDTDYVS--YDV--------LGDVVCGGFAMpirenkAQEIYIVMSGEMMAMYAAnnisKGILKYANS 175
Cdd:COG0455   73 ELAELDPEERLIRVLEELErfYDVvlvdtgagISDSVLLFLAA------ADEVVVVTTPEPTSITDA----YALLKLLRR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 176 -GGVRLGGLICN-------ERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRTLANK 247
Cdd:COG0455  143 rLGVRRAGVVVNrvrseaeARDVFERLEQVAERFLGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAAR 222


                 .
gi 502999844 248 I 248
Cdd:COG0455  223 L 223
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 5-41 1.94e-06

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: 45.50  E-value: 1.94e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502999844   5 RQIAFYG-KGGIGKSTTSQNTLAALAQMGQRILIVGCD 41
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 4-42 1.93e-05

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: 45.42  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 502999844    4 LRQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDP 39
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 11-95 3.33e-05

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: 44.41  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCDpkadstrliLHAKAQDTILSLAADAGSVEDL----ELEDVMK-IGYQNI 85
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDAD---------LRGPSLHRMLGLENRPGLSDVLageaSLEDVIQpTEVEGL 170

                         90
                 ....*....|
gi 502999844  86 RCVESGGPEP 95
Cdd:COG0489  171 DVLPAGPLPP 180
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-42 5.44e-05

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: 44.31  E-value: 5.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 502999844    9 FYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:TIGR04291   8 FTGKGGVGKTSIACATAINLADQGKRVLLVSTDP 41
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 11-228 7.77e-05

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 43.10  E-value: 7.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADaGSVEDLELEDV-MKIGYQNIR-CV 88
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAE-GLKGRVNLDPIlLKEKSDEGGlDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844   89 ESGGPEPGVGCAGRGVITSINFLEE--EGAYDDTDYV--------SYDVLGDVVCG-GFAMPIRenkaQEIYIVMSGEMM 157
Cdd:pfam01656  85 IPGNIDLEKFEKELLGPRKEERLREalEALKEDYDYViidgapglGELLRNALIAAdYVIIPLE----PEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502999844  158 AMYAANniskgILKYANSGGVRLGGLICN-ERKTDKELELATALAA-KLNSKLIHFVPRDNIVQHAELRRMTV 228
Cdd:pfam01656 161 GGVIAA-----LVGGYALLGLKIIGVVLNkVDGDNHGKLLKEALEElLRGLPVLGVIPRDEAVAEAPARGLPV 228
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 6-42 9.28e-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: 42.88  E-value: 9.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502999844   6 QIAFY-GKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:cd02035    1 RIIFFgGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 11-236 1.01e-04

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: 42.56  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADagsveDLELEDVMKIGYQNIRCVeS 90
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKG-----RVSLEDIIVEGPEGLDII-P 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844  91 GGpepgvgcAGRGVITSIN------FLEEEGAYD-DTDYVSYDV---LGDVVCGGFAMpirenkAQEIYIVMSGE---MM 157
Cdd:cd02038   82 GG-------SGMEELANLDpeqkakLIEELSSLEsNYDYLLIDTgagISRNVLDFLLA------ADEVIVVTTPEptsIT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502999844 158 AMYAanniskgILKYAN-SGGVRLGGLICNERKTDKE-LELATALAA------KLNSKLIHFVPRDNIVQHAELRRMTVL 229
Cdd:cd02038  149 DAYA-------LIKVLSrRGGKKNFRLIVNMARSPKEgRATFERLKKvakrflDINLDFVGFIPYDQSVRRAVRSQKPFV 221


                 ....*..
gi 502999844 230 EYAPDSK 236
Cdd:cd02038  222 LLFPNSK 228
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 11-41 1.40e-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: 42.19  E-value: 1.40e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 502999844  11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCD 41
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 11-41 2.25e-04

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: 41.33  E-value: 2.25e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 502999844  11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCD 41
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 5-44 3.81e-04

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 41.79  E-value: 3.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 502999844   5 RQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKA 44
Cdd:NF041417 334 RYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPAS 373
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
7-42 7.24e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 40.57  E-value: 7.24e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:COG0003    6 IFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDP 41
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 11-39 9.98e-04

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: 39.74  E-value: 9.98e-04
                          10        20
                  ....*....|....*....|....*....
gi 502999844   11 GKGGIGKSTTSQNTLAALAQMGQRiliVG 39
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYK---VG 36
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 14-41 1.05e-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: 39.09  E-value: 1.05e-03
                         10        20
                 ....*....|....*....|....*...
gi 502999844  14 GIGKSTTSQNTLAALAQMGQRILIVGCD 41
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDAD 57
PHA02518 PHA02518
ParA-like protein; Provisional
 12-47 1.12e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 39.45  E-value: 1.12e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502999844  12 KGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADST 47
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST 44
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 5-78 1.35e-03

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


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 39.71  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502999844   5 RQIAFYG-KGGIGKSTTSQNTLAALAQM-GQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVM 78
Cdd:COG4963  103 RVIAVVGaKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRAL 178
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 7-44 1.87e-03

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: 38.83  E-value: 1.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKA 44
Cdd:cd02034    3 IAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS 40
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 7-42 2.26e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.48  E-value: 2.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:NF041417  15 VFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDP 50
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 7-42 2.52e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 38.61  E-value: 2.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502999844   7 IAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDP 42
Cdd:COG3640    3 IAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
11-41 2.90e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 38.87  E-value: 2.90e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 502999844  11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCD 41
Cdd:PRK11670 115 GKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
minD CHL00175
septum-site determining protein; Validated
 11-41 3.93e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 38.21  E-value: 3.93e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 502999844  11 GKGGIGKSTTSQNTLAALAQMGQRILIVGCD 41
Cdd:CHL00175  23 GKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
 
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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