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Conserved domains on  [gi|288543432|gb|ADC47316|]
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4Fe-4S iron sulfur cluster binding protein NifH/frxC family [Methanobrevibacter ruminantium M1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 5-263 3.86e-179

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: 492.86  E-value: 3.86e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKDNKKPELDDLVFEGFNKIKC 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMgGRRIPTILDLLRENKNIKEEDVVFEGYGGVRC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  84 VESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNIS 163
Cdd:NF033200  81 VESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 164 RGIKKLKGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAKDIFD 243
Cdd:NF033200 161 KGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKIME 240

                        250       260
                 ....*....|....*....|
gi 288543432 244 NDNYSTPQPMEDEDFENFFK 263
Cdd:NF033200 241 NTDFVIPEPLEDEELEELFR 260
 
Name Accession Description Interval E-value
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 5-263 3.86e-179

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: 492.86  E-value: 3.86e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKDNKKPELDDLVFEGFNKIKC 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMgGRRIPTILDLLRENKNIKEEDVVFEGYGGVRC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  84 VESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNIS 163
Cdd:NF033200  81 VESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 164 RGIKKLKGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAKDIFD 243
Cdd:NF033200 161 KGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKIME 240

                        250       260
                 ....*....|....*....|
gi 288543432 244 NDNYSTPQPMEDEDFENFFK 263
Cdd:NF033200 241 NTDFVIPEPLEDEELEELFR 260
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 3-267 7.38e-176

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 484.69  E-value: 7.38e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   3 RQKKIAIYGKGGIGKSTTVANIAAAYSEDNKkVMVIGCDPKSDTTRTLCGKRIPTIVHTLKDNKKPELDDLVFEGFNKIK 82
Cdd:PRK13231   1 VMKKIAIYGKGGIGKSTTVSNMAAAYSNDHR-VLVIGCDPKADTTRTLCGKRIPTVLDTLKDNRKPELEDIIHEGFNGIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNI 162
Cdd:PRK13231  80 CVESGGPEPGVGCAGRGVIVAMNLLENLGVFDEDIDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAANNI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 163 SRGIKKLKGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAKDIF 242
Cdd:PRK13231 160 ARGIKKLKGKLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYRKLANNIM 239

                        250       260
                 ....*....|....*....|....*
gi 288543432 243 DNDNYSTPQPMEDEDFENFFKSFID 267
Cdd:PRK13231 240 NNTEFSTPEPMDDEEFEEFFKSFRD 264
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 3-267 7.71e-168

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: 465.03  E-value: 7.71e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   3 RQKKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKDNKK-PELDDLVFEGFNK 80
Cdd:COG1348    1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLgGKRIPTVLDTLREKGEdVELEDIVFEGFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAAN 160
Cdd:COG1348   81 VKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 161 NISRGIKKL----KGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRK 236
Cdd:COG1348  161 NICKGIKKYanrgGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYRE 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 288543432 237 LAKDIFDNDNYSTPQPMEDEDFENFFKSFID 267
Cdd:COG1348  241 LAKKILENKKLVIPKPLSDEELEELLLEYGI 271
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 5-261 2.94e-142

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: 399.97  E-value: 2.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKD-NKKPELDDLVFEGFNKIK 82
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLgGKAIPTVLDTLREkGEVEELEDVIKEGFNGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNI 162
Cdd:cd02040   81 CVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAANNI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 163 SRGIKKLKGN----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLA 238
Cdd:cd02040  161 AKGIVKYAERggvrLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRELA 240

                        250       260
                 ....*....|....*....|...
gi 288543432 239 KDIFDNDNYSTPQPMEDEDFENF 261
Cdd:cd02040  241 KKILENKKLVIPKPLTMEELEEL 263
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 5-265 8.38e-141

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: 396.37  E-value: 8.38e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432    5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCG-KRIPTIVHTLKDN--KKPELDDLVFEGFNKI 81
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGgKAQPTVLDVLREKgaEDLELEDVIKEGFGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   82 KCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANN 161
Cdd:TIGR01287  81 RCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAANN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  162 ISRGIKKLKGN----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKL 237
Cdd:TIGR01287 161 ICKGILKYAKSggvrLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYREL 240

                         250       260
                  ....*....|....*....|....*...
gi 288543432  238 AKDIFDNDNYSTPQPMEDEDFENFFKSF 265
Cdd:TIGR01287 241 AKKIYENTEFVIPTPLTMDELEEILMKF 268
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
5-265 6.74e-114

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 328.25  E-value: 6.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432    5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTR-TLCGKRIPTIVHTLKDNKKPE---LDDLVFEGFNK 80
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRlLLGGKLQPTVLDTAREKGYVEdveVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEeFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAAN 160
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAYDD-LDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  161 NISRGIKKlKGN-----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYR 235
Cdd:pfam00142 160 NIAKGIQK-YAKsggvrLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYR 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 288543432  236 KLAKDIFDNDNYSTPQPMEDEDFENFFKSF 265
Cdd:pfam00142 239 ELARKILENPKGTIPTPLSMDELEALLEDF 268
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-48 3.54e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.05  E-value: 3.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 288543432     3 RQKKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTR 48
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVL 46
 
Name Accession Description Interval E-value
F430_CfbC NF033200
Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit; This family, ...
 5-263 3.86e-179

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: 492.86  E-value: 3.86e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKDNKKPELDDLVFEGFNKIKC 83
Cdd:NF033200   1 KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMgGRRIPTILDLLRENKNIKEEDVVFEGYGGVRC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  84 VESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNIS 163
Cdd:NF033200  81 VESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVLGDVVCGGFAVPLREGYADEVYIVTSGEYMSLYAANNIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 164 RGIKKLKGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAKDIFD 243
Cdd:NF033200 161 KGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQKSELEAKTVIEKAPDSEQAAVYRKLAKKIME 240

                        250       260
                 ....*....|....*....|
gi 288543432 244 NDNYSTPQPMEDEDFENFFK 263
Cdd:NF033200 241 NTDFVIPEPLEDEELEELFR 260
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 3-267 7.38e-176

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 484.69  E-value: 7.38e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   3 RQKKIAIYGKGGIGKSTTVANIAAAYSEDNKkVMVIGCDPKSDTTRTLCGKRIPTIVHTLKDNKKPELDDLVFEGFNKIK 82
Cdd:PRK13231   1 VMKKIAIYGKGGIGKSTTVSNMAAAYSNDHR-VLVIGCDPKADTTRTLCGKRIPTVLDTLKDNRKPELEDIIHEGFNGIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNI 162
Cdd:PRK13231  80 CVESGGPEPGVGCAGRGVIVAMNLLENLGVFDEDIDVVIYDVLGDVVCGGFSVPLREDYADEVYIVTSGEYMSLYAANNI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 163 SRGIKKLKGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAKDIF 242
Cdd:PRK13231 160 ARGIKKLKGKLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQASVYRKLANNIM 239

                        250       260
                 ....*....|....*....|....*
gi 288543432 243 DNDNYSTPQPMEDEDFENFFKSFID 267
Cdd:PRK13231 240 NNTEFSTPEPMDDEEFEEFFKSFRD 264
NifH/CfbC COG1348
Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport ...
 3-267 7.71e-168

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: 465.03  E-value: 7.71e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   3 RQKKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKDNKK-PELDDLVFEGFNK 80
Cdd:COG1348    1 MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLgGKRIPTVLDTLREKGEdVELEDIVFEGFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAAN 160
Cdd:COG1348   81 VKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVLGDVVCGGFAMPIREGYADEIYIVTSGEFMALYAAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 161 NISRGIKKL----KGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRK 236
Cdd:COG1348  161 NICKGIKKYanrgGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVPRSNIVQRAELNGKTVIEYAPDSEQADEYRE 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 288543432 237 LAKDIFDNDNYSTPQPMEDEDFENFFKSFID 267
Cdd:COG1348  241 LAKKILENKKLVIPKPLSDEELEELLLEYGI 271
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 5-261 2.94e-142

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: 399.97  E-value: 2.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLC-GKRIPTIVHTLKD-NKKPELDDLVFEGFNKIK 82
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLgGKAIPTVLDTLREkGEVEELEDVIKEGFNGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNI 162
Cdd:cd02040   81 CVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVLGDVVCGGFAMPIREGYADEVYIVTSGEMMALYAANNI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 163 SRGIKKLKGN----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLA 238
Cdd:cd02040  161 AKGIVKYAERggvrLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRSNEVQEAELRGKTVIEYDPDSEQADEYRELA 240

                        250       260
                 ....*....|....*....|...
gi 288543432 239 KDIFDNDNYSTPQPMEDEDFENF 261
Cdd:cd02040  241 KKILENKKLVIPKPLTMEELEEL 263
nifH TIGR01287
nitrogenase iron protein; This model describes nitrogenase (EC 1.18.6.1) iron protein, also ...
 5-265 8.38e-141

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: 396.37  E-value: 8.38e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432    5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCG-KRIPTIVHTLKDN--KKPELDDLVFEGFNKI 81
Cdd:TIGR01287   1 RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGgKAQPTVLDVLREKgaEDLELEDVIKEGFGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   82 KCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANN 161
Cdd:TIGR01287  81 RCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMALYAANN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  162 ISRGIKKLKGN----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKL 237
Cdd:TIGR01287 161 ICKGILKYAKSggvrLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPRSNIVQKAEIRKMTVIEYDPESEQANEYREL 240

                         250       260
                  ....*....|....*....|....*...
gi 288543432  238 AKDIFDNDNYSTPQPMEDEDFENFFKSF 265
Cdd:TIGR01287 241 AKKIYENTEFVIPTPLTMDELEEILMKF 268
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 5-256 8.39e-116

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 333.28  E-value: 8.39e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGKRIPTIVHTLKDN--KKPELDDLVFEGFNKIK 82
Cdd:PRK13230   2 RKFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLREKgiDNLGLEDIIYEGFNGIY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVGCAGRGVIVAMKRLENLNAFEE-EFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANN 161
Cdd:PRK13230  82 CVESGGPEPGYGCAGRGVITAIDLLKKLGVFEElGPDVVIYDILGDVVCGGFAMPLQKGLADDVYIVTTCDPMAIYAANN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 162 ISRGIKKL----KGNLGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKL 237
Cdd:PRK13230 162 ICKGIKRFakrgKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIPMSNIITEAEIYGKTVIEYAPDSEISNIFREL 241

                        250
                 ....*....|....*....
gi 288543432 238 AKDIFDNDNYSTPQPMEDE 256
Cdd:PRK13230 242 AEAIYENNTGTIPNPLEEE 260
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
5-265 6.74e-114

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 328.25  E-value: 6.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432    5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTR-TLCGKRIPTIVHTLKDNKKPE---LDDLVFEGFNK 80
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRlLLGGKLQPTVLDTAREKGYVEdveVEDVVYKGYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEeFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAAN 160
Cdd:pfam00142  81 VKCVESGGPEPGVGCAGRGVITAINLLEELGAYDD-LDFVLYDVLGDVVCGGFAMPIREGKAQEIYIVTSNEMMALYAAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  161 NISRGIKKlKGN-----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYR 235
Cdd:pfam00142 160 NIAKGIQK-YAKsggvrLGGIICNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYR 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 288543432  236 KLAKDIFDNDNYSTPQPMEDEDFENFFKSF 265
Cdd:pfam00142 239 ELARKILENPKGTIPTPLSMDELEALLEDF 268
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 7-263 2.19e-103

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: 301.59  E-value: 2.19e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   7 IAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCG-KRIPTIVHTLKDNKKPE---LDDLVFEGFNKIK 82
Cdd:cd02117    3 IVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGgKVPPTIDEMLTEDGTAEelrREDLLFSGFNGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAANNI 162
Cdd:cd02117   83 CVEAGGPEPGVGCGGRGIGTMLELLEEHGLLDDDYDVVIFDVLGDVVCGGFAAPLRRGFAQKVVIVVSEELMSLYAANNI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 163 SRGIKKLKGN---LGGIICNCKGIDnEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAK 239
Cdd:cd02117  163 VKAVENYSKNgvrLAGLVANLRDPA-GTEEIQAFAAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAA 241

                        250       260
                 ....*....|....*....|....*
gi 288543432 240 DIFDNDN-YSTPQPMEDEDFENFFK 263
Cdd:cd02117  242 KIADAVPpVPGPRPLSDRELFALLG 266
nifH PRK13233
nitrogenase iron protein;
5-259 4.46e-98

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 288.26  E-value: 4.46e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSE-DNKKVMVIGCDPKSDTTR-TLCGKRIPTIVHTLKDN--KKPELDDLVFEGFNK 80
Cdd:PRK13233   3 RKIAIYGKGGIGKSTTTQNTAAAMAYfHDKKVFIHGCDPKADSTRlILGGKPQTTMMDTLRELgeEKVTPDKVIKTGFKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSLYAAN 160
Cdd:PRK13233  83 IRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDDLDFVFFDVLGDVVCGGFAMPIRDGKAQEVYIVASGEMMAIYAAN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 161 NISRGIKKLKGN----LGGIICNCKGIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRK 236
Cdd:PRK13233 163 NICKGLVKYAEQsgvrLGGIICNSRNVDGELELLEEFTDAIGTQMIHFVPRDNIVQKAEFNKKTVVEFDPDCNQAKEYKE 242

                        250       260
                 ....*....|....*....|...
gi 288543432 237 LAKDIFDNDNYSTPQPMEDEDFE 259
Cdd:PRK13233 243 LARKIIENKDFVIPKPLTMDELE 265
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 5-265 4.05e-78

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: 237.20  E-value: 4.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGKRIPTIVHTLKD-NKKPE---LDDLVFEGFNK 80
Cdd:cd02032    1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSvDFHYEevwPEDVIFTGYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFeEEFDVILYDVLGDVVCGGFSVPLreDYADEVFIVSSGEYMSLYAAN 160
Cdd:cd02032   81 VDCVEAGGPPAGTGCGGYVVGETVKLLKELNAF-DEYDVILFDVLGDVVCGGFAAPL--NYADYCLIVTANDFDSLFAAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 161 NISRGI----KKLKGNLGGIICN-CKGIDneeeIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIE----S 231
Cdd:cd02032  158 RIAAAVrekaKTYPVRLAGIIGNrTDKTD----LIDKFVEAVPMPVLEVLPLIEDIRRSRVKGKTLFEMEESEPElnyvC 233

                        250       260       270
                 ....*....|....*....|....*....|....
gi 288543432 232 DAYRKLAKDIFDNDNYSTPQPMEDEDFENFFKSF 265
Cdd:cd02032  234 DEYLNIADQLLSDPEGVVPKPLPDREIFDLLGDF 267
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 5-259 2.07e-75

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 230.23  E-value: 2.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGKRIPTIVHTL--KDNKKPEL--DDLVFEGFNK 80
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILeeVDFHSEELrpEDFVYEGYNG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  81 IKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFeEEFDVILYDVLGDVVCGGFSVPLreDYADEVFIVSSGEYMSLYAAN 160
Cdd:PRK13185  83 VDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLL-DDYDVILFDVLGDVVCGGFAAPL--QYADYALIVTANDFDSIFAAN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 161 NISRGI----KKLKGNLGGIICN-CKGIDneeeIVNSFAKEIGTQVIGVIGRSNLIQRSELDAKTVVEYA--PESIES-- 231
Cdd:PRK13185 160 RIAAAIqakaKNYKVRLAGVIANrSAGTD----LIDKFNEAVGLKVLAHVPDLDAIRRSRLKGKTLFEMEetDPGLEEvq 235

                        250       260
                 ....*....|....*....|....*....
gi 288543432 232 DAYRKLAKDIFDNDNYSTPQPMEDED-FE 259
Cdd:PRK13185 236 NEYLRLAEQLLAGPEPLVPKPLKDREiFE 264
chlL CHL00072
photochlorophyllide reductase subunit L
 6-167 3.14e-54

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 176.85  E-value: 3.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   6 KIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGKRIPTIVHTL--KD----NKKPEldDLVFEGFN 79
Cdd:CHL00072   2 KLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLqsKDyhyeDVWPE--DVIYKGYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  80 KIKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFeEEFDVILYDVLGDVVCGGFSVPLreDYADEVFIVSSGEYMSLYAA 159
Cdd:CHL00072  80 GVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAF-YEYDIILFDVLGDVVCGGFAAPL--NYADYCIIITDNGFDALFAA 156


                 ....*...
gi 288543432 160 NNISRGIK 167
Cdd:CHL00072 157 NRIAASVR 164
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 2-213 8.17e-47

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: 158.84  E-value: 8.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   2 KRQKKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCG-KRIPTIVHTLKDNK----KPELDDLVFE 76
Cdd:cd02033   29 KETQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFGgKACPTIIETSTRKKlageEVKIGDVCFK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  77 GfNKIKCVESGGPEPGVGCAGRGVIVAMKRLENLNAFEEEFDVILYDVLGDVVCGGFSVPLREDYADEVFIVSSGEYMSL 156
Cdd:cd02033  109 R-GGVFAMELGGPEVGRGCGGRGIIHGFELLEKLGFHDWGFDYVLLDFLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSL 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288543432 157 YAANNISRGI---KKLKGNLG--GIICNckgIDNEEEIVNSFAKEIGTQVIGVIGRSNLIQR 213
Cdd:cd02033  188 YVANNVCSAVeyfRKLGGNVGvaGIVIN---KDDGTGEAQAFAKAAGIPVLAAIPADEDIRR 246
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 5-243 6.01e-21

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: 88.76  E-value: 6.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIY-GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLcG----KRIPTIVHTLKDNKkpELDDLVFE-GF 78
Cdd:COG1192    2 KVIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGL-GldpdDLDPTLYDLLLDDA--PLEDAIVPtEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  79 NKIKCVESGGPEPGVGCAGRGVIVAMKRLEN-LNAFEEEFDVILYDV---LGDVVCGGFSVplredyADEVFIVSSGEYM 154
Cdd:COG1192   79 PGLDLIPANIDLAGAEIELVSRPGRELRLKRaLAPLADDYDYILIDCppsLGLLTLNALAA------ADSVLIPVQPEYL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 155 SLYAANNISRGIKKLKGNLG------GIICNC--KGIDNEEEIVNSFAKEIGTQVIG-VIGRSNLIQRSELDAKTVVEYA 225
Cdd:COG1192  153 SLEGLAQLLETIEEVREDLNpkleilGILLTMvdPRTRLSREVLEELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYD 232

                        250
                 ....*....|....*...
gi 288543432 226 PESIESDAYRKLAKDIFD 243
Cdd:COG1192  233 PKSKGAKAYRALAEELLE 250
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 19-243 2.97e-15

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: 72.61  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  19 TTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGKRI-PTIVHTLKDNKkpELDDLVFEGFNKIKCVeSGGPEPgvgcAG 97
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPkATLADVLAGEA--DLEDAIVQGPGGLDVL-PGGSGP----AE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  98 RGVIVAMKRLEN-LNAFEEEFDVILYDV---LGDVVcggfSVPLREdyADEVFIVSSGEYMSLYAAnniSRGIKKLKGNL 173
Cdd:COG0455   74 LAELDPEERLIRvLEELERFYDVVLVDTgagISDSV----LLFLAA--ADEVVVVTTPEPTSITDA---YALLKLLRRRL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 174 G----GIICNCkgIDNEEEIVNSFAK---------EIGTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRKLAKD 240
Cdd:COG0455  145 GvrraGVVVNR--VRSEAEARDVFERleqvaerflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAAR 222


                 ...
gi 288543432 241 IFD 243
Cdd:COG0455  223 LAG 225
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 7-221 8.68e-13

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: 65.83  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432    7 IAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGK-RIPTIVHTLKDNKKPE--LDDLVFEGFNKIK- 82
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEgDIAPALQALAEGLKGRvnLDPILLKEKSDEGg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   83 -CVESGGPEPGVGCAGRGVIVAMKRL-ENLNAFEEEFDVILYDvlgdvvC-GGFSVPLREDY--ADEVFIVSSGEYMSLY 157
Cdd:pfam01656  82 lDLIPGNIDLEKFEKELLGPRKEERLrEALEALKEDYDYVIID------GaPGLGELLRNALiaADYVIIPLEPEVILVE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288543432  158 AANNISRGIKKLKG-------NLGGIICNCKGIDNEEEIVNSFAKEI--GTQVIGVIGRSNLIQRSELDAKTV 221
Cdd:pfam01656 156 DAKRLGGVIAALVGgyallglKIIGVVLNKVDGDNHGKLLKEALEELlrGLPVLGVIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-50 8.98e-11

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 58.32  E-value: 8.98e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 288543432   5 KKIAIYG-KGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTL 50
Cdd:cd02042    1 KVIAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 7-179 1.55e-10

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: 60.20  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   7 IAIY-GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDP-KSDTTRTLCGKRIPTIVHTLKDNKKPElDDLVFEGFNKIKCV 84
Cdd:COG0489   95 IAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGLENRPGLSDVLAGEASLE-DVIQPTEVEGLDVL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  85 ESGG-PEPGVGcagrgvIVAMKRLENL-NAFEEEFDVILYD---VLGDvvcggfsVPLR--EDYADEVFIVSSGEYMSLY 157
Cdd:COG0489  174 PAGPlPPNPSE------LLASKRLKQLlEELRGRYDYVIIDtppGLGV-------ADATllASLVDGVLLVVRPGKTALD 240

                        170       180
                 ....*....|....*....|..
gi 288543432 158 AANNISRGIKKLKGNLGGIICN 179
Cdd:COG0489  241 DVRKALEMLEKAGVPVLGVVLN 262
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 5-241 1.15e-09

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 57.10  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVI------------GCDPKSDTTRTLCGKR--------IPTIvHTLKD 64
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVdadpnanlaealGLEVEADLIKPLGEMRelikertgAPGG-GMFKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  65 NkkPELDDLVFEGF---NKIKCVESGGPE-PGVGCAGRgVIVAMKR-LENLNafEEEFDVILYD------VLGDVVCGGF 133
Cdd:COG3640   80 N--PKVDDIPEEYLvegDGVDLLVMGTIEeGGSGCYCP-ENALLRAlLNHLV--LGNYEYVVVDmeagieHLGRGTAEGV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 134 svplredyaDEVFIVSSGEYMSLYAAnnisRGIKKLKGNLGgiICNCKGIDN---EEEIVNSFAKEIGTQVIGVIGRSNL 210
Cdd:COG3640  155 ---------DLLLVVSEPSRRSIETA----RRIKELAEELG--IKKIYLVGNkvrEEEDEEFLRELLGLELLGFIPYDEE 219

                        250       260       270
                 ....*....|....*....|....*....|.
gi 288543432 211 IQRSELDAKTVVEyAPESIESDAYRKLAKDI 241
Cdd:COG3640  220 VREADLEGKPLLD-LPDSPAVAAVEEIAEKL 249
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 5-237 2.02e-09

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: 56.55  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTL-CGKRIPTIVHTLKD----------------NKK 67
Cdd:cd02034    1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLgVEVEKLPLIKTIGDirertgakkgeppegmSLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  68 PELDDLVFEGF---NKIKCVESGGPE-PGVGCAGRGVIVAMKRLENLNAFEEEFDVIlydvlgDVVCG--GFSvplR--E 139
Cdd:cd02034   81 PYVDDIIKEIIvepDGIDLLVMGRPEgGGSGCYCPVNALLRELLRHLALKNYEYVVI------DMEAGieHLS---RgtI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 140 DYADEVFIVSSGEYMSLYAANNisrgIKKLKGNLG----GIICNCKGIDNEEEIVNSFAKEIgtQVIGVIGRSNLIQRSE 215
Cdd:cd02034  152 RAVDLLIIVIEPSKRSIQTAKR----IKELAEELGikkiYLIVNKVRNEEEQELIEELLIKL--KLIGVIPYDEEIMEAD 225

                        250       260
                 ....*....|....*....|....
gi 288543432 216 LDAKTVVEYAPESI--ESDAYRKL 237
Cdd:cd02034  226 LKGKPLFDLDSAAVkaIEKIVEKL 249
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 5-47 2.48e-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: 52.20  E-value: 2.48e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 288543432    5 KKIAIYG-KGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTT 47
Cdd:pfam13614   2 KVIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAT 45
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 4-241 5.40e-08

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 52.46  E-value: 5.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432    4 QKKIAIY-GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDpksdttrtLCGKRIPTIVHTlkDNKKPELDDlvfegfNKIK 82
Cdd:pfam10609   3 KHVIAVAsGKGGVGKSTVAVNLALALARLGYKVGLLDAD--------IYGPSIPRMLGL--EGERPEQSD------GGII 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   83 CVESGG----------PEPGVGCAGRGVIVaMKRLENL--NAFEEEFDVILYDV---LGDV---VCGgfSVPLredyaDE 144
Cdd:pfam10609  67 PVEAHGikvmsigfllPDEDDAVIWRGPMK-SGAIKQFltDVDWGELDYLIIDLppgTGDEqltLAQ--LLPL-----TG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  145 VFIVSSGEYMSLYAAnniSRGI---KKLKGNLGGIICN-----CKGIDNEEEI-----VNSFAKEIGTQVIGVIGRSNLI 211
Cdd:pfam10609 139 AVIVTTPQDVALLDV---RKAIdmfKKVNVPVLGVVENmsyfvCPHCGEETYIfgkggGEKLAEELGVPFLGEIPLDPDI 215

                         250       260       270
                  ....*....|....*....|....*....|.
gi 288543432  212 qRSELDA-KTVVEYAPESIESDAYRKLAKDI 241
Cdd:pfam10609 216 -REAGDEgKPFVLADPDSPAAKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 5-61 9.71e-08

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 51.35  E-value: 9.71e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 288543432   5 KKIAIY-GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDpksdttrtLCGKRIPTIVHT 61
Cdd:cd02037    1 HIIAVLsGKGGVGKSTVAVNLALALAKKGYKVGLLDAD--------IYGPSIPRLLGV 50
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 5-228 1.95e-07

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 50.65  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   5 KKIAIY-GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTRTLCGKRIP-TIVHTLKDNKKpeLDDLVFEGFNKIK 82
Cdd:cd02038    1 RIIAVTsGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKkTLGDVLKGRVS--LEDIIVEGPEGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  83 CVESGGPEPGVgcAGRGVIVAMKRLENLNAFEEEFDVILYD----VLGDVVcgGFSVPlredyADEVFIVSSGEYMSL-- 156
Cdd:cd02038   79 IIPGGSGMEEL--ANLDPEQKAKLIEELSSLESNYDYLLIDtgagISRNVL--DFLLA-----ADEVIVVTTPEPTSItd 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 157 -YAA-NNISRgiKKLKGNLGGIICNCKGIDNEEEIVNSFAK------EIGTQVIGVIGRSNLIQRSELDAKTVVEYAPES 228
Cdd:cd02038  150 aYALiKVLSR--RGGKKNFRLIVNMARSPKEGRATFERLKKvakrflDINLDFVGFIPYDQSVRRAVRSQKPFVLLFPNS 227
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 11-241 5.57e-07

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


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 49.12  E-value: 5.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  11 GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPksdTTRTL-----CGKRIP-TIVHTLkdNKKPELDDLVFEGfnkikcv 84
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDADI---GLRNLdlilgLENRIVyTLVDVL--EGECRLEQALIKD------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432  85 eSGGPEPGVGCAGR---GVIVAMKRLENL-NAFEEEFDVILYDVLGDVVCGGFSVPLredYADEVFIVSSGEYMSLYAAN 160
Cdd:cd02036   76 -KRWENLYLLPASQtrdKDALTPEKLEELvKELKDSFDFILIDSPAGIESGFINAIA---PADEAIIVTNPEISSVRDAD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432 161 NISRGIKKL-KGNLGGII--CNCKGIDNEEEIVNSFAKEI-GTQVIGVIGRSNLIQRSELDAKTVVEYAPESIESDAYRK 236
Cdd:cd02036  152 RVIGLLESKgIVNIGLIVnrYRPEMVKSGDMLSVEDIQEIlGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFEN 231


                 ....*
gi 288543432 237 LAKDI 241
Cdd:cd02036  232 IARRL 236
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 5-41 6.04e-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: 47.04  E-value: 6.04e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 288543432   5 KKIAIYG-KGGIGKSTTVANIAAAYSEDNKKVMVIGCD 41
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-123 2.80e-06

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: 46.79  E-value: 2.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288543432   2 KRQKKIAIYG-KGGIGKSTTVANIAAAYSEDNKKVMVIGCDP-KSDTTRTLCGKRIPTIVHTLKDnkKPELDDLVfegfn 79
Cdd:cd05387   17 AGPKVIAVTSaSPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNEPGLSEVLSG--QASLEDVI----- 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 288543432  80 kikcveSGGPEPGVGCAGRGVIVAM-------KRLENL-NAFEEEFDVILYD 123
Cdd:cd05387   90 ------QSTNIPNLDVLPAGTVPPNpsellssPRFAELlEELKEQYDYVIID 135
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 1-38 1.81e-04

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


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 41.94  E-value: 1.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 288543432    1 MKRQKKIAIYGKGGIGKSTTVANIAA--AYSEDNKKVMVI 38
Cdd:TIGR03499 191 LEQGGVIALVGPTGVGKTTTLAKLAArfALEHGKKKVALI 230
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-48 3.54e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.05  E-value: 3.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 288543432     3 RQKKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSDTTR 48
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVL 46
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-42 6.76e-04

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: 40.18  E-value: 6.76e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 288543432  11 GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDP 42
Cdd:cd02035    7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 5-42 1.04e-03

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 39.64  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 288543432    5 KKIAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCDP 42
Cdd:pfam02374   2 RWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDP 39
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-45 1.26e-03

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


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 39.25  E-value: 1.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 288543432    1 MKRqkkIAIYG-KGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSD 45
Cdd:TIGR03371   1 MKV---IAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNL 43
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
5-42 1.48e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 39.42  E-value: 1.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 288543432   5 KKIAIY-GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDP 42
Cdd:COG0003    3 TRIIFFtGKGGVGKTTVAAATALALAERGKRTLLVSTDP 41
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
1-41 1.68e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.08  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 288543432   1 MKRQKKIAIYGKGGIGKSTTVANIAAAYS-EDNKKVMVIGCD 41
Cdd:COG1419  161 LDEGGVIALVGPTGVGKTTTIAKLAARFVlRGKKKVALITTD 202
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 7-41 2.02e-03

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 38.29  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 288543432    7 IAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCD 41
Cdd:pfam00448   3 ILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAAD 37
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 7-41 2.41e-03

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


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 38.12  E-value: 2.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 288543432   7 IAIYGKGGIGKSTTVANIAAAYSEDNKKVMVIGCD 41
Cdd:cd03115    3 ILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAAD 37
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-45 4.33e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 38.15  E-value: 4.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 288543432   11 GKGGIGKSTTVANIAAAYSEDNKKVMVIGCDPKSD 45
Cdd:TIGR04291  10 GKGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 5-41 6.55e-03

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


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 36.76  E-value: 6.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 288543432   5 KKIAIYGKGGIGKSTTVANIAAAYSEDN-KKVMVIGCD 41
Cdd:cd17873    1 RVIALVGPTGVGKTTTLAKLAARYVLKKgKKVALITTD 38
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 14-68 7.34e-03

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


Pssm-ID: 349786  Cd Length: 193  Bit Score: 36.42  E-value: 7.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 288543432  14 GIGKSTTVANIAAAYSEDNKKVMVIGCD---PKS-DTTRTLcGKRIPTIVHTLKDNKKP 68
Cdd:cd18539   10 GSGKTTTAAKLALYLKKKGKKVLLVAADvyrPAAiEQLQTL-GEQVGVPVFESGDGQSP 67
 
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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