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Conserved domains on  [gi|18423220|ref|NP_568748|]
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nucleotide binding protein 35 [Arabidopsis thaliana]

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

CATH:  3.40.50.300
Gene Ontology:  GO:0046872|GO:0005524|GO:0051536|GO:0140663|GO:0016226|GO:0016887
PubMed:  8921898

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 ...
 58-343 4.56e-131

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: 374.10  E-value: 4.56e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    58 VKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVeDNLGVMSIGF 137
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   138 MLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVRKEV 217
Cdd:pfam10609  81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   218 SFCKKVGVPVLGVVENMSGLSQPlkdvkfmklatETGSsinvtedviaclrknapelldivaCSEVFdsSGGGAERMCRE 297
Cdd:pfam10609 158 DMFKKVNVPVLGVVENMSYFVCP-----------HCGE------------------------ETYIF--GKGGGEKLAEE 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 18423220   298 MGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVV 343
Cdd:pfam10609 201 LGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 58-343 4.56e-131

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: 374.10  E-value: 4.56e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    58 VKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVeDNLGVMSIGF 137
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   138 MLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVRKEV 217
Cdd:pfam10609  81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   218 SFCKKVGVPVLGVVENMSGLSQPlkdvkfmklatETGSsinvtedviaclrknapelldivaCSEVFdsSGGGAERMCRE 297
Cdd:pfam10609 158 DMFKKVNVPVLGVVENMSYFVCP-----------HCGE------------------------ETYIF--GKGGGEKLAEE 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 18423220   298 MGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVV 343
Cdd:pfam10609 201 LGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 60-314 3.23e-120

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: 345.26  E-value: 3.23e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  60 HKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVeDNLGVMSIGFML 139
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFLL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 140 PnSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVRKEVSF 219
Cdd:cd02037  80 P-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAIDM 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 220 CKKVGVPVLGVVENMSGLSQPLkdvkfmklatetgssinvtedviaclrknapelldivaCSEVFD-SSGGGAERMCREM 298
Cdd:cd02037 156 CKKLNIPVLGIVENMSGFVCPH--------------------------------------CGKKIYiFGKGGGEKLAEEL 197

                       250
                ....*....|....*.
gi 18423220 299 GVPFLGKVPMDPQLCK 314
Cdd:cd02037 198 GVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
55-343 5.75e-112

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 330.24  E-value: 5.75e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   55 MSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVEDNLGVMS 134
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  135 IGFMLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVR 214
Cdd:NF041136  81 IGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI---PDAGAVIVTTPQELALADVR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  215 KEVSFCKKVGVPVLGVVENMSGLSQPlkdvkfmklatETGSSINvtedviaclrknapelldivacseVFDSSGGgaERM 294
Cdd:NF041136 158 KSINFCRKLNIPILGIVENMSGFVCP-----------HCGKEID------------------------IFKSGGG--EKL 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18423220  295 CREMGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVV 343
Cdd:NF041136 201 AEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPIL 249
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
58-235 5.68e-51

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 173.69  E-value: 5.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   58 VKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQE-IHQSNLGWSPVYVEdNLGVMSIG 136
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATNSIG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  137 FMLpNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLLPTgidGAIIVTTPQEVSLIDVRKE 216
Cdd:PRK11670 185 YLV-TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVT---GAVVVTTPQDIALIDAKKG 260

                        170
                 ....*....|....*....
gi 18423220  217 VSFCKKVGVPVLGVVENMS 235
Cdd:PRK11670 261 IVMFEKVEVPVLGIVENMS 279
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 48-234 8.88e-49

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: 165.75  E-value: 8.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  48 LVAIAERMSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQ----EIHQSNLGWSP 123
Cdd:COG0489  81 LLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLED 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 124 V---YVEDNLGVMSIGFMLPNSDEaviwrgPRKNGLIKQFLKDVYwGEIDYLVVDAPPGTSDEHISIVQYLlptgIDGAI 200
Cdd:COG0489 161 ViqpTEVEGLDVLPAGPLPPNPSE------LLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL----VDGVL 229

                       170       180       190
                ....*....|....*....|....*....|....
gi 18423220 201 IVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENM 234
Cdd:COG0489 230 LVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM 263
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 62-211 4.95e-10

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 59.27  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQ------EIHQSNLGWSPVYVED----NLG 131
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRivytlvDVVEGECRLQQALIKDkrlkNLY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   132 VMSIGfmlPNSDEAVIWRGPRKNgLIKQFLKDvywgeIDYLVVDAPPGTSDEHISIVqyllpTGIDGAIIVTTPqEVSLI 211
Cdd:TIGR01968  84 LLPAS---QTRDKDAVTPEQMKK-LVNELKEE-----FDYVIIDCPAGIESGFRNAV-----APADEAIVVTTP-EVSAV 148
ParA_partition NF041546
ParA family partition ATPase;
62-97 1.18e-04

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 42.54  E-value: 1.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 18423220   62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDID 97
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 58-343 4.56e-131

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: 374.10  E-value: 4.56e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    58 VKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVeDNLGVMSIGF 137
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   138 MLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVRKEV 217
Cdd:pfam10609  81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   218 SFCKKVGVPVLGVVENMSGLSQPlkdvkfmklatETGSsinvtedviaclrknapelldivaCSEVFdsSGGGAERMCRE 297
Cdd:pfam10609 158 DMFKKVNVPVLGVVENMSYFVCP-----------HCGE------------------------ETYIF--GKGGGEKLAEE 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 18423220   298 MGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVV 343
Cdd:pfam10609 201 LGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 60-314 3.23e-120

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: 345.26  E-value: 3.23e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  60 HKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVeDNLGVMSIGFML 139
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFLL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 140 PnSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVRKEVSF 219
Cdd:cd02037  80 P-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAIDM 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 220 CKKVGVPVLGVVENMSGLSQPLkdvkfmklatetgssinvtedviaclrknapelldivaCSEVFD-SSGGGAERMCREM 298
Cdd:cd02037 156 CKKLNIPVLGIVENMSGFVCPH--------------------------------------CGKKIYiFGKGGGEKLAEEL 197

                       250
                ....*....|....*.
gi 18423220 299 GVPFLGKVPMDPQLCK 314
Cdd:cd02037 198 GVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
55-343 5.75e-112

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 330.24  E-value: 5.75e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   55 MSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVEDNLGVMS 134
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  135 IGFMLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLlptGIDGAIIVTTPQEVSLIDVR 214
Cdd:NF041136  81 IGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI---PDAGAVIVTTPQELALADVR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  215 KEVSFCKKVGVPVLGVVENMSGLSQPlkdvkfmklatETGSSINvtedviaclrknapelldivacseVFDSSGGgaERM 294
Cdd:NF041136 158 KSINFCRKLNIPILGIVENMSGFVCP-----------HCGKEID------------------------IFKSGGG--EKL 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18423220  295 CREMGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVV 343
Cdd:NF041136 201 AEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPIL 249
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
58-235 5.68e-51

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 173.69  E-value: 5.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   58 VKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQE-IHQSNLGWSPVYVEdNLGVMSIG 136
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATNSIG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  137 FMLpNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLLPTgidGAIIVTTPQEVSLIDVRKE 216
Cdd:PRK11670 185 YLV-TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVT---GAVVVTTPQDIALIDAKKG 260

                        170
                 ....*....|....*....
gi 18423220  217 VSFCKKVGVPVLGVVENMS 235
Cdd:PRK11670 261 IVMFEKVEVPVLGIVENMS 279
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 48-234 8.88e-49

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: 165.75  E-value: 8.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  48 LVAIAERMSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQ----EIHQSNLGWSP 123
Cdd:COG0489  81 LLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLED 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 124 V---YVEDNLGVMSIGFMLPNSDEaviwrgPRKNGLIKQFLKDVYwGEIDYLVVDAPPGTSDEHISIVQYLlptgIDGAI 200
Cdd:COG0489 161 ViqpTEVEGLDVLPAGPLPPNPSE------LLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL----VDGVL 229

                       170       180       190
                ....*....|....*....|....*....|....
gi 18423220 201 IVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENM 234
Cdd:COG0489 230 LVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM 263
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 62-235 6.54e-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: 81.46  E-value: 6.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLG----------LEGqeihQSNLGWSPVYVEDNLG 131
Cdd:cd02038   3 IAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGlapkktlgdvLKG----RVSLEDIIVEGPEGLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 132 VMS--IGFM-LPNSDEAviwrgpRKNGLIKQFLKDVYwgEIDYLVVDAPPGTSDehiSIVQYLLPTgiDGAIIVTTPQEV 208
Cdd:cd02038  79 IIPggSGMEeLANLDPE------QKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAA--DEVIVVTTPEPT 145

                       170       180       190
                ....*....|....*....|....*....|
gi 18423220 209 SLID---VRKEVSfcKKVGVPVLGVVENMS 235
Cdd:cd02038 146 SITDayaLIKVLS--RRGGKKNFRLIVNMA 173
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 50-233 3.93e-14

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: 69.91  E-value: 3.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  50 AIAERMSTVKHK-ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQE--------------- 113
Cdd:cd05387   9 NLLFAGSDAGPKvIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPglsevlsgqasledv 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 114 IHQSNLGwspvyvedNLGVMSIGFMLPNSDEAViwRGPRKNGLIKQfLKDVYwgeiDYLVVDAPP--GTSDEHIsIVQYL 191
Cdd:cd05387  89 IQSTNIP--------NLDVLPAGTVPPNPSELL--SSPRFAELLEE-LKEQY----DYVIIDTPPvlAVADALI-LAPLV 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18423220 192 lptgiDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVEN 233
Cdd:cd05387 153 -----DGVLLVVRAGKTRRREVKEALERLEQAGAKVLGVVLN 189
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 62-321 2.20e-12

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: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNL--------GWSPVYVEDNLGVM 133
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALaeglkgrvNLDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   134 SIGFMLPNSDEAVI---WRGPRKNGLIK---QFLKDVYwgeiDYLVVDAPPGTSDEHISivqYLLPTgiDGAIIVTTPQE 207
Cdd:pfam01656  81 GLDLIPGNIDLEKFekeLLGPRKEERLRealEALKEDY----DYVIIDGAPGLGELLRN---ALIAA--DYVIIPLEPEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   208 VSLIDVRKEVSFCKKVG-------VPVLGVVENMsglsqplkdvkfmklatetgssinvtedviacLRKNAPELLDIVAC 280
Cdd:pfam01656 152 ILVEDAKRLGGVIAALVggyallgLKIIGVVLNK--------------------------------VDGDNHGKLLKEAL 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 18423220   281 SEVfdssgggaermcrEMGVPFLGKVPMDPQLCKAAEQGKS 321
Cdd:pfam01656 200 EEL-------------LRGLPVLGVIPRDEAVAEAPARGLP 227
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 62-233 1.87e-11

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: 62.99  E-value: 1.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEG------QEIHQSNLGWSPVYVED----NLG 131
Cdd:cd02036   3 IVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENrivytlVDVLEGECRLEQALIKDkrweNLY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 132 VMSIGFMLPN---SDEAVIWrgprkngLIKQfLKDVYwgeiDYLVVDAPPGT-SDEHISIvqyllpTGIDGAIIVTTPQE 207
Cdd:cd02036  83 LLPASQTRDKdalTPEKLEE-------LVKE-LKDSF----DFILIDSPAGIeSGFINAI------APADEAIIVTNPEI 144

                       170       180
                ....*....|....*....|....*.
gi 18423220 208 VSLIDVRKEVSFCKKVGVPVLGVVEN 233
Cdd:cd02036 145 SSVRDADRVIGLLESKGIVNIGLIVN 170
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 75-320 2.52e-11

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: 62.60  E-value: 2.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  75 TFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEgqeiHQSNLG---WSPVYVEDNLGVMSIGF-MLP-NSDEAVIWR 149
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLE----PKATLAdvlAGEADLEDAIVQGPGGLdVLPgGSGPAELAE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 150 GPRKNGLIKQF--LKDVYwgeiDYLVVDAPPGTSDEHISIVQYllptgIDGAIIVTTPQEVSLIDVRKevsFCK----KV 223
Cdd:COG0455  77 LDPEERLIRVLeeLERFY----DVVLVDTGAGISDSVLLFLAA-----ADEVVVVTTPEPTSITDAYA---LLKllrrRL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 224 GVPVLGVVENMsglsqplkdvkfmklATETGSSINVTEDVIAclrknapelldivACSEVFDSSgggaermcremgVPFL 303
Cdd:COG0455 145 GVRRAGVVVNR---------------VRSEAEARDVFERLEQ-------------VAERFLGVR------------LRVL 184

                       250
                ....*....|....*..
gi 18423220 304 GKVPMDPQLCKAAEQGK 320
Cdd:COG0455 185 GVIPEDPAVREAVRRGR 201
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 62-211 4.95e-10

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 59.27  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQ------EIHQSNLGWSPVYVED----NLG 131
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRivytlvDVVEGECRLQQALIKDkrlkNLY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   132 VMSIGfmlPNSDEAVIWRGPRKNgLIKQFLKDvywgeIDYLVVDAPPGTSDEHISIVqyllpTGIDGAIIVTTPqEVSLI 211
Cdd:TIGR01968  84 LLPAS---QTRDKDAVTPEQMKK-LVNELKEE-----FDYVIIDCPAGIESGFRNAV-----APADEAIVVTTP-EVSAV 148
minD CHL00175
septum-site determining protein; Validated
 62-343 2.92e-09

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 57.09  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLE------GQEIHQSNLGWSPVYVED----NLG 131
Cdd:CHL00175  18 IVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLEnrvlytAMDVLEGECRLDQALIRDkrwkNLS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  132 VMSIGfmlPNSDEAVIWRGPRKNgLIKQFLKDVYwgeiDYLVVDAPPGTSDEHISIVQyllPTgiDGAIIVTTPQEVSLI 211
Cdd:CHL00175  98 LLAIS---KNRQRYNVTRKNMNM-LVDSLKNRGY----DYILIDCPAGIDVGFINAIA---PA--QEAIVVTTPEITAIR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  212 DVRKevsfckkvgvpVLGVVEnmsglSQPLKDVKFMklatetgssIN-VTEDVIaclRKNapellDIVACSEVfdssggg 290
Cdd:CHL00175 165 DADR-----------VAGLLE-----ANGIYNVKLL---------VNrVRPDMI---QAN-----DMMSVRDV------- 204

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18423220  291 aermcREM-GVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVV 343
Cdd:CHL00175 205 -----QEMlGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFENAARRLV 253
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 61-342 5.60e-09

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 55.94  E-value: 5.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  61 KILVlSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDIcGPSIPKMLGLEGQEIHQSNLGWSPVYVEDNLGVMSIGF--- 137
Cdd:COG3640   2 KIAV-AGKGGVGKTTLSALLARYLAEKGKPVLAVDADP-NANLAEALGLEVEADLIKPLGEMRELIKERTGAPGGGMfkl 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 138 -----MLPnsDEAVIWRG---------PRK---------NGLIKQFLKDVYWGEIDYLVVDAPPGTsdEHISivqYLLPT 194
Cdd:COG3640  80 npkvdDIP--EEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG---RGTAE 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 195 GIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENMsglSQPLKDVKFMKlatetgssinvtedviaclrknapel 274
Cdd:COG3640 153 GVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGNK---VREEEDEEFLR-------------------------- 203

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18423220 275 ldivacsevfdssgggaermcREMGVPFLGKVPMDPQLCKAAEQGKSCFEDNKClISAPALKSIIQKV 342
Cdd:COG3640 204 ---------------------ELLGLELLGFIPYDEEVREADLEGKPLLDLPDS-PAVAAVEEIAEKL 249
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 62-226 9.44e-09

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


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 56.28  E-value: 9.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  62 ILVLSGKGGVGKSTFSAQLSFALAGM-DHQVGLMDIDICGPSIPKMLGLEGQ-----------EIHQSNLGWSPVYVEDN 129
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRrgladalrnpdRLDETLLDRALTRHSSG 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 130 LGVMSigfmLPNSDEAVIWRGPRKNGLIKQFLKDVYwgeiDYLVVDAPPGTSDEHISIVqyllptgiDGA--IIVTTPQE 207
Cdd:COG4963 185 LSVLA----APADLERAEEVSPEAVERLLDLLRRHF----DYVVVDLPRGLNPWTLAAL--------EAAdeVVLVTEPD 248

                       170       180
                ....*....|....*....|
gi 18423220 208 V-SLIDVRKEVSFCKKVGVP 226
Cdd:COG4963 249 LpSLRNAKRLLDLLRELGLP 268
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 55-98 2.75e-08

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 53.91  E-value: 2.75e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 18423220  55 MSTVkhkILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDI 98
Cdd:COG2894   1 MGKV---IVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADI 41
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 62-233 3.85e-08

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 52.82  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIP-------KMLGLEGQEIHQSNLGWSPVYVE-DNLGVM 133
Cdd:TIGR01007  20 LLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSgtfksqnKITGLTNFLSGTTDLSDAICDTNiENLDVI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   134 SIGFMLPNSDEAViwRGPRKNGLIKQFLKdvywgEIDYLVVDAPPgtsdehISIV--QYLLPTGIDGAIIVTTPQEVSLI 211
Cdd:TIGR01007 100 TAGPVPPNPTELL--QSSNFKTLIETLRK-----RFDYIIIDTPP------IGTVtdAAIIARACDASILVTDAGKIKKR 166

                         170       180
                  ....*....|....*....|..
gi 18423220   212 DVRKEVSFCKKVGVPVLGVVEN 233
Cdd:TIGR01007 167 EVKKAKEQLEQAGSNFLGVVLN 188
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 61-238 4.05e-08

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: 53.54  E-value: 4.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  61 KILVLSGKGGVGKSTFSAQLSFALAGmdhqVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVED------------ 128
Cdd:cd03110   1 IIAVLSGKGGTGKTTITANLAVLLYN----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncervc 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 129 NLGVMSIGFMLPNSDEAV---------------IWRGPRKNG------------------------------LIKQFLKD 163
Cdd:cd03110  77 KFGAILEFFQKLIVDESLcegcgacviicprgaIYLKDRDTGkifisssdggplvhgrlnigeensgklvteLRKKALER 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18423220 164 VYwgEIDYLVVDAPPGTSDEHISIVqyllpTGIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVlGVVENMSGLS 238
Cdd:cd03110 157 SK--ECDLAIIDGPPGTGCPVVASI-----TGADAVLLVTEPTPSGLHDLKRAIELAKHFGIPT-GIVINRYDIN 223
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 62-179 6.73e-08

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: 52.94  E-value: 6.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGpSIPKMLGLEGQEIHQS-------NLGWSPVYVEDNLGVMS 134
Cdd:COG1192   4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIVPTEIPGLD 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18423220 135 IgfmLPNSD-----EAVIWRGPRKNGLIKQFLKDVyWGEIDYLVVDAPPG 179
Cdd:COG1192  83 L---IPANIdlagaEIELVSRPGRELRLKRALAPL-ADDYDYILIDCPPS 128
PRK10818 PRK10818
septum site-determining protein MinD;
62-327 1.84e-07

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 51.86  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220   62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIH------QSNLGWSPVYVED----NLg 131
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  132 vmsigFMLPNSD----EAVIWRGprknglIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYllptgIDGAIIVTTPQE 207
Cdd:PRK10818  84 -----YILPASQtrdkDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMALYF-----ADEAIITTNPEV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  208 VSLIDVRKevsfckkvgvpVLGVVENMSGLSQ----PLKD----VKFMKLATETGSSINVtEDVIACLRknapelldiva 279
Cdd:PRK10818 148 SSVRDSDR-----------ILGILASKSRRAEngeePIKEhlllTRYNPGRVSRGDMLSM-EDVLEILR----------- 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18423220  280 csevfdssgggaermcremgVPFLGKVPMDPQLCKAAEQGKSCFEDNK 327
Cdd:PRK10818 205 --------------------IKLVGVIPEDQSVLRASNQGEPVILDIE 232
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 60-97 6.81e-07

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: 47.92  E-value: 6.81e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 18423220  60 HKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDID 97
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
61-178 2.19e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 48.66  E-value: 2.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  61 KILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDIcGPSIPKMLGL----EGQEIHQSNL-------------GWSP 123
Cdd:COG0003   4 RIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDP-AHSLGDVLGTelgnEPTEVAVPNLyaleidpeaeleeYWER 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 124 V--YVED---NLGVMSIGFMLPNSDEAVIWRgprkngLIKQFLKDvywGEIDYLVVDAPP 178
Cdd:COG0003  83 VraPLRGllpSAGVDELAESLPGTEELAALD------ELLELLEE---GEYDVIVVDTAP 133
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 62-258 2.37e-06

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: 48.04  E-value: 2.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  62 ILVLSGKGGVGKSTFSAQLSFALAG-MDHQVGLMDIDICGPSIPKMLGLEGQ----EIHQ--SNLGwsPVYVEDNLGVMS 134
Cdd:cd03111   3 VAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPFGDLGLYLNLRPDydlaDVIQnlDRLD--RTLLDSAVTRHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 135 IGFML----PNSDEAVIWRGPRKNGLIkQFLKDVYwgeiDYLVVDAPPgtsdeHISIVQYLLPTGIDGAIIVTTPQEVSL 210
Cdd:cd03111  81 SGLSLlpapQELEDLEALGAEQVDKLL-QVLRAFY----DHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18423220 211 IDVRKEVSFCKKVGVP------VLGVVENMSGLSqpLKDVK-------FMKLATET---GSSIN 258
Cdd:cd03111 151 RNARRLLDSLRELEGSsdrlrlVLNRYDKKSEIS--PKDIEealglevFATLPNDYkavSESAN 212
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 61-97 4.16e-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: 4.16e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 18423220  61 KILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDID 97
Cdd:cd01983   2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 61-341 6.09e-06

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 46.92  E-value: 6.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  61 KILVlSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDiCGPSIPKMLGLegqEIHQSNLGWSPVYVEDNLG----VMSIG 136
Cdd:cd02034   2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGKVLAVDAD-PNSNLAETLGV---EVEKLPLIKTIGDIRERTGakkgEPPEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 137 FMLPNSDEAVIWRG--------------PRK---------NGLIKQFLKDVYWGEIDYLVVDAPPGTsdEHIS--IVQyl 191
Cdd:cd02034  77 MSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 192 lptGIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENMSGlsqplkdvkfmklatetgssinvTEDVIACLRKNA 271
Cdd:cd02034 153 ---AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVR-----------------------NEEEQELIEELL 206

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 272 PELldivacsevfdssgggaermcremgvPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISapALKSIIQK 341
Cdd:cd02034 207 IKL--------------------------KLIGVIPYDEEIMEADLKGKPLFDLDSAAVK--AIEKIVEK 248
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 60-181 6.65e-06

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 47.34  E-value: 6.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220    60 HKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDIcGPSIPKMLG-------------LEGQEIH-QSNL--GWSP 123
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDP-AHSLSDSFNqkfgheptkvkenLSAMEIDpNMELeeYWQE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18423220   124 VYVEDNLGVMS---IGFM------LPNSDEAVIWrgprkngliKQFLKDVYWGEIDYLVVD-APPGTS 181
Cdd:pfam02374  80 VQKYMNALLGLrmlEGILaeelasLPGIDEAASF---------DEFKKYMDEGEYDVVVFDtAPTGHT 138
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 38-97 9.15e-05

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 44.31  E-value: 9.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18423220    38 ATAPKGPD-PDLVAIAERMSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDID 97
Cdd:TIGR04291 298 ITTPQVPDlPSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
ParA_partition NF041546
ParA family partition ATPase;
62-97 1.18e-04

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 42.54  E-value: 1.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 18423220   62 ILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDID 97
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 61-233 2.32e-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: 42.11  E-value: 2.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220  61 KILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLM------------DIDIcGPSIPKML--GLEGQEI------------ 114
Cdd:cd02035   1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVstdpahslsdafGQKL-GGETPVKGapNLWAMEIdpeealeeywee 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423220 115 HQSNLGWSPVYVEDNLGVMSIGFMLPNSDEAViwrgprknGL--IKQFLKDvywGEIDYLVVDAPPgtsDEHI------- 185
Cdd:cd02035  80 VKELLAQYLRLPGLDEVYAEELLSLPGMDEAA--------AFdeLREYVES---GEYDVIVFDTAP---TGHTlrllslp 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18423220 186 --SIVQYLLPTGIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVEN 233
Cdd:cd02035 146 leQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 60-97 1.63e-03

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


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 39.74  E-value: 1.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 18423220    60 HKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDID 97
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 61-106 6.37e-03

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: 37.73  E-value: 6.37e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18423220  61 KILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDicgpsiPKM 106
Cdd:cd02117   1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCD------PKH 40
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 61-85 9.61e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 37.25  E-value: 9.61e-03
                         10        20
                 ....*....|....*....|....*
gi 18423220   61 KILVLSGKGGVGKSTFSAQLSFALA 85
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFA 27
 
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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