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Conserved domains on  [gi|6754906|ref|NP_036085|]
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cytosolic Fe-S cluster assembly factor NUBP1 [Mus musculus]

Protein Classification

Mrp/NBP35 family ATP-binding protein (domain architecture ID 10566257)

Mrp (multiple resistance and pH adaptation)/NBP35 (nucleotide-binding protein 35) family ATP-binding protein is an iron-sulfur (FeS) cluster protein that functions as a scaffold to assemble nascent FeS clusters for transfer to FeS-requiring enzymes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
53-303 5.38e-148

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: 402307 [Multi-domain]  Cd Length: 246  Bit Score: 415.69  E-value: 5.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906     53 VRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609   2 VKNVIAVASGKGGVGKSTVAVNLALALAKLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEKTYIF--GKGGGEKLAEELGVPFLGEIPLDPAIREAGDEGKPFVLADPDSPA 234
                         250
                  ....*....|.
gi 6754906    293 TAAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
53-303 5.38e-148

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: 402307 [Multi-domain]  Cd Length: 246  Bit Score: 415.69  E-value: 5.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906     53 VRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609   2 VKNVIAVASGKGGVGKSTVAVNLALALAKLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEKTYIF--GKGGGEKLAEELGVPFLGEIPLDPAIREAGDEGKPFVLADPDSPA 234
                         250
                  ....*....|.
gi 6754906    293 TAAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
55-275 6.90e-131

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: 371.06  E-value: 6.90e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVGFL 134
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037  79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754906  215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
Mrp COG0489
Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell ...
30-277 2.17e-72

Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 223563 [Multi-domain]  Cd Length: 265  Bit Score: 224.60  E-value: 2.17e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   30 LCASGAGAAPDPAVEEIREKM---KTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLE 106
Cdd:COG0489  30 LPKSTASEALRALRTNLKFAKvlrKGVKNVIAVTSGKGGVGKSTVAVNLAAALAQLGK-RVLLLDADLRGPSIPRMLGLE 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  107 GEQVHQ---SGSGWSPVYVDDNLGVMSVGFLLSSPddaVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSV 183
Cdd:COG0489 109 NLPGLTellAGEALEPVIQHDGIKVLSILPLGPVP---VIPRGLLGSKAMLQLLEDVLWGEYDYVIIDTPPGTGDADATV 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  184 VQYLAaahiDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKesqifppttGGAEAMCQDLRiPL 263
Cdd:COG0489 186 LQRIP----DGVVIVTTPGKTALEDVKKAIDMLEKAGIPVLGVVENMSYFICPRCGE---------GGGEKYAERYG-PY 251
                       250
                ....*....|....
gi 6754906  264 LGKVPLDPHIGKSC 277
Cdd:COG0489 252 LGSIPLDPSAREAS 265
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.11e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.66  E-value: 1.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    51 KTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVDdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
                        250
                 ....*....|....
gi 6754906   290 SPATAAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
41-83 9.57e-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: 40.84  E-value: 9.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6754906     41 PAVEEIREKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:TIGR04291 307 PSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKG 349
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
53-303 5.38e-148

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: 402307 [Multi-domain]  Cd Length: 246  Bit Score: 415.69  E-value: 5.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906     53 VRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609   2 VKNVIAVASGKGGVGKSTVAVNLALALAKLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEKTYIF--GKGGGEKLAEELGVPFLGEIPLDPAIREAGDEGKPFVLADPDSPA 234
                         250
                  ....*....|.
gi 6754906    293 TAAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
55-275 6.90e-131

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: 371.06  E-value: 6.90e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVGFL 134
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037  79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754906  215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
Mrp COG0489
Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell ...
30-277 2.17e-72

Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 223563 [Multi-domain]  Cd Length: 265  Bit Score: 224.60  E-value: 2.17e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   30 LCASGAGAAPDPAVEEIREKM---KTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLE 106
Cdd:COG0489  30 LPKSTASEALRALRTNLKFAKvlrKGVKNVIAVTSGKGGVGKSTVAVNLAAALAQLGK-RVLLLDADLRGPSIPRMLGLE 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  107 GEQVHQ---SGSGWSPVYVDDNLGVMSVGFLLSSPddaVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSV 183
Cdd:COG0489 109 NLPGLTellAGEALEPVIQHDGIKVLSILPLGPVP---VIPRGLLGSKAMLQLLEDVLWGEYDYVIIDTPPGTGDADATV 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  184 VQYLAaahiDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKesqifppttGGAEAMCQDLRiPL 263
Cdd:COG0489 186 LQRIP----DGVVIVTTPGKTALEDVKKAIDMLEKAGIPVLGVVENMSYFICPRCGE---------GGGEKYAERYG-PY 251
                       250
                ....*....|....
gi 6754906  264 LGKVPLDPHIGKSC 277
Cdd:COG0489 252 LGSIPLDPSAREAS 265
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.11e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.66  E-value: 1.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    51 KTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVDdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
                        250
                 ....*....|....
gi 6754906   290 SPATAAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
59-303 3.80e-21

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: 89.95  E-value: 3.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   59 VLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQV-------------HQSgsgwspVYVD-- 123
Cdd:cd02036   5 ITSGKGGVGKTTTTANLGVALAKLGK-KVLLIDADIGLRNLDLILGLENRIVytlvdvlegecrlEQA------LIKDkr 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  124 -DNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSvvqylAAAHIDGAVILTTPQ 202
Cdd:cd02036  78 wENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTNPE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  203 EVALQDVRKEISFCHKVKLPIIGVVENMsgfICPKCKKESQIFPPttggaEAMCQDLRIPLLGKVPLDPHIGKSCDKGQS 282
Cdd:cd02036 144 ISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRGEP 215
                       250       260
                ....*....|....*....|.
gi 6754906  283 FFVEAPDSPATAAYRSIIQRI 303
Cdd:cd02036 216 LVLYKPNSLAAKAFENIARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
57-276 1.76e-19

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: 396295 [Multi-domain]  Cd Length: 224  Bit Score: 85.09  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906     57 LLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVDDNLG 127
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRG-LRVLLIDLDP-QSNNSSVLGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVILTTPQEV 204
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGPPGLGE---LLRNALIAA--DYVIIPLEPEVI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    205 ALQDVRKEISFCHKVK-------LPIIGVVENMSGficPKCKKESQIfppttggaEAMCQDLR-IPLLGKVPLDPHIGKS 276
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLRgLPVLGVIPRDEAVAEA 221
FlhG COG0455
MinD-like ATPase involved in chromosome partitioning or flagellar assembly [Cell cycle control, ...
55-299 1.41e-18

MinD-like ATPase involved in chromosome partitioning or flagellar assembly [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 223531 [Multi-domain]  Cd Length: 262  Bit Score: 83.48  E-value: 1.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGE--QVHQSGSGWSP------VYVDDNL 126
Cdd:COG0455   3 KVIAVVSGKGGVGKTTITANLGAALAALGGKVVLLIDADLGLGNLSLLLGVESKptTLHDVLAGEASiediiyETPQDGL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  127 GVMSVG-----FLLSSPDDaviwrgpkKNGMIKQFLRdvdwgDVDYLIVDTPPGTSDEhlsVVQYLAAAhiDGAVILTTP 201
Cdd:COG0455  83 YVLPGGsgledLAKLDPED--------LEDVIKELEE-----LYDYILIDTGAGLSRD---TLSFILSS--DELVIVTTP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  202 QEVALQDVRK--EISFCHKVKLPIIGVVENMSgficpkckkeSQIFPPTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDK 279
Cdd:COG0455 145 EPTSITDAYKtiKILSKLGLDLLGRRVVLNRV----------RSTKEGVDVAALLIQVVKQVPVLQVIPFDPEVRRALAE 214
                       250       260
                ....*....|....*....|
gi 6754906  280 GQSFFVEAPDSPATAAYRSI 299
Cdd:COG0455 215 GKPIVLYSPNSKASQAIKEL 234
BcsQ COG1192
Cellulose biosynthesis protein BcsQ [Cell motility];
49-309 3.85e-18

Cellulose biosynthesis protein BcsQ [Cell motility];


Pssm-ID: 224113 [Multi-domain]  Cd Length: 259  Bit Score: 82.18  E-value: 3.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   49 KMKTVRhkllVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDicgPSIPKIMGLEGEQVHQ-------SGSGWSPVY 121
Cdd:COG1192   1 MMKIIA----VANQKGGVGKTTTAVNLAAALAKRGGKKVLLIDLD---PQGSLTSWLGLRPDLEgdlynllSGLKERPDI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  122 VDDNLGVMSVGFLLSSPDDAV---IWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVvqyLAAAhiDGAVIL 198
Cdd:COG1192  74 LDYTVVIEGLDLIPSNIDLAEgaeIELNAVAKELLLKRLLDPVKDDYDYIIIDTPPSLGVLTLNA---LAAA--DHVLIP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  199 TTPQEVAL-------QDVRKEISFcHKVKLPIIGVVENMsgfICPKCKKESQIFppttggaEAMCQDLRIPLLG-KVPLD 270
Cdd:COG1192 149 VQPEFLDLegleqllNTLEDLLKL-RRNKLIVVGILITR---FDSRTKLADEVL-------QELKQLLGDPVLKtKIPRR 217
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6754906  271 PHIGKSCDKGQSFFVEAPDSPATAAYRSIIQRIRDFCNS 309
Cdd:COG1192 218 VAYREAAAEGKPLYEYDPKSKAAEEYYELAKELLEELLK 256
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
59-293 5.35e-18

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: 81.08  E-value: 5.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   59 VLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVDDNLGV 128
Cdd:cd02038   5 VTSGKGGVGKTNVSANLALALSKLGKR-VLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGLDI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  129 MSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgDVDYLIVDTPPGTSDehlSVVQYLAAAHIdgAVILTTPQEVALQD 208
Cdd:cd02038  80 IPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSITD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  209 ---VRKEISfcHKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAEAMCQ---DLRIPLLGKVPLDPHIGKSCDKGQS 282
Cdd:cd02038 150 ayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQKP 219
                       250
                ....*....|.
gi 6754906  283 FFVEAPDSPAT 293
Cdd:cd02038 220 FVLLFPNSKAS 230
MinD COG2894
Septum formation inhibitor-activating ATPase MinD [Cell cycle control, cell division, ...
59-304 5.05e-17

Septum formation inhibitor-activating ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225447 [Multi-domain]  Cd Length: 272  Bit Score: 79.20  E-value: 5.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   59 VLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQsgsgwspvYVD--------------- 123
Cdd:COG2894   7 VTSGKGGVGKTTTTANIGTALAQLGK-KVVLIDFDIGLRNLDLIMGLENRIVYD--------LVDviegeatlnqalikd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  124 ---DNLgvmsvgFLL----SSPDDAViwrgpKKNGMIKqFLRDVDWGDVDYLIVDTPPGTSDEHLsvvqyLAAAHIDGAV 196
Cdd:COG2894  78 krlENL------FLLpasqTRDKDAL-----TPEGVKK-VVNELKAMDFDYIIIDSPAGIEQGFK-----NAVYFADEAI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  197 ILTTPQEVALQDVRKeisfchkvklpIIGVVENMSgficPKCKKESQIFPP-----------TTG---GAEAMCQDLRIP 262
Cdd:COG2894 141 VVTNPEVSSVRDSDR-----------IIGLLESKS----RRAEIGEEPKEHlllnryrpemvKRGemlSVEDVLEILSIP 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 6754906  263 LLGKVPLDPHIGKSCDKGQSfFVEAPDSPATAAYRSIIQRIR 304
Cdd:COG2894 206 LIGVIPEDQDVLRASNKGEP-VILDDNSDAGKAYRDIARRLL 246
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
56-306 2.88e-16

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 224071 [Multi-domain]  Cd Length: 284  Bit Score: 77.39  E-value: 2.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   56 KLLVLSGKGGVGKSTFSAHLAHGLAEDgdTQVALLDIDICGPSIPKIMGLEGEQVH---------------------QSG 114
Cdd:COG1149   3 QVAVASGKGGTGKTTVAANLAVLLGDK--YKLVLADCDVEAPNLHLLLGVEVLEEEevirgeipeidpekcircgkcAEV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  115 SGWSPVYVDDNLGVMSVGFL--------LSSPDDAvIWRGPKKNGMIKQFLrdVDWGD---------------------- 164
Cdd:COG1149  81 CRFGAIVVLPGGKPVLNPDLcegcgacsIVCPEPA-IEEEPVVIGKIYESK--TDYGFplisgrlnvgeeesgklvtalk 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  165 ------VDYLIVDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkc 238
Cdd:COG1149 158 khakelADLLIIDSAAGT---GCPVIASLKGA--DLAILVTEPTPFGLHDLKRALELVEHFGIP-TGIVINRYN------ 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6754906  239 kkesqifpPTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVeaPDSPATAAYRSIIQRIRDF 306
Cdd:COG1149 226 --------LGDSEIEEYCEEEGIPILGEIPYDKDIPEAYVNGEPFVE--PDSKEAEAILEEAEKLKEF 283
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
58-299 4.79e-14

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


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 70.38  E-value: 4.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   58 LVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVDDNLGVMSVGF 133
Cdd:cd03111   4 AVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSGL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  134 -LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGDVDYLIVDTPPgtsdeHLSVVQYLAAAHIDGAVILTTPQEVALQDV 209
Cdd:cd03111  84 sLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  210 RKEISFC-------HKVKLpIIGVVENMSGfICPKckkesQIfppttggAEAmcqdLRIPLLGKVPLDPH-IGKSCDKGQ 281
Cdd:cd03111 154 RRLLDSLrelegssDRLRL-VLNRYDKKSE-ISPK-----DI-------EEA----LGLEVFATLPNDYKaVSESANTGR 215
                       250
                ....*....|....*...
gi 6754906  282 SFFVEAPDSPATAAYRSI 299
Cdd:cd03111 216 PLVEVAPRSALVRALQDL 233
PRK10818 PRK10818
septum site-determining protein MinD;
57-303 1.29e-13

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 69.58  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    57 LLVLSGKGGVGKSTFSAHLAHGLAEDGDTQVaLLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVDD----NL 126
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTV-VIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVqYLAaahiDGAVILTTPQEVAL 206
Cdd:PRK10818  84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   207 QDVRKeisfchkvklpIIGVVENMS--GFICPKCKKESQIFPPTTGG---------AEAMCQDLRIPLLGKVPLDPHIGK 275
Cdd:PRK10818 151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219
                        250       260
                 ....*....|....*....|....*...
gi 6754906   276 SCDKGQSFFVEApDSPATAAYRSIIQRI 303
Cdd:PRK10818 220 ASNQGEPVILDI-EADAGKAYADTVDRL 246
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
54-229 6.74e-12

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: 63.36  E-value: 6.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   54 RHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ------VHQSgSGWSPVYVDD--N 125
Cdd:cd05387  19 PKVIAVTSASPGEGKSTVAANLAVALAQSG-KRVLLIDADLRRPSLHRLLGLPNEPglsevlSGQA-SLEDVIQSTNipN 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  126 LGVMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgDVDYLIVDTPP--GTSDEHlsvvqyLAAAHIDGAVILTTPQE 203
Cdd:cd05387  97 LDVLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADAL------ILAPLVDGVLLVVRAGK 163
                       170       180
                ....*....|....*....|....*.
gi 6754906  204 VALQDVRKEISFCHKVKLPIIGVVEN 229
Cdd:cd05387 164 TRRREVKEALERLEQAGAKVLGVVLN 189
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
56-268 9.68e-10

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 58.17  E-value: 9.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   56 KLLVLSGKGGVGKSTFSAHLAHGLAEdgdtqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDD----------- 124
Cdd:cd03110   1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  125 -NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 159
Cdd:cd03110  76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  160 VDWGDVDYLIVDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkck 239
Cdd:cd03110 155 ERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD------- 221
                       250       260
                ....*....|....*....|....*....
gi 6754906  240 kesqIFPPTTGGAEAMCQDLRIPLLGKVP 268
Cdd:cd03110 222 ----INDEISEEIEDFADEEGIPLLGKIP 246
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
55-93 3.47e-08

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 51.39  E-value: 3.47e-08
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 6754906   55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
56-308 6.11e-08

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


Pssm-ID: 226166 [Multi-domain]  Cd Length: 255  Bit Score: 52.64  E-value: 6.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   56 KLLVlSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDiCGPSIPKIMGLEGEQVHQSG------------SGWSPVYVD 123
Cdd:COG3640   2 KIAI-TGKGGVGKTTIAALLLKRLLSKGGYNVLVVDAD-PDSNLPEALGVEEPMKYLGGkrellkkrtgaePGGPPGEMF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  124 D-NLGVMSVgfllssPDDAVIWRGPKK------------------NGMIKQFLRDVDWGDVDYLIVDTPPGTsdEHLS-- 182
Cdd:COG3640  80 KeNPLVSDL------PDEYLVENGDIDllvmgkieeggegcacpmNALLRRLLRHLILNRYEVVIVDTEAGI--EHFGrg 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  183 VVQylaaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENmsgficpKCKKESQIFppttggaEAMCQDLRIP 262
Cdd:COG3640 152 TIE-----GVDLVIVVVDPSYKSLRTAERIKELAEELGIKRIFVVLN-------KVDEEEELL-------RELAEELGLE 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 6754906  263 LLGKVPLDPHIGKSCDKGQSFFVEAPDSPATaayRSIIQRIRDFCN 308
Cdd:COG3640 213 VLGVIPYDPEVVEADLKGEPLNEEPEVLKEI---EEIAERLIKLVE 255
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
58-303 1.28e-07

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: 51.54  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   58 LVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDiCGPSIPKIMGLEGEQVHQSGSgwspvyVDD-------NLGVMS 130
Cdd:cd02034   3 IAVAGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKT------IGDirertgaKKGEPP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  131 VGFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGDVDYLIVDTPPGTsdEHLS--VVQ 185
Cdd:cd02034  75 EGMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  186 ylaaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGficpkcKKESQIFPPTTGgaeamcqdLRIPLLG 265
Cdd:cd02034 153 -----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVR------NEEEQELIEELL--------IKLKLIG 213
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6754906  266 KVPLDPHIGKSCDKGQSFFveAPDSPATAAYRSIIQRI 303
Cdd:cd02034 214 VIPYDEEIMEADLKGKPLF--DLDSAAVKAIEKIVEKL 249
minD CHL00175
septum-site determining protein; Validated
48-306 1.89e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 51.31  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    48 EKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyvddnLG 127
Cdd:CHL00175   9 EKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA------------MD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   128 VMSVGFLLsspDDAVI----WRG---------------PKKNgmIKQFLRDVDWGDVDYLIVDTPPGtsdehLSVVQYLA 188
Cdd:CHL00175  76 VLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKN--MNMLVDSLKNRGYDYILIDCPAG-----IDVGFINA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   189 AAHIDGAVILTTPQEVALQDVRK-----EISFCHKVKLPIIGVVENMsgficpkCKKESQIfppTTGGAEAMcqdLRIPL 263
Cdd:CHL00175 146 IAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM---SVRDVQEM---LGIPL 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6754906   264 LGKVPLDPHIGKSCDKG--------------------------QSFFVEApDSPataaYRSIIQRIRDF 306
Cdd:CHL00175 213 LGAIPEDENVIISTNRGeplvlnkkltlsgiafenaarrlvgkQDYFIDL-DSP----SKGPLKRLQKF 276
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
56-93 3.05e-06

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 45.11  E-value: 3.05e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 6754906   56 KLLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:cd01983   2 VIAVTGGKGGVGKTTLAAALAVALAAKGYK-VLLIDLD 38
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
55-174 5.26e-06

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


Pssm-ID: 223082  Cd Length: 322  Bit Score: 47.35  E-value: 5.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTQVAL-----------LDIDIcGPSIPKIMG-LEGEQVHQSGS---GWSP 119
Cdd:COG0003   2 TRIVFFTGKGGVGKTTIAAATAVKLAESGKKVLLVstdpahslgdvFDLEL-GHDPRKVGPnLDALELDPEKAleeYWDE 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6754906  120 VY--VDDNLGVMSVGFLLssPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPP 174
Cdd:COG0003  81 VKdyLARLLRTRGLGGIY--ADELATLPGIDEALALLKILEYYVSGEYDVIVVDTAP 135
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
55-174 5.99e-05

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 43.88  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906     55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDIcGPSIPKIMGLEgeqvhqsgSGWSPVYVDDNLGVMSVG-- 132
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGK-KVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIDpn 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754906    133 -----------------------------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGDVDYLIVDTPP 174
Cdd:pfam02374  71 meleeywqevqkymnallglrmlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
58-305 1.74e-04

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: 42.35  E-value: 1.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906   58 LVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDidicGPSIPKIMGLEGEQVHQSGSGWSPVYVDDN 125
Cdd:cd02117   3 IVVYGKGGIGKSTTASNLSAALAEGGkkvlhvgcdpkhDSTLLLTG----GKVPPTIDEMLTEDGTAEELRREDLLFSGF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  126 LGVMSVGflLSSPDDAViwrGPKKNGMIK--QFLRDV---DW----------GDV---------------DYLIVdtppg 175
Cdd:cd02117  79 NGVDCVE--AGGPEPGV---GCGGRGIGTmlELLEEHgllDDdydvvifdvlGDVvcggfaaplrrgfaqKVVIV----- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906  176 TSDEHLSVvqyLAAAHIDGAVilttpQEVALQDVRkeisfchkvklpIIGVVENMSGficpkckkesqifPPTTGGAEAM 255
Cdd:cd02117 149 VSEELMSL---YAANNIVKAV-----ENYSKNGVR------------LAGLVANLRD-------------PAGTEEIQAF 195
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6754906  256 CQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPATAAYRSIIQRIRD 305
Cdd:cd02117 196 AAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKIAD 245
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
41-83 9.57e-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: 40.84  E-value: 9.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6754906     41 PAVEEIREKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:TIGR04291 307 PSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKG 349
PHA02518 PHA02518
ParA-like protein; Provisional
57-123 1.38e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 39.45  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    57 LLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDICG-------------PSIPKI-MGLE-GEQVHQSGSGWSPVY 121
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHK-VLLVDLDPQGsstdwaeareegePLIPVVrMGKSiRADLPKVASGYDYVV 81

                 ..
gi 6754906   122 VD 123
Cdd:PHA02518  82 VD 83
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
63-223 1.50e-03

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: 404498 [Multi-domain]  Cd Length: 177  Bit Score: 38.71  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906     63 KGGVGKSTFSAHLAHGLAE--------DGDTQVAL-----LDIDICGPSIPKIMGLEG---EQVHQSgsgwspvyVDDNL 126
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKkgkkvlliDLDPQGNAtsglgIDKNNLEKTIYEVLIGEKnisEAIIKT--------VIENL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754906    127 GVMSVGFLLSSPDDAVIWRGPKKNgMIKQFLRDVDwGDVDYLIVDTPPGtsdehLSVVQY--LAAAhiDGAVILTTPQEV 204
Cdd:pfam13614  82 DLLPSNIDLAGAEIELIGIENREN-ILKEALKPVK-DNYDYIIIDCPPS-----LGLLTInaLTAS--DSVIIPVQCEYY 152
                         170
                  ....*....|....*....
gi 6754906    205 ALQDVRKEISFCHKVKLPI 223
Cdd:pfam13614 153 ALEGLSQLLNTIKLVKKRL 171
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
56-83 1.54e-03

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  Cd Length: 250  Bit Score: 39.41  E-value: 1.54e-03
                        10        20
                ....*....|....*....|....*...
gi 6754906   56 KLLVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02035   1 RIIFFGGKGGVGKTTIAAATAVRLAEQG 28
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
62-83 3.80e-03

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: 38.26  E-value: 3.80e-03
                        10        20
                ....*....|....*....|..
gi 6754906   62 GKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02040   7 GKGGIGKSTTASNLSAALAEMG 28
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
62-83 4.88e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 37.81  E-value: 4.88e-03
                          10        20
                  ....*....|....*....|..
gi 6754906     62 GKGGVGKSTFSAHLAHGLAEDG 83
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMG 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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