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Conserved domains on  [gi|649131939|ref|YP_009033653|]
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ATP-binding subunit of protochlorophyllide reductase (chloroplast) [Klebsormidium flaccidum]

Protein Classification

ferredoxin:protochlorophyllide reductase (ATP-dependent) iron-sulfur ATP-binding protein( domain architecture ID 10784682)

ferredoxin:protochlorophyllide reductase (ATP-dependent) iron-sulfur ATP-binding protein is a 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 CHL00072
photochlorophyllide reductase subunit L
 1-289 0e+00

photochlorophyllide reductase subunit L


:

Pssm-ID: 177011  Cd Length: 290  Bit Score: 617.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:CHL00072   1 MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:CHL00072  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:CHL00072 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMVESEPSLNYVCDYYLNIA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 649131939 241 DQILARPEGVVPKEVPDRELFSLLSDFYLNPTNQ-KAEQVPGEHLDFMMV 289
Cdd:CHL00072 241 DQLLSQPEGVVPKEVPDRELFSLLSDFYLNPIGNeGQKNDQENLLDFTIV 290
 
Name Accession Description Interval E-value
chlL CHL00072
photochlorophyllide reductase subunit L
 1-289 0e+00

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 617.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:CHL00072   1 MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:CHL00072  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:CHL00072 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMVESEPSLNYVCDYYLNIA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 649131939 241 DQILARPEGVVPKEVPDRELFSLLSDFYLNPTNQ-KAEQVPGEHLDFMMV 289
Cdd:CHL00072 241 DQLLSQPEGVVPKEVPDRELFSLLSDFYLNPIGNeGQKNDQENLLDFTIV 290
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-267 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: 538.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:cd02032    1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:cd02032   81 VDCVEAGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTANDFDSLFAANRIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:cd02032  161 AAVREKAKTYPVRLAGIIGNRTDKTDLIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPELNYVCDEYLNIA 240

                        250       260
                 ....*....|....*....|....*..
gi 649131939 241 DQILARPEGVVPKEVPDRELFSLLSDF 267
Cdd:cd02032  241 DQLLSDPEGVVPKPLPDREIFDLLGDF 267
DPOR_bchL TIGR01281
light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; The BchL ...
 1-268 4.53e-167

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: 463.90  E-value: 4.53e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939    1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:TIGR01281   1 MILAVYGKGGIGKSTTSSNLSVAFAKLGKRVLQIGCDPKHDSTFTLTGRLIPTVIDVLQAVNYHYEDVRPEDVIYTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:TIGR01281  81 VDCVEAGGPPAGSGCGGYVVGETVKLLKEHHILDDYDVILFDVLGDVVCGGFATPLQYADYALVVAANDFDALFAANRIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:TIGR01281 161 ASVQEKAKNYDVRLAGIIGNRSDATDLIERFNERVGMPVLGVVPDLEVIRRSRVKGKTLFEMEESGPELAAVTQEYLRMA 240

                         250       260
                  ....*....|....*....|....*...
gi 649131939  241 DQILARPEGVVPKEVPDRELFSLLSDFY 268
Cdd:TIGR01281 241 EYLLAGPEGVVPTPLIDREIFELLGGFD 268
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
1-270 2.95e-132

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 375.63  E-value: 2.95e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939    1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDST-FTLTGFLIPTIIDTLQSKDYHyEDVWPEDVIYQGYG 79
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrLLLGGKLQPTVLDTAREKGYV-EDVEVEDVVYKGYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   80 GVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLN--YADYCIIITDNGFDALFAAN 157
Cdd:pfam00142  80 GVKCVESGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIRegKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  158 RIAASVREKARTHPLRLAGLVGNR---TSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPslsyVCD 234
Cdd:pfam00142 160 NIAKGIQKYAKSGGVRLGGIICNSrkvDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSE----QAQ 235

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 649131939  235 FYLNIADQILARPEGVVPKEVPDRELFSLLSDFYLN 270
Cdd:pfam00142 236 EYRELARKILENPKGTIPTPLSMDELEALLEDFGLM 271
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 1-269 2.49e-91

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: 272.04  E-value: 2.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLT-GFLIPTIIDTLQSKDyhyEDVWPEDVIYQGYG 79
Cdd:COG1348    3 RQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLgGKRIPTVLDTLREKG---EDVELEDIVFEGFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  80 GVDCVEaggppagagcggYVVGETVKLLKELNAFYE-YDVILFDVLGDVVCGGFAAPLN--YADYCIIITDNGFDALFAA 156
Cdd:COG1348   80 GVKCVEaggpepgvgcagRGIITAIELLEELGAYEEdLDVVIYDVLGDVVCGGFAMPIRegYADEIYIVTSGEFMALYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 157 NRIAASVREKARTHPLRLAGLVGNRTSK---RDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPslsyVC 233
Cdd:COG1348  160 NNICKGIKKYANRGGVRLGGIICNSRNVdgeRELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSE----QA 235

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 649131939 234 DFYLNIADQILARPEGVVPKEVPDRELFSLLSDFYL 269
Cdd:COG1348  236 DEYRELAKKILENKKLVIPKPLSDEELEELLLEYGI 271
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 7-38 8.97e-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: 40.63  E-value: 8.97e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 649131939   7 GKGGIGKSTTSCNISIALARRGKRVLQIGCDP 38
Cdd:NF041417  19 GKGGVGKSTVSCATAQWLARNGYDTLLVTTDP 50
 
Name Accession Description Interval E-value
chlL CHL00072
photochlorophyllide reductase subunit L
 1-289 0e+00

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 617.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:CHL00072   1 MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:CHL00072  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:CHL00072 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMVESEPSLNYVCDYYLNIA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 649131939 241 DQILARPEGVVPKEVPDRELFSLLSDFYLNPTNQ-KAEQVPGEHLDFMMV 289
Cdd:CHL00072 241 DQLLSQPEGVVPKEVPDRELFSLLSDFYLNPIGNeGQKNDQENLLDFTIV 290
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-267 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: 538.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:cd02032    1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWPEDVIFTGYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:cd02032   81 VDCVEAGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTANDFDSLFAANRIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:cd02032  161 AAVREKAKTYPVRLAGIIGNRTDKTDLIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPELNYVCDEYLNIA 240

                        250       260
                 ....*....|....*....|....*..
gi 649131939 241 DQILARPEGVVPKEVPDRELFSLLSDF 267
Cdd:cd02032  241 DQLLSDPEGVVPKPLPDREIFDLLGDF 267
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-268 1.96e-179

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 494.87  E-value: 1.96e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILEEVDFHSEELRPEDFVYEGYNG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:PRK13185  83 VDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPLQYADYALIVTANDFDSIFAANRIA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:PRK13185 163 AAIQAKAKNYKVRLAGVIANRSAGTDLIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEETDPGLEEVQNEYLRLA 242

                        250       260
                 ....*....|....*....|....*...
gi 649131939 241 DQILARPEGVVPKEVPDRELFSLLSDFY 268
Cdd:PRK13185 243 EQLLAGPEPLVPKPLKDREIFELLGFDY 270
DPOR_bchL TIGR01281
light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; The BchL ...
 1-268 4.53e-167

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: 463.90  E-value: 4.53e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939    1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:TIGR01281   1 MILAVYGKGGIGKSTTSSNLSVAFAKLGKRVLQIGCDPKHDSTFTLTGRLIPTVIDVLQAVNYHYEDVRPEDVIYTGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   81 VDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIA 160
Cdd:TIGR01281  81 VDCVEAGGPPAGSGCGGYVVGETVKLLKEHHILDDYDVILFDVLGDVVCGGFATPLQYADYALVVAANDFDALFAANRIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  161 ASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYVCDFYLNIA 240
Cdd:TIGR01281 161 ASVQEKAKNYDVRLAGIIGNRSDATDLIERFNERVGMPVLGVVPDLEVIRRSRVKGKTLFEMEESGPELAAVTQEYLRMA 240

                         250       260
                  ....*....|....*....|....*...
gi 649131939  241 DQILARPEGVVPKEVPDRELFSLLSDFY 268
Cdd:TIGR01281 241 EYLLAGPEGVVPTPLIDREIFELLGGFD 268
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
1-270 2.95e-132

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 375.63  E-value: 2.95e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939    1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDST-FTLTGFLIPTIIDTLQSKDYHyEDVWPEDVIYQGYG 79
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrLLLGGKLQPTVLDTAREKGYV-EDVEVEDVVYKGYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   80 GVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLN--YADYCIIITDNGFDALFAAN 157
Cdd:pfam00142  80 GVKCVESGGPEPGVGCAGRGVITAINLLEELGAYDDLDFVLYDVLGDVVCGGFAMPIRegKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  158 RIAASVREKARTHPLRLAGLVGNR---TSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPslsyVCD 234
Cdd:pfam00142 160 NIAKGIQKYAKSGGVRLGGIICNSrkvDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSE----QAQ 235

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 649131939  235 FYLNIADQILARPEGVVPKEVPDRELFSLLSDFYLN 270
Cdd:pfam00142 236 EYRELARKILENPKGTIPTPLSMDELEALLEDFGLM 271
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 1-269 2.49e-91

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: 272.04  E-value: 2.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLT-GFLIPTIIDTLQSKDyhyEDVWPEDVIYQGYG 79
Cdd:COG1348    3 RQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLgGKRIPTVLDTLREKG---EDVELEDIVFEGFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  80 GVDCVEaggppagagcggYVVGETVKLLKELNAFYE-YDVILFDVLGDVVCGGFAAPLN--YADYCIIITDNGFDALFAA 156
Cdd:COG1348   80 GVKCVEaggpepgvgcagRGIITAIELLEELGAYEEdLDVVIYDVLGDVVCGGFAMPIRegYADEIYIVTSGEFMALYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 157 NRIAASVREKARTHPLRLAGLVGNRTSK---RDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPslsyVC 233
Cdd:COG1348  160 NNICKGIKKYANRGGVRLGGIICNSRNVdgeRELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSE----QA 235

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 649131939 234 DFYLNIADQILARPEGVVPKEVPDRELFSLLSDFYL 269
Cdd:COG1348  236 DEYRELAKKILENKKLVIPKPLSDEELEELLLEYGI 271
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 1-265 1.27e-82

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: 249.59  E-value: 1.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYQGYGG 80
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDLLFSGFNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  81 VDCVEAGGPPAGAGCGGYVVGETVKLLKElNAFYE--YDVILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAA 156
Cdd:cd02117   81 VDCVEAGGPEPGVGCGGRGIGTMLELLEE-HGLLDddYDVVIFDVLGDVVCGGFAAPLrrGFAQKVVIVVSEELMSLYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 157 NRIAASVREKARTHpLRLAGLVGNR--TSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPslsyVCD 234
Cdd:cd02117  160 NNIVKAVENYSKNG-VRLAGLVANLrdPAGTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSP----AAS 234

                        250       260       270
                 ....*....|....*....|....*....|..
gi 649131939 235 FYLNIADQILARPEGVVPKE-VPDRELFSLLS 265
Cdd:cd02117  235 EFARLAAKIADAVPPVPGPRpLSDRELFALLG 266
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 1-265 2.34e-74

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: 228.55  E-value: 2.34e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFL-IPTIIDTLQSKDyhyEDVWPEDVIYQGYG 79
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKaIPTVLDTLREKG---EVEELEDVIKEGFN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  80 GVDCVEaggppagagcggyvVG--------------ETVKLLKELNAF-YEYDVILFDVLGDVVCGGFAAPL--NYADYC 142
Cdd:cd02040   78 GIKCVE--------------SGgpepgvgcagrgiiTAINLLEELGAYeEDLDVVFYDVLGDVVCGGFAMPIreGYADEV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 143 IIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNR---TSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTL 219
Cdd:cd02040  144 YIVTSGEMMALYAANNIAKGIVKYAERGGVRLGGLICNSrnvDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTV 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 649131939 220 FEMAETEPslsyVCDFYLNIADQILARPEGVVPKEVPDRELFSLLS 265
Cdd:cd02040  224 IEYDPDSE----QADEYRELAKKILENKKLVIPKPLTMEELEELLM 265
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 2-260 6.57e-57

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 184.20  E-value: 6.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   2 KIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVwpEDVIYQGYGGV 81
Cdd:PRK13230   3 KFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLREKGIDNLGL--EDIIYEGFNGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  82 DCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEY--DVILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAAN 157
Cdd:PRK13230  81 YCVESGGPEPGYGCAGRGVITAIDLLKKLGVFEELgpDVVIYDILGDVVCGGFAMPLqkGLADDVYIVTTCDPMAIYAAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 158 RIAASVREKARTHPLRLAGLVGNRTSKRD---LIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETepslSYVCD 234
Cdd:PRK13230 161 NICKGIKRFAKRGKSALGGIIYNGRSVIDapdIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPD----SEISN 236

                        250       260
                 ....*....|....*....|....*.
gi 649131939 235 FYLNIADQILARPEGVVPKEVPDREL 260
Cdd:PRK13230 237 IFRELAEAIYENNTGTIPNPLEEEEI 262
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 2-259 3.48e-44

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 151.10  E-value: 3.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   2 KIAVYGKGGIGKSTTSCNISIALARRgKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLqsKDYHYEDVwpEDVIYQGYGGV 81
Cdd:PRK13231   4 KIAIYGKGGIGKSTTVSNMAAAYSND-HRVLVIGCDPKADTTRTLCGKRIPTVLDTL--KDNRKPEL--EDIIHEGFNGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  82 DCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYE-YDVILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAANR 158
Cdd:PRK13231  79 LCVESGGPEPGVGCAGRGVIVAMNLLENLGVFDEdIDVVIYDVLGDVVCGGFSVPLreDYADEVYIVTSGEYMSLYAANN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 159 IAASVReKARThplRLAGLVGNRTSKR---DLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMA-ETEPSlsyvcD 234
Cdd:PRK13231 159 IARGIK-KLKG---KLGGIICNCRGIDnevEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFpESEQA-----S 229

                        250       260
                 ....*....|....*....|....*
gi 649131939 235 FYLNIADQILARPEGVVPKEVPDRE 259
Cdd:PRK13231 230 VYRKLANNIMNNTEFSTPEPMDDEE 254
BchX TIGR02016
chlorophyllide reductase iron protein subunit X; This model represents the X subunit of the ...
 3-278 2.57e-40

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: 141.92  E-value: 2.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939    3 IAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFL-IPTIIDTLQSKDYHYEDVWPEDVIYQ----- 76
Cdd:TIGR02016   3 IAIYGKGGSGKSFTTTNLSHMMAEMGKRVLQLGCDPKHDSTSLLFGGIsLPTIIEVATEKKLAGEEVKVGDVCFKttimn 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   77 GYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAF-YEYDVILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDAL 153
Cdd:TIGR02016  83 GSGGVYGMELGGPEVGRGCGGRGIIHGFDLLEKLGFHdWDFDFVLMDFLGDVVCGGFATPLarSLAEEVIVIGSNDRQSL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  154 FAANRIAASVREKART-HPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLieDIRVSRVKGKTLFEMAETEPSLSYV 232
Cdd:TIGR02016 163 YVANNICNAVEYFRKLgGRVGLLGLVVNRDDGSGEAQAFAREVGIPVLAAIPA--DEELRRKSLAYQIVGSHATPRFGKL 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 649131939  233 CD-FYLNIADQILARPEGVVP-------KEVPDRELFSLL--SDFYLNPTNQKAEQ 278
Cdd:TIGR02016 241 FEeLAGNVADAPPLRPRPLSPdallalfETLPETRVVDLVgaTEEDLRGSNAAAKK 296
nifH PRK13233
nitrogenase iron protein;
2-269 1.45e-35

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 128.78  E-value: 1.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   2 KIAVYGKGGIGKSTTSCNISIALAR-RGKRVLQIGCDPKHDST-FTLTGFLIPTIIDTLQSKDYhyEDVWPEDVIYQGYG 79
Cdd:PRK13233   4 KIAIYGKGGIGKSTTTQNTAAAMAYfHDKKVFIHGCDPKADSTrLILGGKPQTTMMDTLRELGE--EKVTPDKVIKTGFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  80 GVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYE-YDVILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAA 156
Cdd:PRK13233  82 DIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDdLDFVFFDVLGDVVCGGFAMPIrdGKAQEVYIVASGEMMAIYAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 157 NRIAASVREKARTHPLRLAGLVGNRTS---KRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETEPSLSYvc 233
Cdd:PRK13233 162 NNICKGLVKYAEQSGVRLGGIICNSRNvdgELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKE-- 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 649131939 234 dfYLNIADQILARPEGVVPKEVPDRELFSLLSDFYL 269
Cdd:PRK13233 240 --YKELARKIIENKDFVIPKPLTMDELEEMVVKYGL 273
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 3-210 3.19e-29

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: 113.39  E-value: 3.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   3 IAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTL-TGFLIPTIIDTLQSKDYHYEDVWPEDVIYQgYGGV 81
Cdd:cd02033   34 IAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLfGGKACPTIIETSTRKKLAGEEVKIGDVCFK-RGGV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  82 DCVEAGGPPAGAGCGGYVVGETVKLLKELnAFYE--YDVILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAAN 157
Cdd:cd02033  113 FAMELGGPEVGRGCGGRGIIHGFELLEKL-GFHDwgFDYVLLDFLGDVVCGGFGLPIarDMCQKVIVVGSNDLQSLYVAN 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 649131939 158 RIAASVrEKART--HPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIR 210
Cdd:cd02033  192 NVCSAV-EYFRKlgGNVGVAGIVINKDDGTGEAQAFAKAAGIPVLAAIPADEDIR 245
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-246 4.64e-20

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 86.84  E-value: 4.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MK-IAVY-GKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLtGF----LIPTIIDTLQskdyhyEDVWPEDVI 74
Cdd:COG1192    1 MKvIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGL-GLdpddLDPTLYDLLL------DDAPLEDAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  75 YQ-GYGGVDCV-------EAGGPPAGAGCGGYVVGETVKLLKElnafyEYDVILFDvlgdvvCGGFAAPLNY-----ADY 141
Cdd:COG1192   74 VPtEIPGLDLIpanidlaGAEIELVSRPGRELRLKRALAPLAD-----DYDYILID------CPPSLGLLTLnalaaADS 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 142 CIIITDNGFDALFAANRIAASVREKARTH--PLRLAGLVGNRTSKRDLIDKYV-----EACPMPVLE-VLPliEDIRVSR 213
Cdd:COG1192  143 VLIPVQPEYLSLEGLAQLLETIEEVREDLnpKLEILGILLTMVDPRTRLSREVleelrEEFGDKVLDtVIP--RSVALAE 220

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 649131939 214 --VKGKTLFEMAETepslSYVCDFYLNIADQILAR 246
Cdd:COG1192  221 apSAGKPVFEYDPK----SKGAKAYRALAEELLER 251
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-213 2.00e-14

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: 70.84  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939    3 IAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPkhDSTFTLTGFLIPTIIDTLQSK-DYHYEDVWPEDVIY---QGY 78
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDP--QSNNSSVEGLEGDIAPALQALaEGLKGRVNLDPILLkekSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   79 GGVDCV------EAGGPPAGAGCGGYVVGETVKLLKElnafyEYDVILFDVLGDVVCGGFAAPLNyADYCIIITD----- 147
Cdd:pfam01656  80 GGLDLIpgnidlEKFEKELLGPRKEERLREALEALKE-----DYDYVIIDGAPGLGELLRNALIA-ADYVIIPLEpevil 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 649131939  148 -NGFDALfaaNRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEAC-----PMPVLEVLPliEDIRVSR 213
Cdd:pfam01656 154 vEDAKRL---GGVIAALVGGYALLGLKIIGVVLNKVDGDNHGKLLKEALeellrGLPVLGVIP--RDEAVAE 220
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-57 8.18e-13

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: 64.10  E-value: 8.18e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 649131939   1 MKIAVYG-KGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLiptIIDT 57
Cdd:cd02042    1 KVIAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWLYDYI---LIDT 55
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-226 2.41e-09

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 56.71  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVL------------QIGCDPKHDSTFTLTGfLIPTIIDTLQSKDYHY--- 65
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLavdadpnanlaeALGLEVEADLIKPLGE-MRELIKERTGAPGGGMfkl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  66 ----EDVwPEDVIYQGyGGVDCVeaggppagagcggyVVGeTVK------------LLKE-LN--AFYEYDVILFD---- 122
Cdd:COG3640   80 npkvDDI-PEEYLVEG-DGVDLL--------------VMG-TIEeggsgcycpenaLLRAlLNhlVLGNYEYVVVDmeag 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 123 --VLGDVVCGGFaaplnyaDYCIIITDNGFDALFAANRIaasvREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVL 200
Cdd:COG3640  143 ieHLGRGTAEGV-------DLLLVVSEPSRRSIETARRI----KELAEELGIKKIYLVGNKVREEEDEEFLRELLGLELL 211

                        250       260
                 ....*....|....*....|....*.
gi 649131939 201 EVLPLIEDIRVSRVKGKTLFEMAETE 226
Cdd:COG3640  212 GFIPYDEEVREADLEGKPLLDLPDSP 237
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-44 2.78e-09

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: 55.28  E-value: 2.78e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 649131939    1 MK-IAVYG-KGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTF 44
Cdd:pfam13614   1 GKvIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATS 46
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-186 5.83e-09

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 55.96  E-value: 5.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939   3 IAVY-GKGGIGKSTTSCNISIALARRGKRVLQIGCDpkhdstftLTGFLIPTIIDtLQSK----DYHYEDVWPEDVIYQ- 76
Cdd:COG0489   95 IAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDAD--------LRGPSLHRMLG-LENRpglsDVLAGEASLEDVIQPt 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  77 GYGGVDCVeaGGPPAGAGCGGYVVGETVK-LLKELNAfyEYDVILFD---VLGDVVcggfAAPL-NYADYCIIITDNGFD 151
Cdd:COG0489  166 EVEGLDVL--PAGPLPPNPSELLASKRLKqLLEELRG--RYDYVIIDtppGLGVAD----ATLLaSLVDGVLLVVRPGKT 237

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649131939 152 ALFAANRiaasVREKARTHPLRLAGLVGNRTSKRD 186
Cdd:COG0489  238 ALDDVRK----ALEMLEKAGVPVLGVVLNMVCPKG 268
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-31 3.14e-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: 53.23  E-value: 3.14e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 649131939    2 KIAVY-GKGGIGKSTTSCNISIALARRGKRV 31
Cdd:pfam10609   5 VIAVAsGKGGVGKSTVAVNLALALARLGYKV 35
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 7-37 4.58e-08

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: 52.59  E-value: 4.58e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 649131939   7 GKGGIGKSTTSCNISIALARRGKRVLQIGCD 37
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-54 4.83e-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: 52.50  E-value: 4.83e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649131939   2 KIAVY-GKGGIGKSTTSCNISIALARRGKRVLQIGCDpkhdstftLTGFLIPTI 54
Cdd:cd02037    2 IIAVLsGKGGVGKSTVAVNLALALAKKGYKVGLLDAD--------IYGPSIPRL 47
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-40 1.44e-07

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 51.74  E-value: 1.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 649131939   1 MKIAVY-GKGGIGKSTTSCNISIALARRGKRVLQIGCDPKH 40
Cdd:COG0003    3 TRIIFFtGKGGVGKTTVAAATALALAERGKRTLLVSTDPAH 43
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 7-40 1.45e-07

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: 51.35  E-value: 1.45e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 649131939   7 GKGGIGKSTTSCNISIALARRGKRVLQIGCDPKH 40
Cdd:cd02035    7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAH 40
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 15-247 1.96e-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: 50.66  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  15 TTSCNISIALARRGKRVL-------------QIGCDPKHdstftltgflipTIIDTLQskdyhyEDVWPEDVIYQGYGGV 81
Cdd:COG0455    1 TVAVNLAAALARLGKRVLlvdadlglanldvLLGLEPKA------------TLADVLA------GEADLEDAIVQGPGGL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  82 DCV--EAGGPPAGAGCGGYVVGETVKLLKElnafyEYDVILFDV---LGDVVcggfAAPLNYADYCIIITDNGFDALFAA 156
Cdd:COG0455   63 DVLpgGSGPAELAELDPEERLIRVLEELER-----FYDVVLVDTgagISDSV----LLFLAAADEVVVVTTPEPTSITDA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939 157 NRIAASVREKartHPLRLAGLVGNRT----SKRDLIDKYVEAC------PMPVLEVLPLIEDIRVSRVKGKTLFEMA-ET 225
Cdd:COG0455  134 YALLKLLRRR---LGVRRAGVVVNRVrseaEARDVFERLEQVAerflgvRLRVLGVIPEDPAVREAVRRGRPLVLAApDS 210

                        250       260
                 ....*....|....*....|..
gi 649131939 226 EPSLSyvcdfYLNIADQILARP 247
Cdd:COG0455  211 PAARA-----IRELAARLAGWP 227
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-37 2.67e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 48.20  E-value: 2.67e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 649131939   1 MKIAVYG-KGGIGKSTTSCNISIALARRGKRVLQIGCD 37
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 7-38 9.36e-07

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: 49.70  E-value: 9.36e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 649131939    7 GKGGIGKSTTSCNISIALARRGKRVLQIGCDP 38
Cdd:TIGR04291  10 GKGGVGKTSIACATAINLADQGKRVLLVSTDP 41
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-37 1.42e-06

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: 48.33  E-value: 1.42e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 649131939   3 IAVY-GKGGIGKSTTSCNISIALARRGKRVLQIGCD 37
Cdd:cd02038    3 IAVTsGKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-38 1.59e-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: 48.08  E-value: 1.59e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 649131939   1 MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDP 38
Cdd:cd02034    1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 3-40 1.69e-06

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: 48.50  E-value: 1.69e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 649131939    3 IAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKH 40
Cdd:pfam02374   4 IFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAH 41
PHA02518 PHA02518
ParA-like protein; Provisional
 1-43 4.15e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 43.69  E-value: 4.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 649131939   1 MKIAVYG-KGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDST 43
Cdd:PHA02518   1 KIIAVLNqKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST 44
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
3-31 6.27e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.88  E-value: 6.27e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 649131939   3 IAVY-GKGGIGKSTTSCNISIALARRGKRV 31
Cdd:PRK11670 110 IAVSsGKGGVGKSSTAVNLALALAAEGAKV 139
minD CHL00175
septum-site determining protein; Validated
 7-37 1.56e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 42.45  E-value: 1.56e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 649131939   7 GKGGIGKSTTSCNISIALARRGKRVLQIGCD 37
Cdd:CHL00175  23 GKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 10-181 2.47e-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: 41.02  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  10 GIGKSTTSCNISIALARRGKRVLQIGCD---PKHDSTFTLTGflIPTIIDTLQSKDYHyedvwpEDVIYQ-GYGGVDCVe 85
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGLPN--EPGLSEVLSGQASL------EDVIQStNIPNLDVL- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649131939  86 aggppagagcggyVVGETV-------------KLLKELNAfyEYDVILFDvlgdvvcggfAAPLN----------YADYC 142
Cdd:cd05387  101 -------------PAGTVPpnpsellssprfaELLEELKE--QYDYVIID----------TPPVLavadalilapLVDGV 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649131939 143 IIITDNGFDALFAANRiaasVREKARTHPLRLAGLVGNR 181
Cdd:cd05387  156 LLVVRAGKTRRREVKE----ALERLEQAGAKVLGVVLNK 190
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-39 3.37e-04

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


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 41.18  E-value: 3.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 649131939    1 MK-IAVYG-KGGIGKSTTSCNISIALARRGKRVLQIGCDPK 39
Cdd:TIGR03371   1 MKvIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-32 5.93e-04

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


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 40.87  E-value: 5.93e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 649131939   3 IAVYG-KGGIGKSTTSCNISIALARR-GKRVL 32
Cdd:COG4963  105 IAVVGaKGGVGATTLAVNLAWALAREsGRRVL 136
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 7-50 6.24e-04

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 41.23  E-value: 6.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 649131939    7 GKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFL 50
Cdd:TIGR04291 328 GKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSL 371
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 7-38 8.97e-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: 40.63  E-value: 8.97e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 649131939   7 GKGGIGKSTTSCNISIALARRGKRVLQIGCDP 38
Cdd:NF041417  19 GKGGVGKSTVSCATAQWLARNGYDTLLVTTDP 50
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-37 1.10e-03

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 39.74  E-value: 1.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 649131939    3 IAVYG--KGGIGKSTTSCNISIALARRGKRVLQIGCD 37
Cdd:pfam09140   2 VIVVGneKGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
PRK10818 PRK10818
septum site-determining protein MinD;
7-37 2.75e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 38.38  E-value: 2.75e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 649131939   7 GKGGIGKSTTSCNISIALARRGKRVLQIGCD 37
Cdd:PRK10818  10 GKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 8-62 2.85e-03

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 38.19  E-value: 2.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649131939    8 KGGIGKSTTSCNISIALARRGKRVLQIGCD---PKHDSTFT-------LTGFLI--PTIIDTLQSKD 62
Cdd:TIGR01007  26 KPGEGKSTTSANIAIAFAQAGYKTLLIDGDmrnSVMSGTFKsqnkitgLTNFLSgtTDLSDAICDTN 92
 
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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