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Conserved domains on  [gi|1304970004|gb|PKG36860|]
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iron-sulfur cluster carrier protein ApbC [Psychrobacter sp. Sarcosine-3u-12]

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 ...
 151-393 1.33e-145

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: 413.39  E-value: 1.33e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 151 RIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAHGMAMLSIGS 230
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAHGIKVMSIGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 231 LLDGDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMF 310
Cdd:pfam10609  81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDMF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 311 NKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLA--DDEFAPYYLN 388
Cdd:pfam10609 161 KKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLAdpDSPAAKAFLK 240


                  ....*
gi 1304970004 389 IAKNI 393
Cdd:pfam10609 241 IADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 151-393 1.33e-145

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: 413.39  E-value: 1.33e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 151 RIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAHGMAMLSIGS 230
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAHGIKVMSIGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 231 LLDGDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMF 310
Cdd:pfam10609  81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDMF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 311 NKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLA--DDEFAPYYLN 388
Cdd:pfam10609 161 KKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLAdpDSPAAKAFLK 240


                  ....*
gi 1304970004 389 IAKNI 393
Cdd:pfam10609 241 IADKV 245
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
152-395 3.14e-133

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 386.71  E-value: 3.14e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 152 IRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFI-PINAHGMAMLSIGS 230
Cdd:PRK11670  106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRPTSPDGTHMaPIMAHGLATNSIGY 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 231 LLDGDNTPVaWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMF 310
Cdd:PRK11670  186 LVTDDNAMV-WRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMF 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 311 NKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLA--DDEFAPYYLN 388
Cdd:PRK11670  265 EKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSrpESEFTAIYRQ 344


                  ....*..
gi 1304970004 389 IAKNIEA 395
Cdd:PRK11670  345 LADRVAA 351
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 154-367 3.23e-119

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-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 154 HIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAHGMAMLSIGSLLD 233
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGGIKVMSIGFLLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 234 gDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMFNKT 313
Cdd:cd02037    81 -EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1304970004 314 NIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRA 367
Cdd:cd02037   160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
151-410 1.51e-101

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 305.97  E-value: 1.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 151 RIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAH-GMAMLSIG 229
Cdd:NF041136    3 RIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSdNLKVMSIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 230 SLLDGDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEM 309
Cdd:NF041136   83 FLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 310 FNKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVL--ADDEFAPYYL 387
Cdd:NF041136  163 CRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLdyAWSPAAKALE 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1304970004 388 NIAKNI------------EANISKFAKPVDDKRIF 410
Cdd:NF041136  243 KIVDPIlellenkkslteEPGTMKIAIPTANGKLC 277
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 150-343 6.07e-56

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: 186.16  E-value: 6.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 150 PRIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNvRPELEN---------EQFIPINA 220
Cdd:COG0489    89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLEN-RPGLSDvlageasleDVIQPTEV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 221 HGMAMLSIGSLLDGDNTPVawrgpkATGALMQLYNQTNwPQLDYLVIDMPPGTGDIQLTLAQRIpVTGAVIVTTPQHIAL 300
Cdd:COG0489   168 EGLDVLPAGPLPPNPSELL------ASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTAL 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1304970004 301 LDAQKGIEMFNKTNIPVLGVVENMAlhtcsnCNHTEAIFGTGG 343
Cdd:COG0489   240 DDVRKALEMLEKAGVPVLGVVLNMV------CPKGERYYGGGE 276
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 155-394 6.03e-21

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 91.33  E-value: 6.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELEN--------EQFIPINAHGMAML 226
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDvlageadiKDAIYEGPFGVKVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 227 SIGSLLDGDNTPVAWRGPKATGALMQLYnqtnwpqlDYLVIDMPPGtgdIQLTLAQRIPV-TGAVIVTTPQHIALLDAQK 305
Cdd:TIGR01969  82 PAGVSLEGLRKADPDKLEDVLKEIIDDT--------DFLLIDAPAG---LERDAVTALAAaDELLLVVNPEISSITDALK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 306 GIEMFNKTNIPVLGVVENMALHTCSNCNHTEAifgtgggEKIAEqyhVPLLGQLPLASGIRAQVDKGEPSVL--ADDEFA 383
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVTRDKTELGREEI-------ETILE---VPVLGVVPEDPEVRRAAAFGEPVVIynPNSPAA 220

                         250
                  ....*....|.
gi 1304970004 384 PYYLNIAKNIE 394
Cdd:TIGR01969 221 QAFMELAAELA 231
ParA_partition NF041546
ParA family partition ATPase;
155-191 2.79e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.41  E-value: 2.79e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDAD 191
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 151-393 1.33e-145

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: 413.39  E-value: 1.33e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 151 RIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAHGMAMLSIGS 230
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAHGIKVMSIGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 231 LLDGDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMF 310
Cdd:pfam10609  81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDMF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 311 NKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLA--DDEFAPYYLN 388
Cdd:pfam10609 161 KKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLAdpDSPAAKAFLK 240


                  ....*
gi 1304970004 389 IAKNI 393
Cdd:pfam10609 241 IADKV 245
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
152-395 3.14e-133

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 386.71  E-value: 3.14e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 152 IRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFI-PINAHGMAMLSIGS 230
Cdd:PRK11670  106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRPTSPDGTHMaPIMAHGLATNSIGY 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 231 LLDGDNTPVaWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMF 310
Cdd:PRK11670  186 LVTDDNAMV-WRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMF 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 311 NKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLA--DDEFAPYYLN 388
Cdd:PRK11670  265 EKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSrpESEFTAIYRQ 344


                  ....*..
gi 1304970004 389 IAKNIEA 395
Cdd:PRK11670  345 LADRVAA 351
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 154-367 3.23e-119

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-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 154 HIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAHGMAMLSIGSLLD 233
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGGIKVMSIGFLLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 234 gDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMFNKT 313
Cdd:cd02037    81 -EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1304970004 314 NIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRA 367
Cdd:cd02037   160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
151-410 1.51e-101

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 305.97  E-value: 1.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 151 RIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQFIPINAH-GMAMLSIG 229
Cdd:NF041136    3 RIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSdNLKVMSIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 230 SLLDGDNTPVAWRGPKATGALMQLYNQTNWPQLDYLVIDMPPGTGDIQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEM 309
Cdd:NF041136   83 FLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 310 FNKTNIPVLGVVENMALHTCSNCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVL--ADDEFAPYYL 387
Cdd:NF041136  163 CRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLdyAWSPAAKALE 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1304970004 388 NIAKNI------------EANISKFAKPVDDKRIF 410
Cdd:NF041136  243 KIVDPIlellenkkslteEPGTMKIAIPTANGKLC 277
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 150-343 6.07e-56

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: 186.16  E-value: 6.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 150 PRIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNvRPELEN---------EQFIPINA 220
Cdd:COG0489    89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLEN-RPGLSDvlageasleDVIQPTEV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 221 HGMAMLSIGSLLDGDNTPVawrgpkATGALMQLYNQTNwPQLDYLVIDMPPGTGDIQLTLAQRIpVTGAVIVTTPQHIAL 300
Cdd:COG0489   168 EGLDVLPAGPLPPNPSELL------ASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTAL 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1304970004 301 LDAQKGIEMFNKTNIPVLGVVENMAlhtcsnCNHTEAIFGTGG 343
Cdd:COG0489   240 DDVRKALEMLEKAGVPVLGVVLNMV------CPKGERYYGGGE 276
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 156-374 1.62e-22

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: 95.11  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 156 IVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENEQ------------FIPINAHGM 223
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAeglkgrvnldpiLLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 224 AMLSIGSLLDGDNTPVAWRGPKATGALMQLYNQTNwPQLDYLVIDMPPGTGDiqLTLAQRIPVTGAVIVTTPQHIALLDA 303
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE--LLRNALIAADYVIIPLEPEVILVEDA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304970004 304 QKGIEMF-------NKTNIPVLGVVENMALHTCSNCNHTEAIfgtgggekIAEQYHVPLLGQLPLASGIRAQVDKGEP 374
Cdd:pfam01656 158 KRLGGVIaalvggyALLGLKIIGVVLNKVDGDNHGKLLKEAL--------EELLRGLPVLGVIPRDEAVAEAPARGLP 227
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 155-325 4.31e-21

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: 91.09  E-value: 4.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVdnvrpeleneqfipinahgMAMLSIGSLLDG 234
Cdd:cd02038     2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGL-------------------APKKTLGDVLKG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 235 DNT--PVAWRGPK-------ATG----------ALMQLYN--QTNWPQLDYLVIDMPPGTGDIQLTLAqrIPVTGAVIVT 293
Cdd:cd02038    63 RVSleDIIVEGPEgldiipgGSGmeelanldpeQKAKLIEelSSLESNYDYLLIDTGAGISRNVLDFL--LAADEVIVVT 140

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1304970004 294 TPQHIALLDAQKGIEMFNKTNIPV-LGVVENMA 325
Cdd:cd02038   141 TPEPTSITDAYALIKVLSRRGGKKnFRLIVNMA 173
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 155-394 6.03e-21

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 91.33  E-value: 6.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELEN--------EQFIPINAHGMAML 226
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDvlageadiKDAIYEGPFGVKVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 227 SIGSLLDGDNTPVAWRGPKATGALMQLYnqtnwpqlDYLVIDMPPGtgdIQLTLAQRIPV-TGAVIVTTPQHIALLDAQK 305
Cdd:TIGR01969  82 PAGVSLEGLRKADPDKLEDVLKEIIDDT--------DFLLIDAPAG---LERDAVTALAAaDELLLVVNPEISSITDALK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 306 GIEMFNKTNIPVLGVVENMALHTCSNCNHTEAifgtgggEKIAEqyhVPLLGQLPLASGIRAQVDKGEPSVL--ADDEFA 383
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVTRDKTELGREEI-------ETILE---VPVLGVVPEDPEVRRAAAFGEPVVIynPNSPAA 220

                         250
                  ....*....|.
gi 1304970004 384 PYYLNIAKNIE 394
Cdd:TIGR01969 221 QAFMELAAELA 231
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 155-393 1.93e-19

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: 86.49  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRP-----ELENE----------QFIPin 219
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVytlvdVLEGEcrleqalikdKRWE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 220 ahGMAMLSIGSLLDGDN-TPVAWrgPKATGALMQLYnqtnwpqlDYLVIDMPPGtgdIQLTLAQRI-PVTGAVIVTTPQH 297
Cdd:cd02036    80 --NLYLLPASQTRDKDAlTPEKL--EELVKELKDSF--------DFILIDSPAG---IESGFINAIaPADEAIIVTNPEI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 298 IALLDAQKGIEMFNKTNIPVLGVVENMALHTCSNCNHTEAIfgtgggEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVL 377
Cdd:cd02036   145 SSVRDADRVIGLLESKGIVNIGLIVNRYRPEMVKSGDMLSV------EDIQEILGIPLLGVIPEDPEVIVATNRGEPLVL 218

                         250
                  ....*....|....*...
gi 1304970004 378 ADDEF--APYYLNIAKNI 393
Cdd:cd02036   219 YKPNSlaAKAFENIARRL 236
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 169-395 7.48e-19

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: 84.94  E-value: 7.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 169 TTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDN-------VRPELENEQFIPINAHGMAMLSigslldGDNTPVAW 241
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPkatladvLAGEADLEDAIVQGPGGLDVLP------GGSGPAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 242 RGPKATGALMQLYNQTNwPQLDYLVIDMPPGTGDI---QLTLAQRIpvtgaVIVTTPQHIALLDAQKGIEMFNKTN-IPV 317
Cdd:COG0455    75 AELDPEERLIRVLEELE-RFYDVVLVDTGAGISDSvllFLAAADEV-----VVVTTPEPTSITDAYALLKLLRRRLgVRR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 318 LGVVENMALHTCSNCNHTEAIfgtgggEKIAEQY---HVPLLGQLPLASGIRAQVDKGEPSVLA--DDEFAPYYLNIAKN 392
Cdd:COG0455   149 AGVVVNRVRSEAEARDVFERL------EQVAERFlgvRLRVLGVIPEDPAVREAVRRGRPLVLAapDSPAARAIRELAAR 222


                  ...
gi 1304970004 393 IEA 395
Cdd:COG0455   223 LAG 225
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 83-379 3.92e-16

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: 79.00  E-value: 3.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004  83 AIHMNVRLPAPAKGTGSSLPKAMPKTTNAMDAQNQSASKPdsgtktdtaAEPPITKAAPTQASLTAHPRIRHIIVVASGK 162
Cdd:COG4963    41 AVASGGAAAAAAAYLSAPTPNLILLEALSESAALLADVLP---------LSPDELRAALARLLDPGAARRGRVIAVVGAK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 163 GGVGKSTTTVNIALALQKL-GNRVGVLDADIYGPSMPTMLGVDNVR--------PELENEQFIpinAHGMAMLSIG-SLL 232
Cdd:COG4963   112 GGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRgladalrnPDRLDETLL---DRALTRHSSGlSVL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 233 DGDNTPVAWRGPKAT------GALMQLYnqtnwpqlDYLVIDMPPGTGDIQLTL---AQRIpvtgaVIVTTPQHIALLDA 303
Cdd:COG4963   189 AAPADLERAEEVSPEaverllDLLRRHF--------DYVVVDLPRGLNPWTLAAleaADEV-----VLVTEPDLPSLRNA 255

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304970004 304 QKGIEMFNKTNIPV--LGVVENMALHtcsncnhteaiFGTGGGEKIAEQYHVPLLGQLPLASGIRAQ-VDKGEPSVLAD 379
Cdd:COG4963   256 KRLLDLLRELGLPDdkVRLVLNRVPK-----------RGEISAKDIEEALGLPVAAVLPNDPKAVAEaANQGRPLAEVA 323
minD CHL00175
septum-site determining protein; Validated
 155-379 4.46e-15

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 74.81  E-value: 4.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDN---------VRPELENEQFIPINAH--GM 223
Cdd:CHL00175   17 IIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENrvlytamdvLEGECRLDQALIRDKRwkNL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 224 AMLSIGSLLDGDNTpvawrgpkaTGALMQ-LYNQTNWPQLDYLVIDMPPGtgdIQLTLAQRI-PVTGAVIVTTPQHIALL 301
Cdd:CHL00175   97 SLLAISKNRQRYNV---------TRKNMNmLVDSLKNRGYDYILIDCPAG---IDVGFINAIaPAQEAIVVTTPEITAIR 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304970004 302 DAQKGIEMFNKTNIPVLGVVENMALHTCSNCNHTEAIfgtgggEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLAD 379
Cdd:CHL00175  165 DADRVAGLLEANGIYNVKLLVNRVRPDMIQANDMMSV------RDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNK 236
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 155-394 6.89e-14

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: 71.22  E-value: 6.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLG---------VDNVRPELENEQFIPINAH--GM 223
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGlenrivytlVDVVEGECRLQQALIKDKRlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 224 AMLSIGSLLDGDNTpvawrgpkaTGALMQLYNQTNWPQLDYLVIDMPPGtgdIQLTLAQRI-PVTGAVIVTTPQHIALLD 302
Cdd:TIGR01968  83 YLLPASQTRDKDAV---------TPEQMKKLVNELKEEFDYVIIDCPAG---IESGFRNAVaPADEAIVVTTPEVSAVRD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 303 AQKGI---EMFNKTNIPVLgvVENMALHTCSNcNHTEAIfgtgggEKIAEQYHVPLLGQLPLASGIRAQVDKGEPSVLAD 379
Cdd:TIGR01968 151 ADRVIgllEAKGIEKIHLI--VNRLRPEMVKK-GDMLSV------DDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLND 221

                         250
                  ....*....|....*.
gi 1304970004 380 DEFAPY-YLNIAKNIE 394
Cdd:TIGR01968 222 KSRAGKaFENIARRIL 237
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 155-192 8.33e-14

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 70.86  E-value: 8.33e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADI 192
Cdd:COG2894     4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADI 41
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 142-323 2.35e-13

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: 67.98  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 142 TQASLTAHPRIRHIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVR--------PELENE 213
Cdd:cd05387     8 TNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPglsevlsgQASLED 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 214 QFIPINAHGMAMLSIGSLLDgdnTPVAWRGPKATGALMQLYNQtnwpQLDYLVIDMPP--GTGDIQLtLAQRipVTGAVI 291
Cdd:cd05387    88 VIQSTNIPNLDVLPAGTVPP---NPSELLSSPRFAELLEELKE----QYDYVIIDTPPvlAVADALI-LAPL--VDGVLL 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1304970004 292 VT----TPQHiallDAQKGIEMFNKTNIPVLGVVEN 323
Cdd:cd05387   158 VVragkTRRR----EVKEALERLEQAGAKVLGVVLN 189
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 154-324 1.51e-12

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: 67.19  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 154 HIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGpSMPTMLGVDnvRPELENeqfipinahgmamlSIGSLLD 233
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGLGLD--PDDLDP--------------TLYDLLL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 234 GDNT------PVAWRG-------PKATGALMQLYNQTNWPQL------------DYLVIDMPPGTGDIQ---LTLAQRIp 285
Cdd:COG1192    65 DDAPledaivPTEIPGldlipanIDLAGAEIELVSRPGRELRlkralapladdyDYILIDCPPSLGLLTlnaLAAADSV- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1304970004 286 vtgaVIVTTPQHIA------LLDAQKGIEMFNKTNIPVLGVVENM 324
Cdd:COG1192   144 ----LIPVQPEYLSleglaqLLETIEEVREDLNPKLEILGILLTM 184
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 154-191 1.84e-12

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 64.10  E-value: 1.84e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1304970004 154 HIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDAD 191
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 154-270 8.45e-11

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: 62.09  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 154 HIIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGvdNVRPELENEQF-IPINAHGMAMLSIGSLL 232
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYFE--NRSATADRTGLsLPTPEHLNLPDNDVAEV 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1304970004 233 DGDNTPVAWRGPKATGALMQLYnqtnwpqlDYLVIDMP 270
Cdd:pfam09140  79 PDGENIDDARLEEAFADLEARC--------DFIVIDTP 108
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 153-323 3.57e-10

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: 59.83  E-value: 3.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 153 RHIIVvaSGKGGVGKSTTTVNIALALQKLGNRV------------GVLDADIyGPSMPTmLGVDN-----VRPELENEQF 215
Cdd:cd02035     1 RIIFF--GGKGGVGKTTIAAATAVRLAEQGKRVllvstdpahslsDAFGQKL-GGETPV-KGAPNlwameIDPEEALEEY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 216 I-----PINAHGMAMLSIGSLLDGDNTP-----VAwrgpkATGALMQLYNQTNWpqlDYLVIDMPPgTGD----IQLTLA 281
Cdd:cd02035    77 WeevkeLLAQYLRLPGLDEVYAEELLSLpgmdeAA-----AFDELREYVESGEY---DVIVFDTAP-TGHtlrlLSLPLE 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1304970004 282 QRIPV------TGAVIVTTPQHIALLDAQKGIEMFNKTNIPVLGVVEN 323
Cdd:cd02035   148 QVRELlrdperTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
ParA_partition NF041546
ParA family partition ATPase;
155-191 2.79e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.41  E-value: 2.79e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDAD 191
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 155-323 4.20e-09

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: 56.29  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNVRPELENeqFIPINA---HGMAMLSIGSL 231
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTN--FLSGTTdlsDAICDTNIENL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 232 LDGDNTPVawrgPKATGALMQLYNQTNWPQL-----DYLVIDMPPGTGDIQLTLAQRIpVTGAVIVTTPQHIALLDAQKG 306
Cdd:TIGR01007  97 DVITAGPV----PPNPTELLQSSNFKTLIETlrkrfDYIIIDTPPIGTVTDAAIIARA-CDASILVTDAGKIKKREVKKA 171

                         170
                  ....*....|....*..
gi 1304970004 307 IEMFNKTNIPVLGVVEN 323
Cdd:TIGR01007 172 KEQLEQAGSNFLGVVLN 188
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 155-191 2.16e-08

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 53.36  E-value: 2.16e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDAD 191
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 155-191 4.53e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 47.81  E-value: 4.53e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDAD 191
Cdd:cd01983     2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 155-360 1.14e-06

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: 49.31  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALqklgNRVGVLDADIYGPSMPTMLGVDNV---------RPELENEQFI--------- 216
Cdd:cd03110     1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEeeedfvggkKAFIDQEKCIrcgncervc 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 217 ---PINAHGMAMLSIGSLLDG----------------------------DNTP-------VAWRGPKATGALMQLYNQTN 258
Cdd:cd03110    77 kfgAILEFFQKLIVDESLCEGcgacviicprgaiylkdrdtgkifisssDGGPlvhgrlnIGEENSGKLVTELRKKALER 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 259 WPQLDYLVIDMPPGTGdiQLTLAQRIPVTGAVIVTTPQHIALLDAQKGIEMFNKTNIPVLGVVENMALhtcsNCNHTEAI 338
Cdd:cd03110   157 SKECDLAIIDGPPGTG--CPVVASITGADAVLLVTEPTPSGLHDLKRAIELAKHFGIPTGIVINRYDI----NDEISEEI 230

                         250       260
                  ....*....|....*....|..
gi 1304970004 339 fgtgggEKIAEQYHVPLLGQLP 360
Cdd:cd03110   231 ------EDFADEEGIPLLGKIP 246
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 155-204 3.52e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.85  E-value: 3.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVAsGKGGVGKSTTTVNIALALQKLGNRVGVLDADIyGPSMPTMLGVD 204
Cdd:COG3640     2 KIAVA-GKGGVGKTTLSALLARYLAEKGKPVLAVDADP-NANLAEALGLE 49
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
161-410 4.18e-06

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 47.82  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 161 GKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLG-------VDNVR-----PELENEQFIPINAHGMAMLSI 228
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGgklqptvLDTARekgyvEDVEVEDVVYKGYGGVKCVES 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 229 GSlldgdntPVAWRGPKATGAL--MQLYNQTN-WPQLDYLVIDMppgTGD---------IQLTLAQRIpvtgaVIVTTPQ 296
Cdd:pfam00142  87 GG-------PEPGVGCAGRGVItaINLLEELGaYDDLDFVLYDV---LGDvvcggfampIREGKAQEI-----YIVTSNE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 297 HIALLDAQ---KGIEMFNKTN-IPVLGVVenmalhtcsnCNHTEAIFGTGGGEKIAEQYHVPLLGQLPLASGIRAQVDKG 372
Cdd:pfam00142 152 MMALYAANniaKGIQKYAKSGgVRLGGII----------CNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRK 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1304970004 373 EP--SVLADDEFAPYYLNIAKNIEANiSKFA--KPVDDKRIF 410
Cdd:pfam00142 222 QTviEYAPDSEQAQEYRELARKILEN-PKGTipTPLSMDELE 262
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 161-185 1.01e-05

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 46.91  E-value: 1.01e-05
                          10        20
                  ....*....|....*....|....*
gi 1304970004 161 GKGGVGKSTTTVNIALALQKLGNRV 185
Cdd:cd02032     7 GKGGIGKSTTSSNLSAAFAKRGKKV 31
PRK10818 PRK10818
septum site-determining protein MinD;
155-192 1.25e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 46.47  E-value: 1.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADI 192
Cdd:PRK10818    4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDI 41
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 161-185 1.32e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 46.49  E-value: 1.32e-05
                          10        20
                  ....*....|....*....|....*
gi 1304970004 161 GKGGVGKSTTTVNIALALQKLGNRV 185
Cdd:PRK13185    9 GKGGIGKSTTSSNLSAAFAKLGKKV 33
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 155-323 4.56e-05

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 45.87  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLGVDNvRP----ELENEQFIPINAH-----GMAM 225
Cdd:TIGR01005 555 LIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAP-KPglldLLAGEASIEAGIHrdqrpGLAF 633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 226 LSIGSLLDGDNTPVAWRGPKATGALMQLYNQtnwpQLDYLVIDMPP--GTGDIQLtLAQRipVTGAVIVTTPQHIALLDA 303
Cdd:TIGR01005 634 IAAGGASHFPHNPNELLANPAMAELIDNARN----AFDLVLVDLAAlaAVADAAA-FAAL--ADGILFVTEFERSPLGEI 706

                         170       180
                  ....*....|....*....|
gi 1304970004 304 QKGIEMFNKTNIPVLGVVEN 323
Cdd:TIGR01005 707 RDLIHQEPHANSDVLGVIFN 726
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 156-210 9.38e-05

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: 43.84  E-value: 9.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1304970004 156 IVVAsGKGGVGKSTTTVNIALALQKLGNRVGVLDADIyGPSMPTMLGVDNVRPEL 210
Cdd:cd02034     3 IAVA-GKGGVGKTTIAALLIRYLAKKGGKVLAVDADP-NSNLAETLGVEVEKLPL 55
chlL CHL00072
photochlorophyllide reductase subunit L
 161-202 2.10e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 42.80  E-value: 2.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1304970004 161 GKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPSMPTMLG 202
Cdd:CHL00072    7 GKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTG 48
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 161-203 2.92e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 42.45  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1304970004 161 GKGGVGKSTTTVNIALALQKLGNRVGVLDAD--------IYGPSMPTMLGV 203
Cdd:PRK13230    8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDpkadctrnLVGEKIPTVLDV 58
PHA02518 PHA02518
ParA-like protein; Provisional
 155-196 4.34e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 41.37  E-value: 4.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKLGNRVGVLDADIYGPS 196
Cdd:PHA02518    2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSS 43
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 161-185 4.66e-04

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: 41.73  E-value: 4.66e-04
                          10        20
                  ....*....|....*....|....*
gi 1304970004 161 GKGGVGKSTTTVNIALALQKLGNRV 185
Cdd:cd02040     7 GKGGIGKSTTASNLSAALAEMGKKV 31
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 161-212 7.28e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 40.94  E-value: 7.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304970004 161 GKGGVGKSTTTVNIALALQKlGNRVGVLDAD--------IYGPSMPTMLGV--DNVRPELEN 212
Cdd:PRK13231    9 GKGGIGKSTTVSNMAAAYSN-DHRVLVIGCDpkadttrtLCGKRIPTVLDTlkDNRKPELED 69
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 155-410 8.30e-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: 40.81  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVAsGKGGVGKSTTTVNIALALQKLGNRVGVLDAD--------IYGPSMPT----MLGVDNVRPELENEQFIPINAHG 222
Cdd:cd02117     2 SIVVY-GKGGIGKSTTASNLSAALAEGGKKVLHVGCDpkhdstllLTGGKVPPtideMLTEDGTAEELRREDLLFSGFNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 223 MAMLSIGSLLDGdnTPVAWRGPKATGALMQLYNQTNWpQLDYLVIDMppgTGD---------IQLTLAQRipvtgAVIVT 293
Cdd:cd02117    81 VDCVEAGGPEPG--VGCGGRGIGTMLELLEEHGLLDD-DYDVVIFDV---LGDvvcggfaapLRRGFAQK-----VVIVV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 294 TPQHIALLDAQ---KGIEMFNKTNIPVLGVVENMalhtcSNCNHTEAIfgtgggEKIAEQYHVPLLGQLPL------ASG 364
Cdd:cd02117   150 SEELMSLYAANnivKAVENYSKNGVRLAGLVANL-----RDPAGTEEI------QAFAAAVGTKILAVIPRdpavrrAEL 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1304970004 365 IRAQVDKGEPSVLADDEFAPYYLNIAKNIEANISKfaKPVDDKRIF 410
Cdd:cd02117   219 ARVTVFEHDPVSPAASEFARLAAKIADAVPPVPGP--RPLSDRELF 262
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
156-326 8.75e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 40.96  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 156 IVVASGKGGVGKSTTTVNIALALQKLGNRVGVL--D-----ADIYG---PSMPTMLGVDN------------------VR 207
Cdd:COG0003     5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVstDpahslGDVLGtelGNEPTEVAVPNlyaleidpeaeleeywerVR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 208 PELEN---EQFIPINAHGMA-MLSIGSLLdgdntpvawrgpkatgALMQLYNQTNWpqlDYLVIDMPPgTG--------- 274
Cdd:COG0003    85 APLRGllpSAGVDELAESLPgTEELAALD----------------ELLELLEEGEY---DVIVVDTAP-TGhtlrllslp 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 275 ------------------------------------DIQLTLAQRI----------PVTGAVIVTTPQHIALLDAQKGIE 308
Cdd:COG0003   145 ellgwwldrllklrrkasglgrplagilglpddpvlEGLEELRERLerlrellrdpERTSFRLVTNPERLAIAETRRALE 224

                         250
                  ....*....|....*...
gi 1304970004 309 MFNKTNIPVLGVVENMAL 326
Cdd:COG0003   225 ELALYGIPVDGLVVNRVL 242
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 155-316 1.08e-03

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: 40.34  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 155 IIVVASGKGGVGKSTTTVNIALALQKL-GNRVGVLDADIYGPSMPTMLG-------------VDNVRPELENEQFIPInA 220
Cdd:cd03111     2 VVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNlrpdydladviqnLDRLDRTLLDSAVTRH-S 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 221 HGMAMLSIGSLLDGDNTpvawRGPKATGALMQLYNQtnwpQLDYLVIDMPPGTGDIQLTLAQriPVTGAVIVTTPQHIAL 300
Cdd:cd03111    81 SGLSLLPAPQELEDLEA----LGAEQVDKLLQVLRA----FYDHIIVDLGHFLDEVTLAVLE--AADEILLVTQQDLPSL 150

                         170
                  ....*....|....*.
gi 1304970004 301 LDAQKGIEMFNKTNIP 316
Cdd:cd03111   151 RNARRLLDSLRELEGS 166
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
 144-270 5.69e-03

Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440952  Cd Length: 353  Bit Score: 38.46  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970004 144 ASLTAHPRIRHIIVVasgkGGV--GKSTTT---VNIALALqklGNRVGVLDADI----YGPsmPTMLGVDNVRP------ 208
Cdd:COG1341    27 LEEILSSGPGRIMVL----GPVdsGKSTLTtllANKLLAE---GLKVAIIDADVgqsdLGP--PTTVSLGLVREpvlsls 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304970004 209 ELENEQFIPInahgmamlsigslldGDNTP--VAWRgpkATGALMQLYNQTNWPQLDYLVIDMP 270
Cdd:COG1341    98 ELKAEKLRFV---------------GSISPsgHLLR---IVAGVKRLVERAKERGADRIVIDTD 143
 
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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