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Conserved domains on  [gi|24667611|ref|NP_649243|]
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uncharacterized protein Dmel_CG4858 [Drosophila melanogaster]

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 ...
 4-254 5.78e-141

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: 395.28  E-value: 5.78e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     4 KVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDesqTLAVMS 83
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    84 IGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEvgcHGAIIVTTPQEVALDDVR 163
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPL---TGAVIVTTPQDVALLDVR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   164 KEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDSTT 243
Cdd:pfam10609 155 KAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 24667611   244 AEVLTHIVEKL 254
Cdd:pfam10609 235 AKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 4-254 5.78e-141

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: 395.28  E-value: 5.78e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     4 KVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDesqTLAVMS 83
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    84 IGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEvgcHGAIIVTTPQEVALDDVR 163
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPL---TGAVIVTTPQDVALLDVR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   164 KEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDSTT 243
Cdd:pfam10609 155 KAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 24667611   244 AEVLTHIVEKL 254
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 7-225 4.79e-127

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: 359.12  E-value: 4.79e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDEsqtLAVMSIGF 86
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGG---IKVMSIGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  87 LLkNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKevgCHGAIIVTTPQEVALDDVRKEI 166
Cdd:cd02037  78 LL-PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIP---IDGAVVVTTPQEVSLIDVRKAI 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24667611 167 TFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVG 225
Cdd:cd02037 154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELA 212
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
2-254 7.80e-119

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 344.11  E-value: 7.80e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    2 LDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVytDESQTLAV 81
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPV--EYSDNLKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   82 MSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEVGchgAIIVTTPQEVALDD 161
Cdd:NF041136  79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAG---AVIVTTPQELALAD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  162 VRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDS 241
Cdd:NF041136 156 VRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWS 235

                        250
                 ....*....|...
gi 24667611  242 TTAEVLTHIVEKL 254
Cdd:NF041136 236 PAAKALEKIVDPI 248
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
5-258 4.45e-59

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 191.41  E-value: 4.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    5 VKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDifqcddgwvPVYTD-------ESQ 77
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQR---------PTSPDgthmapiMAH 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   78 TLAVMSIGFLLkNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMEclkEVGCHGAIIVTTPQEV 157
Cdd:PRK11670 177 GLATNSIGYLV-TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQ---NIPVTGAVVVTTPQDI 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  158 ALDDVRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLP--IDPRVGILAGTTTSVL 235
Cdd:PRK11670 253 ALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPlhISLREDLDRGTPTVVS 332

                        250       260
                 ....*....|....*....|...
gi 24667611  236 DelPDSTTAEVLTHIVEKLKTML 258
Cdd:PRK11670 333 R--PESEFTAIYRQLADRVAAQL 353
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-190 1.94e-47

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: 159.20  E-value: 1.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   2 LDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGR----DIFQCDDGWVPV-YTDES 76
Cdd:COG0489  88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDViQPTEV 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  77 QTLAVMSIGFLLKNREDPViwrgpkKTMMIRQFLTDVRwDELDYLIIDTPPGTSDEHITVMECLkevgCHGAIIVTTPQE 156
Cdd:COG0489 168 EGLDVLPAGPLPPNPSELL------ASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL----VDGVLLVVRPGK 236

                       170       180       190
                ....*....|....*....|....*....|....
gi 24667611 157 VALDDVRKEITFCKKTGINILGIVENMsgfVCPH 190
Cdd:COG0489 237 TALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 7-161 3.60e-13

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: 67.36  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIF--------QCDDGWVPVYTDESQT 78
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvegECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    79 LAVMSIGfllKNREDPVIwrgPKKTMmirQFLTDVRWDELDYLIIDTPPGTSDEHITVMeclkeVGCHGAIIVTTPQEVA 158
Cdd:TIGR01968  82 LYLLPAS---QTRDKDAV---TPEQM---KKLVNELKEEFDYVIIDCPAGIESGFRNAV-----APADEAIVVTTPEVSA 147


                  ...
gi 24667611   159 LDD 161
Cdd:TIGR01968 148 VRD 150
ParA_partition NF041546
ParA family partition ATPase;
8-44 1.55e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.24  E-value: 1.55e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 24667611    8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDID 44
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 10-61 4.12e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 38.32  E-value: 4.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24667611   10 VVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgPSvPYLLGLEGRDI 61
Cdd:NF041417  15 VFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTD---PA-PNLSDIFGQSI 62
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 4-254 5.78e-141

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: 395.28  E-value: 5.78e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     4 KVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDesqTLAVMS 83
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    84 IGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEvgcHGAIIVTTPQEVALDDVR 163
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPL---TGAVIVTTPQDVALLDVR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   164 KEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDSTT 243
Cdd:pfam10609 155 KAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 24667611   244 AEVLTHIVEKL 254
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 7-225 4.79e-127

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: 359.12  E-value: 4.79e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDEsqtLAVMSIGF 86
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGG---IKVMSIGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  87 LLkNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKevgCHGAIIVTTPQEVALDDVRKEI 166
Cdd:cd02037  78 LL-PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIP---IDGAVVVTTPQEVSLIDVRKAI 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24667611 167 TFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVG 225
Cdd:cd02037 154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELA 212
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
2-254 7.80e-119

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 344.11  E-value: 7.80e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    2 LDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVytDESQTLAV 81
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPV--EYSDNLKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   82 MSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEVGchgAIIVTTPQEVALDD 161
Cdd:NF041136  79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAG---AVIVTTPQELALAD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  162 VRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDS 241
Cdd:NF041136 156 VRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWS 235

                        250
                 ....*....|...
gi 24667611  242 TTAEVLTHIVEKL 254
Cdd:NF041136 236 PAAKALEKIVDPI 248
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
5-258 4.45e-59

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 191.41  E-value: 4.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    5 VKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDifqcddgwvPVYTD-------ESQ 77
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQR---------PTSPDgthmapiMAH 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   78 TLAVMSIGFLLkNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMEclkEVGCHGAIIVTTPQEV 157
Cdd:PRK11670 177 GLATNSIGYLV-TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQ---NIPVTGAVVVTTPQDI 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  158 ALDDVRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLP--IDPRVGILAGTTTSVL 235
Cdd:PRK11670 253 ALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPlhISLREDLDRGTPTVVS 332

                        250       260
                 ....*....|....*....|...
gi 24667611  236 DelPDSTTAEVLTHIVEKLKTML 258
Cdd:PRK11670 333 R--PESEFTAIYRQLADRVAAQL 353
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-190 1.94e-47

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: 159.20  E-value: 1.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   2 LDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGR----DIFQCDDGWVPV-YTDES 76
Cdd:COG0489  88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDViQPTEV 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  77 QTLAVMSIGFLLKNREDPViwrgpkKTMMIRQFLTDVRwDELDYLIIDTPPGTSDEHITVMECLkevgCHGAIIVTTPQE 156
Cdd:COG0489 168 EGLDVLPAGPLPPNPSELL------ASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL----VDGVLLVVRPGK 236

                       170       180       190
                ....*....|....*....|....*....|....
gi 24667611 157 VALDDVRKEITFCKKTGINILGIVENMsgfVCPH 190
Cdd:COG0489 237 TALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 7-254 4.64e-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: 83.02  E-value: 4.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDD---GWVP----VYTDESQT- 78
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDvleGECRleqaLIKDKRWEn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  79 LAVMSIGfllKNREDPVIwrGPKKtmmIRQFLTDVRwDELDYLIIDTPPGTSDEHITVMeclkeVGCHGAIIVTTPQEVA 158
Cdd:cd02036  81 LYLLPAS---QTRDKDAL--TPEK---LEELVKELK-DSFDFILIDSPAGIESGFINAI-----APADEAIIVTNPEISS 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611 159 LDDVRKEITFCKKTGINILGIVENMsgfVCPHCTSCTNIFSSNggvSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDEL 238
Cdd:cd02036 147 VRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSVE---DIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYK 220

                       250
                ....*....|....*.
gi 24667611 239 PDSTTAEVLTHIVEKL 254
Cdd:cd02036 221 PNSLAAKAFENIARRL 236
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 7-161 2.60e-18

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


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 81.08  E-value: 2.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLegrdifqcddgwVPVYTdesqtlavmsIGF 86
Cdd:cd02038   1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGL------------APKKT----------LGD 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  87 LLKNR---EDpVIWRGPK-----------------KTMMIRQFLTDVR--WDELDYLIIDTPPGTSDEHITVMECLKEVg 144
Cdd:cd02038  59 VLKGRvslED-IIVEGPEgldiipggsgmeelanlDPEQKAKLIEELSslESNYDYLLIDTGAGISRNVLDFLLAADEV- 136

                       170
                ....*....|....*..
gi 24667611 145 chgaIIVTTPQEVALDD 161
Cdd:cd02038 137 ----IVVTTPEPTSITD 149
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 9-187 1.06e-15

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: 73.92  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDI-FQ------CDDGWVP--VYTDESQTL 79
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPaLQalaeglKGRVNLDpiLLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    80 AVMSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRwDELDYLIIDTPPGTSDEHITVMeclkeVGCHGAIIVTTPQEVAL 159
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGELLRNAL-----IAADYVIIPLEPEVILV 154

                         170       180
                  ....*....|....*....|....*...
gi 24667611   160 DDVRKEITFCKKTGINILGIVENMSGFV 187
Cdd:pfam01656 155 EDAKRLGGVIAALVGGYALLGLKIIGVV 182
minD CHL00175
septum-site determining protein; Validated
 8-174 7.82e-15

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 72.50  E-value: 7.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGR------DIF--QCDDGWVPVYTDESQTL 79
Cdd:CHL00175  17 IIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRvlytamDVLegECRLDQALIRDKRWKNL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   80 AVMSIGfllKNRE-DPVIwrgpKKTMmirQFLTD-VRWDELDYLIIDTPPGTSDEHITVMECLKEvgchgAIIVTTPQEV 157
Cdd:CHL00175  97 SLLAIS---KNRQrYNVT----RKNM---NMLVDsLKNRGYDYILIDCPAGIDVGFINAIAPAQE-----AIVVTTPEIT 161

                        170
                 ....*....|....*..
gi 24667611  158 ALDDVRKEITFCKKTGI 174
Cdd:CHL00175 162 AIRDADRVAGLLEANGI 178
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 8-254 1.37e-14

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: 72.45  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   8 VIVVLSGKGGVGKSTVSTQLSLAL-RKNGFKVGLLDIDLCGPSVPYLLGLEGRD-----IFQCDDgwvpvyTDES---QT 78
Cdd:COG4963 104 VIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFGDVALYLDLEPRRgladaLRNPDR------LDETlldRA 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  79 LAVMSIGF-LLKNREDPVIWRGPKKTmMIRQFLTDVRwDELDYLIIDTPPGTSDEHITVMECLKEVgchgaIIVTTPQEV 157
Cdd:COG4963 178 LTRHSSGLsVLAAPADLERAEEVSPE-AVERLLDLLR-RHFDYVVVDLPRGLNPWTLAALEAADEV-----VLVTEPDLP 250

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611 158 ALDDVRKEITFCKKTGINI--LGIVENMsgfvcphctsctniFSSNGGVSLATYAQ---VPHLGTLPIDPRVGILA---G 229
Cdd:COG4963 251 SLRNAKRLLDLLRELGLPDdkVRLVLNR--------------VPKRGEISAKDIEEalgLPVAAVLPNDPKAVAEAanqG 316

                       250       260
                ....*....|....*....|....*
gi 24667611 230 TTtsVLDELPDSTTAEVLTHIVEKL 254
Cdd:COG4963 317 RP--LAEVAPKSPLAKAIRKLAARL 339
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 7-161 3.60e-13

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: 67.36  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIF--------QCDDGWVPVYTDESQT 78
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvegECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    79 LAVMSIGfllKNREDPVIwrgPKKTMmirQFLTDVRWDELDYLIIDTPPGTSDEHITVMeclkeVGCHGAIIVTTPQEVA 158
Cdd:TIGR01968  82 LYLLPAS---QTRDKDAV---TPEQM---KKLVNELKEEFDYVIIDCPAGIESGFRNAV-----APADEAIVVTTPEVSA 147


                  ...
gi 24667611   159 LDD 161
Cdd:TIGR01968 148 VRD 150
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 22-254 5.81e-13

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: 66.45  E-value: 5.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  22 TVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLE-GRDIFQCDDGWVPVY---TDESQTLAVMSIGfllknrEDPVIW 97
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEpKATLADVLAGEADLEdaiVQGPGGLDVLPGG------SGPAEL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  98 RGPKKTMMIRQFLTDVRwDELDYLIIDTPPGTSDEhitVMECLKEvgCHGAIIVTTPQEVALDDVRKEI-TFCKKTGINI 176
Cdd:COG0455  75 AELDPEERLIRVLEELE-RFYDVVLVDTGAGISDS---VLLFLAA--ADEVVVVTTPEPTSITDAYALLkLLRRRLGVRR 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611 177 LGIVENMsgfvcphctsctnifSSNGGVSLATYAQV------------PHLGTLPIDPRVGILAGTTTSVLDELPDSTTA 244
Cdd:COG0455 149 AGVVVNR---------------VRSEAEARDVFERLeqvaerflgvrlRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAA 213

                       250
                ....*....|
gi 24667611 245 EVLTHIVEKL 254
Cdd:COG0455 214 RAIRELAARL 223
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-182 4.12e-12

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 63.36  E-value: 4.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   1 MLDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRD-----IFQCDDGWVPVYTDE 75
Cdd:cd05387  14 GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPglsevLSGQASLEDVIQSTN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  76 SQTLAVMSIGfllKNREDPviwrgpkktmmiRQFLTDVRWDEL--------DYLIIDTPP--GTSDEHItvmeclkeVG- 144
Cdd:cd05387  94 IPNLDVLPAG---TVPPNP------------SELLSSPRFAELleelkeqyDYVIIDTPPvlAVADALI--------LAp 150

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24667611 145 -CHGAIIVTTPQEVALDDVRKEITFCKKTGINILGIVEN 182
Cdd:cd05387 151 lVDGVLLVVRAGKTRRREVKEALERLEQAGAKVLGVVLN 189
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 8-183 5.63e-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: 63.72  E-value: 5.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGpSVPYLLGLEGRDIFQC------DDGWVP--VYTDESQTL 79
Cdd:COG1192   3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGLGLDPDDLDPTlydlllDDAPLEdaIVPTEIPGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  80 AVMSIGFLLKNREDPVIwRGPKKTMMIRQFLTDVRwDELDYLIIDTPPGTSDEHITVMeclkeVGCHGAIIVTTPQEVAL 159
Cdd:COG1192  82 DLIPANIDLAGAEIELV-SRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNAL-----AAADSVLIPVQPEYLSL 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 24667611 160 ----------DDVRKEItfckKTGINILGIVENM 183
Cdd:COG1192 155 eglaqlletiEEVREDL----NPKLEILGILLTM 184
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 8-183 1.42e-09

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: 54.85  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgpsvpyllglegrdiFQCDdgwvpvytdesqtlavmsigfl 87
Cdd:cd02042   2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD-----------------PQGS---------------------- 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  88 lknredpviwrgpkktmmirqfLTDVRWdelDYLIIDTPPGTSDEHITVMeclkeVGCHGAIIVTTPQEVALDDVRKEIT 167
Cdd:cd02042  43 ----------------------LTSWLY---DYILIDTPPSLGLLTRNAL-----AAADLVLIPVQPSPFDLDGLAKLLD 92

                       170       180
                ....*....|....*....|..
gi 24667611 168 FCKKTGIN------ILGIVENM 183
Cdd:cd02042  93 TLEELKKQlnppllILGILLTR 114
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 8-62 3.77e-09

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 55.83  E-value: 3.77e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667611   8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKV-------GLLDIDLcgpsvpyLLGLEGRDIF 62
Cdd:COG2894   4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVvlidadiGLRNLDL-------VMGLENRIVY 58
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-182 1.98e-08

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 53.21  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     3 DKVKnVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDdgWVPVYTDESQTLAVM 82
Cdd:TIGR01007  15 AEIK-VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTN--FLSGTTDLSDAICDT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    83 SIGFLLKNREDPViwrGPKKTMMI--RQF--LTDVRWDELDYLIIDTPP-GT-SDEHITVMEclkevgCHGAIIVTTPQE 156
Cdd:TIGR01007  92 NIENLDVITAGPV---PPNPTELLqsSNFktLIETLRKRFDYIIIDTPPiGTvTDAAIIARA------CDASILVTDAGK 162

                         170       180
                  ....*....|....*....|....*.
gi 24667611   157 VALDDVRKEITFCKKTGINILGIVEN 182
Cdd:TIGR01007 163 IKKREVKKAKEQLEQAGSNFLGVVLN 188
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 9-185 5.13e-08

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 52.39  E-value: 5.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   9 IVVLSGKGGVGKSTVSTQLSLALRkngfKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDE--------SQTLA 80
Cdd:cd03110   2 IAVLSGKGGTGKTTITANLAVLLY----NVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncERVCK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  81 VMSIGFLLKNRE-DPVIWRG--------PKKTMMIRQFLT------------------------------------DVRW 115
Cdd:cd03110  78 FGAILEFFQKLIvDESLCEGcgacviicPRGAIYLKDRDTgkifisssdggplvhgrlnigeensgklvtelrkkaLERS 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611 116 DELDYLIIDTPPGTsdeHITVMECLKevGCHGAIIVTTPQEVALDDVRKEITFCKKTGINiLGIVENMSG 185
Cdd:cd03110 158 KECDLAIIDGPPGT---GCPVVASIT--GADAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD 221
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 8-252 6.37e-08

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: 51.89  E-value: 6.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   8 VIVVLSGKGGVGKSTVSTQLSLAL-RKNGFKVGLLDIDLCGPSVPYLLGLEGR----DIFQCDDGWVPVYTDESqtLAVM 82
Cdd:cd03111   2 VVAVVGAKGGVGASTLAVNLAQELaQRAKDKVLLIDLDLPFGDLGLYLNLRPDydlaDVIQNLDRLDRTLLDSA--VTRH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611  83 SIGFLL----KNREDPVIWRGPKKTMMI---RQFltdvrwdeLDYLIIDTPPGTSDEHITVMECLKEVgchgaIIVTTPQ 155
Cdd:cd03111  80 SSGLSLlpapQELEDLEALGAEQVDKLLqvlRAF--------YDHIIVDLGHFLDEVTLAVLEAADEI-----LLVTQQD 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611 156 EVALDDVRKEITFCKKTGINI--LGIVenmsgfvcphctscTNIFSSNGGVSLATYAQV---PHLGTLPIDPR-VGILAG 229
Cdd:cd03111 147 LPSLRNARRLLDSLRELEGSSdrLRLV--------------LNRYDKKSEISPKDIEEAlglEVFATLPNDYKaVSESAN 212

                       250       260
                ....*....|....*....|...
gi 24667611 230 TTTSVLDELPDSTTAEVLTHIVE 252
Cdd:cd03111 213 TGRPLVEVAPRSALVRALQDLAA 235
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 8-127 8.48e-08

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


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 50.66  E-value: 8.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYlLGLE----GRDIFQCDDGWVP----VYTDESQTL 79
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSG-LGIDknnvEKTIYELLIGECNieeaIIKTVIENL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 24667611    80 AVMSIGFLLKNREDPVIWRGPKKTMMIRQfLTDVRwDELDYLIIDTPP 127
Cdd:pfam13614  82 DLIPSNIDLAGAEIELIGIENRENILKEA-LEPVK-DNYDYIIIDCPP 127
ParA_partition NF041546
ParA family partition ATPase;
8-44 1.55e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.24  E-value: 1.55e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 24667611    8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDID 44
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
PRK10818 PRK10818
septum site-determining protein MinD;
8-184 6.66e-07

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 49.17  E-value: 6.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQcddgwvpvYTDESQTLAVMSIGFL 87
Cdd:PRK10818   4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYD--------FVNVIQGDATLNQALI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   88 LKNRED-----PVIWRGPKKTMM---IRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEvgchgAIIVTTPQEVAL 159
Cdd:PRK10818  76 KDKRTEnlyilPASQTRDKDALTregVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADE-----AIITTNPEVSSV 150

                        170       180
                 ....*....|....*....|....*
gi 24667611  160 DDVRKeitfckktginILGIVENMS 184
Cdd:PRK10818 151 RDSDR-----------ILGILASKS 164
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 7-44 1.09e-06

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 46.27  E-value: 1.09e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24667611   7 NVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDID 44
Cdd:cd01983   1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 8-45 3.41e-06

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: 47.06  E-value: 3.41e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 24667611     8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDL 45
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDL 39
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
9-127 6.81e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 46.35  E-value: 6.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgP--SVPYLLGLEgrdifqCDDGWVPVYTDEsqtLAVMSIgf 86
Cdd:COG0003   5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTD---PahSLGDVLGTE------LGNEPTEVAVPN---LYALEI-- 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667611  87 llknreDPVIW--------RGPKKTMM-----------------------IRQFLTDVRWdelDYLIIDTPP 127
Cdd:COG0003  71 ------DPEAEleeywervRAPLRGLLpsagvdelaeslpgteelaaldeLLELLEEGEY---DVIVVDTAP 133
PHA02518 PHA02518
ParA-like protein; Provisional
 8-44 7.44e-06

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 45.61  E-value: 7.44e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 24667611    8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDID 44
Cdd:PHA02518   2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 9-57 1.50e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.08  E-value: 1.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24667611   9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVgLL---DIDLCgpsVPYLLGLE 57
Cdd:COG3640   2 KIAVAGKGGVGKTTLSALLARYLAEKGKPV-LAvdaDPNAN---LAEALGLE 49
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 2-55 3.35e-04

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 41.02  E-value: 3.35e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24667611   2 LDKVKNVIVV-LSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgPSVPY----LLG 55
Cdd:cd03114  40 LPQAGRAFRVgITGPPGAGKSTLIEALGRLLREQGHRVAVLAVD---PSSPRsggsILG 95
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 9-127 3.98e-04

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 40.80  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgPSvPYLlglegRDIFQCDDGWVPVYTDESqtLAVMSI---- 84
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTD---PA-HSL-----SDSFNQKFGHEPTKVKEN--LSAMEIdpnm 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667611    85 ------GFLLKNREDPVIWRGPKKTM----MIR----------QFLTDVRWDELDYLIIDTPP 127
Cdd:pfam02374  72 eleeywQEVQKYMNALLGLRMLEGILaeelASLpgideaasfdEFKKYMDEGEYDVVVFDTAP 134
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 10-57 4.04e-04

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: 40.76  E-value: 4.04e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24667611  10 VVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlCGPSVPYLLGLE 57
Cdd:cd02034   3 IAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDAD-PNSNLAETLGVE 49
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 1-182 5.48e-04

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: 41.24  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611     1 MLDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGR----DIFQCDDGW-VPVYTDE 75
Cdd:TIGR01005 548 LADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKpgllDLLAGEASIeAGIHRDQ 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611    76 SQTLAVMSIGFLLKNREDPV-IWRGPKKTMMIRQFLTdvrwdELDYLIIDTPPGTSDEHITVMECLKEvgchGAIIVTTP 154
Cdd:TIGR01005 628 RPGLAFIAAGGASHFPHNPNeLLANPAMAELIDNARN-----AFDLVLVDLAALAAVADAAAFAALAD----GILFVTEF 698

                         170       180
                  ....*....|....*....|....*...
gi 24667611   155 QEVALDDVRKEITFCKKTGINILGIVEN 182
Cdd:TIGR01005 699 ERSPLGEIRDLIHQEPHANSDVLGVIFN 726
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-40 6.44e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.84  E-value: 6.44e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 24667611     9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVGL 40
Cdd:TIGR04291 323 LIMTMGKGGVGKTTVAAAIAVRLANKGLDVHL 354
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 14-38 1.30e-03

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: 39.20  E-value: 1.30e-03
                        10        20
                ....*....|....*....|....*
gi 24667611  14 GKGGVGKSTVSTQLSLALRKNGFKV 38
Cdd:cd02032   7 GKGGIGKSTTSSNLSAAFAKRGKKV 31
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 14-38 1.32e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 39.18  E-value: 1.32e-03
                         10        20
                 ....*....|....*....|....*
gi 24667611   14 GKGGVGKSTVSTQLSLALRKNGFKV 38
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKV 33
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 8-51 1.70e-03

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 38.89  E-value: 1.70e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24667611   8 VIVVLsGKGGVGKSTVSTQLSLALRKNGFKVGLLDID--------LCGPSVP 51
Cdd:cd02117   2 SIVVY-GKGGIGKSTTASNLSAALAEGGKKVLHVGCDpkhdstllLTGGKVP 52
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 8-138 2.08e-03

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 38.29  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667611   8 VIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGpSVPYLLGLEGRdiFQCDDGWVPVYTDESQTLAVMSIgfL 87
Cdd:cd17869   5 VITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQ-STDVFFGASGR--YLMSDHLYTLKSRKANLADKLES--C 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667611  88 LKNREDPVIWRGP----------KKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVME 138
Cdd:cd17869  80 VKQHESGVYYFSPfksaldileiKKDDILHMITKLVEAHAYDYIIMDLSFEFSSTVCKLLQ 140
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 9-38 2.68e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 38.26  E-value: 2.68e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 24667611   9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKV 38
Cdd:cd02035   2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRV 31
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 9-63 3.27e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.48  E-value: 3.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24667611     9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQ 63
Cdd:pfam13191  26 SVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTREGLLR 80
chlL CHL00072
photochlorophyllide reductase subunit L
 14-38 3.47e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.18  E-value: 3.47e-03
                         10        20
                 ....*....|....*....|....*
gi 24667611   14 GKGGVGKSTVSTQLSLALRKNGFKV 38
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKV 31
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 10-61 4.12e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 38.32  E-value: 4.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24667611   10 VVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgPSvPYLLGLEGRDI 61
Cdd:NF041417  15 VFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTD---PA-PNLSDIFGQSI 62
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
 1-38 7.52e-03

Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion transport and metabolism];


Pssm-ID: 441959  Cd Length: 441  Bit Score: 37.12  E-value: 7.52e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24667611   1 MLDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKV 38
Cdd:COG2403 114 MLKSSKPVIAVCAVRTGCGKSQTSRKVARILKERGLKV 151
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 9-41 7.55e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 35.99  E-value: 7.55e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 24667611   9 IVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLL 41
Cdd:cd17933  14 VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLA 46
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
 12-52 8.79e-03

Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.


Pssm-ID: 281323 [Multi-domain]  Cd Length: 272  Bit Score: 36.64  E-value: 8.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 24667611    12 LSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDlcgPSVPY 52
Cdd:pfam03308  38 VTGVPGAGKSTLIEALGMELRRRGHRVAVLAVD---PSSPR 75
 
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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