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Conserved domains on  [gi|19113764|ref|NP_592852|]
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iron-sulfur assembly component [Schizosaccharomyces pombe]

Protein Classification

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 ...
 3-269 3.27e-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: 384.11  E-value: 3.27e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764     3 KVQHVILVLSGKGGVGKSSVTTQLALSLHDskvysRPLKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTDEt 82
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALAR-----LGYKVGLLDADIYGPSIPRMLG--LEGERPEQSDGGIIPVEAHG- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    83 keIGLMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDGAV 162
Cdd:pfam10609  73 --IKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----------PLTGAV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   163 IVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGEMIE 242
Cdd:pfam10609 141 IVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGD 220

                         250       260
                  ....*....|....*....|....*..
gi 19113764   243 NLTPdsnIVHLYSKTEMSKKFSFITNE 269
Cdd:pfam10609 221 EGKP---FVLADPDSPAAKAFLKIADK 244
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 283-606 9.83e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 176.76  E-value: 9.83e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIeRPVLAVASFDSVVSINE 362
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASAD-GTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 363 KIDDdwECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEAtedDEFDCLAVLQEHTQDVKVVTWHPTEDLLVSGS 442
Cdd:cd00200  80 LETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV---ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 443 YDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATIDSTNILRpalqeewkq 522
Cdd:cd00200 155 QDGTIKLW--DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW-------DLSTGKCLGTLR--------- 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 523 qtslphIHKGAVYTISWM-NDATLCSAGGDGKIVVYQREK---------HDEALWHVAYEQDHAhgvyeinsleylrddR 592
Cdd:cd00200 217 ------GHENGVNSVAFSpDGYLLASGSEDGTIRVWDLRTgecvqtlsgHTNSVTSLAWSPDGK---------------R 275

                       330
                ....*....|....
gi 19113764 593 LLSGGDDGECRVWS 606
Cdd:cd00200 276 LASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-269 3.27e-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: 384.11  E-value: 3.27e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764     3 KVQHVILVLSGKGGVGKSSVTTQLALSLHDskvysRPLKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTDEt 82
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALAR-----LGYKVGLLDADIYGPSIPRMLG--LEGERPEQSDGGIIPVEAHG- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    83 keIGLMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDGAV 162
Cdd:pfam10609  73 --IKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----------PLTGAV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   163 IVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGEMIE 242
Cdd:pfam10609 141 IVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGD 220

                         250       260
                  ....*....|....*....|....*..
gi 19113764   243 NLTPdsnIVHLYSKTEMSKKFSFITNE 269
Cdd:pfam10609 221 EGKP---FVLADPDSPAAKAFLKIADK 244
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 6-239 2.37e-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: 352.57  E-value: 2.37e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   6 HVILVLSGKGGVGKSSVTTQLALSLhdskvYSRPLKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTDEtkeI 85
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALAL-----AKKGYKVGLLDADIYGPSIPRLLG--VEGKPLHQSEEGIVPVEVGG---I 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  86 GLMSLGFLLtSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDGAVIVT 165
Cdd:cd02037  71 KVMSIGFLL-PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI----------PIDGAVVVT 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113764 166 TPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGE 239
Cdd:cd02037 140 TPQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
1-274 1.54e-109

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 333.32  E-value: 1.54e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    1 MDKVQHVILVLSGKGGVGKSSVTTQLALSLHDSKVysrplKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTD 80
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGY-----KVGLLDVDIHGPSIPKLLG--LEGKRLGSEDEGILPVEYS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   81 ETKEIglMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDG 160
Cdd:NF041136  74 DNLKV--MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----------PDAG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  161 AVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGEM 240
Cdd:NF041136 142 AVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEA 221

                        250       260       270
                 ....*....|....*....|....*....|....
gi 19113764  241 IENLTPdsnIVHLYSKTEMSKKFSFITNEFLNQL 274
Cdd:NF041136 222 GDAGRP---FVLDYAWSPAAKALEKIVDPILELL 252
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-254 5.69e-57

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 196.03  E-value: 5.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    4 VQHVILVLSGKGGVGKSSVTTQLALSLHDSKVysrplKTGILDIDLTGPSIPRMFGKDAERnrihqssagwvPVYTDETK 83
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGA-----KVGILDADIYGPSIPTMLGAEDQR-----------PTSPDGTH 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   84 EIGLM-------SLGFLLTSKNdSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTiveslLSEtstvrDV 156
Cdd:PRK11670 170 MAPIMahglatnSIGYLVTDDN-AMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLT-----LAQ-----NI 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  157 PIDGAVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPK 236
Cdd:PRK11670 239 PVTGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHIS 318

                        250       260
                 ....*....|....*....|....
gi 19113764  237 FGEMIENLTP------DSNIVHLY 254
Cdd:PRK11670 319 LREDLDRGTPtvvsrpESEFTAIY 342
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 283-606 9.83e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 176.76  E-value: 9.83e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIeRPVLAVASFDSVVSINE 362
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASAD-GTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 363 KIDDdwECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEAtedDEFDCLAVLQEHTQDVKVVTWHPTEDLLVSGS 442
Cdd:cd00200  80 LETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV---ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 443 YDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATIDSTNILRpalqeewkq 522
Cdd:cd00200 155 QDGTIKLW--DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW-------DLSTGKCLGTLR--------- 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 523 qtslphIHKGAVYTISWM-NDATLCSAGGDGKIVVYQREK---------HDEALWHVAYEQDHAhgvyeinsleylrddR 592
Cdd:cd00200 217 ------GHENGVNSVAFSpDGYLLASGSEDGTIRVWDLRTgecvqtlsgHTNSVTSLAWSPDGK---------------R 275

                       330
                ....*....|....
gi 19113764 593 LLSGGDDGECRVWS 606
Cdd:cd00200 276 LASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
282-606 1.94e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 179.72  E-value: 1.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 282 TITTISGHTGRLWSVAAHP---MLplfATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIERpVLAVASFDSVV 358
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPdgkTL---ASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGK-LLASGSDDGTV 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 359 sineKIDD--DWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEATEDDefdCLAVLQEHTQDVKVVTWHPTED 436
Cdd:COG2319 187 ----RLWDlaTGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGR 259

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 437 LLVSGSYDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATIDSTNILRPal 516
Cdd:COG2319 260 LLASGSADGTVRLW--DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-------DLATGKLLRTLTG-- 328

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 517 qeewkqqtslphiHKGAVYTISWMND-ATLCSAGGDGKIVVYQREkhdeALWHVAYEQDHAHGVyeiNSLEYLRDDRLL- 594
Cdd:COG2319 329 -------------HTGAVRSVAFSPDgKTLASGSDDGTVRLWDLA----TGELLRTLTGHTGAV---TSVAFSPDGRTLa 388

                       330
                ....*....|..
gi 19113764 595 SGGDDGECRVWS 606
Cdd:COG2319 389 SGSADGTVRLWD 400
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-203 4.44e-38

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: 142.25  E-value: 4.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   2 DKVQHVILVLSGKGGVGKSSVTTQLALSLHDSKvysrpLKTGILDIDLTGPSIPRMFGKDAER---NRIHQSSAGWVPVY 78
Cdd:COG0489  89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSG-----KRVLLIDADLRGPSLHRMLGLENRPglsDVLAGEASLEDVIQ 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  79 TDETKEIGLMSLGFLLTskNDSvvwrGPKKAAMIRQFISDVSwGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvpI 158
Cdd:COG0489 164 PTEVEGLDVLPAGPLPP--NPS----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-----------V 225

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19113764 159 DGAVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMsgyICPH 203
Cdd:COG0489 226 DGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 367-406 2.77e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 52.70  E-value: 2.77e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 19113764    367 DWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWE 406
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
368-406 2.67e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 2.67e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19113764   368 WECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWE 406
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 374-450 3.25e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 46.87  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  374 LEGHENEVKCIAWS-CNGNYLATCSRDKSVWIWEATEDDEF-----DCLAVLQEHTQDVKVVTWHPTED-LLVSGSYDNS 446
Cdd:PTZ00420  70 LKGHTSSILDLQFNpCFSEILASGSEDLTIRVWEIPHNDESvkeikDPQCILKGHKKKISIIDWNPMNYyIMCSSGFDSF 149


                 ....
gi 19113764  447 ICFW 450
Cdd:PTZ00420 150 VNIW 153
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-269 3.27e-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: 384.11  E-value: 3.27e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764     3 KVQHVILVLSGKGGVGKSSVTTQLALSLHDskvysRPLKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTDEt 82
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALAR-----LGYKVGLLDADIYGPSIPRMLG--LEGERPEQSDGGIIPVEAHG- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    83 keIGLMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDGAV 162
Cdd:pfam10609  73 --IKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----------PLTGAV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   163 IVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGEMIE 242
Cdd:pfam10609 141 IVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGD 220

                         250       260
                  ....*....|....*....|....*..
gi 19113764   243 NLTPdsnIVHLYSKTEMSKKFSFITNE 269
Cdd:pfam10609 221 EGKP---FVLADPDSPAAKAFLKIADK 244
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 6-239 2.37e-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: 352.57  E-value: 2.37e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   6 HVILVLSGKGGVGKSSVTTQLALSLhdskvYSRPLKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTDEtkeI 85
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALAL-----AKKGYKVGLLDADIYGPSIPRLLG--VEGKPLHQSEEGIVPVEVGG---I 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  86 GLMSLGFLLtSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDGAVIVT 165
Cdd:cd02037  71 KVMSIGFLL-PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI----------PIDGAVVVT 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113764 166 TPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGE 239
Cdd:cd02037 140 TPQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
1-274 1.54e-109

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 333.32  E-value: 1.54e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    1 MDKVQHVILVLSGKGGVGKSSVTTQLALSLHDSKVysrplKTGILDIDLTGPSIPRMFGkdAERNRIHQSSAGWVPVYTD 80
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGY-----KVGLLDVDIHGPSIPKLLG--LEGKRLGSEDEGILPVEYS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   81 ETKEIglMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvPIDG 160
Cdd:NF041136  74 DNLKV--MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----------PDAG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  161 AVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGEM 240
Cdd:NF041136 142 AVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEA 221

                        250       260       270
                 ....*....|....*....|....*....|....
gi 19113764  241 IENLTPdsnIVHLYSKTEMSKKFSFITNEFLNQL 274
Cdd:NF041136 222 GDAGRP---FVLDYAWSPAAKALEKIVDPILELL 252
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-254 5.69e-57

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 196.03  E-value: 5.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    4 VQHVILVLSGKGGVGKSSVTTQLALSLHDSKVysrplKTGILDIDLTGPSIPRMFGKDAERnrihqssagwvPVYTDETK 83
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGA-----KVGILDADIYGPSIPTMLGAEDQR-----------PTSPDGTH 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   84 EIGLM-------SLGFLLTSKNdSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTiveslLSEtstvrDV 156
Cdd:PRK11670 170 MAPIMahglatnSIGYLVTDDN-AMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLT-----LAQ-----NI 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  157 PIDGAVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPK 236
Cdd:PRK11670 239 PVTGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHIS 318

                        250       260
                 ....*....|....*....|....
gi 19113764  237 FGEMIENLTP------DSNIVHLY 254
Cdd:PRK11670 319 LREDLDRGTPtvvsrpESEFTAIY 342
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 283-606 9.83e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 176.76  E-value: 9.83e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIeRPVLAVASFDSVVSINE 362
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASAD-GTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 363 KIDDdwECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEAtedDEFDCLAVLQEHTQDVKVVTWHPTEDLLVSGS 442
Cdd:cd00200  80 LETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV---ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 443 YDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATIDSTNILRpalqeewkq 522
Cdd:cd00200 155 QDGTIKLW--DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW-------DLSTGKCLGTLR--------- 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 523 qtslphIHKGAVYTISWM-NDATLCSAGGDGKIVVYQREK---------HDEALWHVAYEQDHAhgvyeinsleylrddR 592
Cdd:cd00200 217 ------GHENGVNSVAFSpDGYLLASGSEDGTIRVWDLRTgecvqtlsgHTNSVTSLAWSPDGK---------------R 275

                       330
                ....*....|....
gi 19113764 593 LLSGGDDGECRVWS 606
Cdd:cd00200 276 LASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
282-606 1.94e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 179.72  E-value: 1.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 282 TITTISGHTGRLWSVAAHP---MLplfATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIERpVLAVASFDSVV 358
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPdgkTL---ASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGK-LLASGSDDGTV 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 359 sineKIDD--DWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEATEDDefdCLAVLQEHTQDVKVVTWHPTED 436
Cdd:COG2319 187 ----RLWDlaTGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGR 259

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 437 LLVSGSYDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATIDSTNILRPal 516
Cdd:COG2319 260 LLASGSADGTVRLW--DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-------DLATGKLLRTLTG-- 328

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 517 qeewkqqtslphiHKGAVYTISWMND-ATLCSAGGDGKIVVYQREkhdeALWHVAYEQDHAHGVyeiNSLEYLRDDRLL- 594
Cdd:COG2319 329 -------------HTGAVRSVAFSPDgKTLASGSDDGTVRLWDLA----TGELLRTLTGHTGAV---TSVAFSPDGRTLa 388

                       330
                ....*....|..
gi 19113764 595 SGGDDGECRVWS 606
Cdd:COG2319 389 SGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
283-606 2.07e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 173.94  E-value: 2.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPiERPVLAVASFDSVVsine 362
Cdd:COG2319  71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSP-DGKTLASGSADGTV---- 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 363 KIDD--DWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEATEDDefdCLAVLQEHTQDVKVVTWHPTEDLLVS 440
Cdd:COG2319 145 RLWDlaTGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK---LLRTLTGHTGAVRSVAFSPDGKLLAS 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 441 GSYDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATidstnilrpalqeeW 520
Cdd:COG2319 222 GSADGTVRLW--DLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW-------DLAT--------------G 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 521 KQQTSLPHiHKGAVYTISWMND-ATLCSAGGDGKIVVYQREKHDEALWHvayeQDHAHGVYeinSLEYLRDDRLL-SGGD 598
Cdd:COG2319 279 ELLRTLTG-HSGGVNSVAFSPDgKLLASGSDDGTVRLWDLATGKLLRTL----TGHTGAVR---SVAFSPDGKTLaSGSD 350


                ....*...
gi 19113764 599 DGECRVWS 606
Cdd:COG2319 351 DGTVRLWD 358
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 273-494 1.37e-46

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 165.59  E-value: 1.37e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 273 QLYGPRKLDTITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIERpVLAVA 352
Cdd:cd00200  76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGT-FVASS 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 353 SFDSVVSInekID-DDWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEAtedDEFDCLAVLQEHTQDVKVVTW 431
Cdd:cd00200 154 SQDGTIKL---WDlRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL---STGKCLGTLRGHENGVNSVAF 227

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113764 432 HPTEDLLVSGSYDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLW 494
Cdd:cd00200 228 SPDGYLLASGSEDGTIRVW--DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
283-606 7.59e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 155.84  E-value: 7.59e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPiERPVLAVASFDSVVSINE 362
Cdd:COG2319  29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLG-HTAAVLSVAFSP-DGRLLASASADGTVRLWD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 363 KidDDWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEATEDDefdCLAVLQEHTQDVKVVTWHPTEDLLVSGS 442
Cdd:COG2319 107 L--ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK---LLRTLTGHSGAVTSVAFSPDGKLLASGS 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 443 YDNSICFWrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWikissneDVATidstnilrpalqeeWKQ 522
Cdd:COG2319 182 DDGTVRLW--DLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW-------DLAT--------------GKL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 523 QTSLPHiHKGAVYTISWMND-ATLCSAGGDGKIVVYQREKHDEalwhVAYEQDHAHGVyeiNSLEYLRDDRLL-SGGDDG 600
Cdd:COG2319 239 LRTLTG-HSGSVRSVAFSPDgRLLASGSADGTVRLWDLATGEL----LRTLTGHSGGV---NSVAFSPDGKLLaSGSDDG 310


                ....*.
gi 19113764 601 ECRVWS 606
Cdd:COG2319 311 TVRLWD 316
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-203 4.44e-38

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: 142.25  E-value: 4.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   2 DKVQHVILVLSGKGGVGKSSVTTQLALSLHDSKvysrpLKTGILDIDLTGPSIPRMFGKDAER---NRIHQSSAGWVPVY 78
Cdd:COG0489  89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSG-----KRVLLIDADLRGPSLHRMLGLENRPglsDVLAGEASLEDVIQ 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  79 TDETKEIGLMSLGFLLTskNDSvvwrGPKKAAMIRQFISDVSwGELDFLIIDTPPGTGDEHLTIVESLlsetstvrdvpI 158
Cdd:COG0489 164 PTEVEGLDVLPAGPLPP--NPS----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-----------V 225

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19113764 159 DGAVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMsgyICPH 203
Cdd:COG0489 226 DGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
WD40 COG2319
WD40 repeat [General function prediction only];
283-454 3.01e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 120.02  E-value: 3.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 283 ITTISGHTGRLWSVAAHP---MLplfATSSQDKSVRIYNSNTYNLVHVIDGfHTRSIRRVAWRPIERpVLAVASFDSVVS 359
Cdd:COG2319 239 LRTLTGHSGSVRSVAFSPdgrLL---ASGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGK-LLASGSDDGTVR 313

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 360 InekID-DDWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEAtedDEFDCLAVLQEHTQDVKVVTWHPTEDLL 438
Cdd:COG2319 314 L---WDlATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL---ATGELLRTLTGHTGAVTSVAFSPDGRTL 387

                       170
                ....*....|....*.
gi 19113764 439 VSGSYDNSICFWRDDG 454
Cdd:COG2319 388 ASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 370-608 8.28e-28

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 113.20  E-value: 8.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 370 CTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEATEDdefDCLAVLQEHTQDVKVVTWHPTEDLLVSGSYDNSICF 449
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG---ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 450 WrdDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWiKISSNEDVATI----DSTNILRPALQ-------- 517
Cdd:cd00200  78 W--DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-DVETGKCLTTLrghtDWVNSVAFSPDgtfvasss 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 518 ----------EEWKQQTSLPHiHKGAVYTISWMND-ATLCSAGGDGKI---------VVYQREKHDEALWHVAYEQDHah 577
Cdd:cd00200 155 qdgtiklwdlRTGKCVATLTG-HTGEVNSVAFSPDgEKLLSSSSDGTIklwdlstgkCLGTLRGHENGVNSVAFSPDG-- 231

                       250       260       270
                ....*....|....*....|....*....|.
gi 19113764 578 gvyeinsleYLrddrLLSGGDDGECRVWSFK 608
Cdd:cd00200 232 ---------YL----LASGSEDGTIRVWDLR 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 8-246 5.88e-13

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 68.53  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764     8 ILVLSGKGGVGKSSVTTQLA--LSLHDSKVysRPLKtgiLDIDLTGPSIprmFGKDAERNRIHQSSAGWVP--------V 77
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLAraLARRGLRV--LLID---LDPQSNNSSV---EGLEGDIAPALQALAEGLKgrvnldpiL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764    78 YTDETKEIGLMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSwGELDFLIIDTPPGTGdehltivESLLSETSTVrdvp 157
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNIDLEKFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLG-------ELLRNALIAA---- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   158 iDGAVIVTTPQGIATLDVQKEIDFCKK-------ASIKILGIVENMSGyicphcadctnifSSGGGLTLSE-----KYKL 225
Cdd:pfam01656 141 -DYVIIPLEPEVILVEDAKRLGGVIAAlvggyalLGLKIIGVVLNKVD-------------GDNHGKLLKEaleelLRGL 206

                         250       260
                  ....*....|....*....|.
gi 19113764   226 PFLGSVPIDPKFGEMIENLTP 246
Cdd:pfam01656 207 PVLGVIPRDEAVAEAPARGLP 227
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 7-246 1.95e-11

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: 64.13  E-value: 1.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   7 VILVLSGKGGVGKSSVTTQLALSLHDSKvysrpLKTGILDIDLTGPSIPRMFGKDAERNRIHqssagwvpvytdetkeig 86
Cdd:cd02038   2 IIAVTSGKGGVGKTNVSANLALALSKLG-----KRVLLLDADLGLANLDILLGLAPKKTLGD------------------ 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  87 lmslgFLLTSKNDS-VVWRGPK-----------------KAAMIRQFISDVS--WGELDFLIIDTPPGTGDEHLTIVESl 146
Cdd:cd02038  59 -----VLKGRVSLEdIIVEGPEgldiipggsgmeelanlDPEQKAKLIEELSslESNYDYLLIDTGAGISRNVLDFLLA- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 147 lsetstvrdvpIDGAVIVTTPQGIATLDVQkeidfckkASIKIL---------GIVENMsgyicphcadctnIFSSGGGL 217
Cdd:cd02038 133 -----------ADEVIVVTTPEPTSITDAY--------ALIKVLsrrggkknfRLIVNM-------------ARSPKEGR 180

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 19113764 218 TLSEK----------YKLPFLGSVPIDPKFGEMIENLTP 246
Cdd:cd02038 181 ATFERlkkvakrfldINLDFVGFIPYDQSVRRAVRSQKP 219
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 367-406 2.77e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 52.70  E-value: 2.77e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 19113764    367 DWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWE 406
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 21-273 2.12e-08

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: 55.28  E-value: 2.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  21 SVTTQLALSLHdskvySRPLKTGILDIDLTGPSIPRMFGKDAERNrIHQSSAGWVPV--YTDETKEiGLmslgFLLTSKN 98
Cdd:COG0455   1 TVAVNLAAALA-----RLGKRVLLVDADLGLANLDVLLGLEPKAT-LADVLAGEADLedAIVQGPG-GL----DVLPGGS 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  99 DSVVWRGPKKAAMIRQFISDVSwGELDFLIIDTPPGTGDEhlTIVESLLSetstvrdvpiDGAVIVTTP--QGI----AT 172
Cdd:COG0455  70 GPAELAELDPEERLIRVLEELE-RFYDVVLVDTGAGISDS--VLLFLAAA----------DEVVVVTTPepTSItdayAL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 173 LDVqkeidFCKKASIKILGIVENMSGyicphcadctnifSSGGGLTLSEK----------YKLPFLGSVPIDPKFGEMIE 242
Cdd:COG0455 137 LKL-----LRRRLGVRRAGVVVNRVR-------------SEAEARDVFERleqvaerflgVRLRVLGVIPEDPAVREAVR 198

                       250       260       270
                ....*....|....*....|....*....|.
gi 19113764 243 NLTPdsnIVHLYSKTEMSKKFSFITNEFLNQ 273
Cdd:COG0455 199 RGRP---LVLAAPDSPAARAIRELAARLAGW 226
WD40 pfam00400
WD domain, G-beta repeat;
368-406 2.67e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 2.67e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19113764   368 WECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWE 406
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 456-494 1.46e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 1.46e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 19113764    456 DWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLW 494
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 7-195 4.71e-07

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


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 51.05  E-value: 4.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   7 VILVLSGKGGVGKSSVTTQLALSLHDskvysRPLKTGILDIDLTGPSIPRMFGKD-----------AERNRIHQSsagwv 75
Cdd:cd02036   2 VIVITSGKGGVGKTTTTANLGVALAK-----LGKKVLLIDADIGLRNLDLILGLEnrivytlvdvlEGECRLEQA----- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  76 pVYTD-ETKEIGLMSLGFllTSKNDSVvwrGPKKaamIRQFISDVSwGELDFLIIDTPPGTGDEHLTIVesllsetstvr 154
Cdd:cd02036  72 -LIKDkRWENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFINAI----------- 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19113764 155 dVPIDGAVIVTTPQGIATLDVQKEIDFCKKASIKILGIVEN 195
Cdd:cd02036 131 -APADEAIIVTNPEISSVRDADRVIGLLESKGIVNIGLIVN 170
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 413-450 9.69e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.38  E-value: 9.69e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 19113764    413 FDCLAVLQEHTQDVKVVTWHPTEDLLVSGSYDNSICFW 450
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
457-494 1.69e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 1.69e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 19113764   457 WALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLW 494
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 6-236 2.56e-06

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: 49.73  E-value: 2.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764   6 HVILVLSGKGGVGKSSVTTQLALSLHDskvySRPLKTGILDIDLTGPSIPRMFG-------KDAERNR-------IHQSs 71
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALAR----ESGRRVLLVDLDLQFGDVALYLDleprrglADALRNPdrldetlLDRA- 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  72 agwVPVYTDetkeiGLmslgFLLTSKNDSVVWRGPkKAAMIRQFISDVSwGELDFLIIDTPPGTGDEHLTivesLLSETS 151
Cdd:COG4963 178 ---LTRHSS-----GL----SVLAAPADLERAEEV-SPEAVERLLDLLR-RHFDYVVVDLPRGLNPWTLA----ALEAAD 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764 152 TVrdvpidgaVIVTTPQGIATLDVQKEIDFCKKASIKI--LGIVENMsgyicphcadctniFSSGGGLT---LSEKYKLP 226
Cdd:COG4963 240 EV--------VLVTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLNR--------------VPKRGEISakdIEEALGLP 297

                       250
                ....*....|
gi 19113764 227 FLGSVPIDPK 236
Cdd:COG4963 298 VAAVLPNDPK 307
WD40 pfam00400
WD domain, G-beta repeat;
413-450 1.15e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.15e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 19113764   413 FDCLAVLQEHTQDVKVVTWHPTEDLLVSGSYDNSICFW 450
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
 374-450 3.25e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 46.87  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764  374 LEGHENEVKCIAWS-CNGNYLATCSRDKSVWIWEATEDDEF-----DCLAVLQEHTQDVKVVTWHPTED-LLVSGSYDNS 446
Cdd:PTZ00420  70 LKGHTSSILDLQFNpCFSEILASGSEDLTIRVWEIPHNDESvkeikDPQCILKGHKKKISIIDWNPMNYyIMCSSGFDSF 149


                 ....
gi 19113764  447 ICFW 450
Cdd:PTZ00420 150 VNIW 153
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 283-318 5.16e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 40.76  E-value: 5.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 19113764    283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYN 318
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
283-318 1.04e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.04e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 19113764   283 ITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYN 318
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 6-48 2.80e-04

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: 40.99  E-value: 2.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19113764   6 HVILVLSGKGGVGKSSVTTQLALSLHDSKvysrpLKTGILDID 48
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRG-----KRVLLIDLD 38
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 278-318 3.89e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 42.71  E-value: 3.89e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 19113764 278 RKLDTITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYN 318
Cdd:cd00200 249 RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 6-132 6.72e-04

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: 41.67  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113764     6 HVILVLSGKGGVGKSSVTTQLALSLHDskvysRPLKTGILDIDLTGPSIPRMFGkdaerNRihqssAGWVpvytdETKEI 85
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLY-----KGARVAAIDLDLRQRTFHRYFE-----NR-----SATA-----DRTGL 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19113764    86 GLMSLGFLLTSKNDSVVWRGPKKAAMIR--QFISDVSwGELDFLIIDTP 132
Cdd:pfam09140  61 SLPTPEHLNLPDNDVAEVPDGENIDDARleEAFADLE-ARCDFIVIDTP 108
 
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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