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Conserved domains on  [gi|1119673244|ref|WP_072592533|]
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MULTISPECIES: flagellum location/number ATPase FlhG [Bacillus]

Protein Classification

MinD/ParA family protein( domain architecture ID 10114187)

MinD/ParA family protein similar to flagellum site-determining protein FlhG (also known as YlxH, FleN, MinD2, or MotR), an MinD-like ATPase that regulates location and number of bacterial flagella during C-ring assembly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 32-261 3.83e-107

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: 310.66  E-value: 3.83e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSLSIGPKGLRYI 111
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPEGLDII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 112 SGGTGLDVMFQLDQRKWTFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSAVKHLVLT 191
Cdd:cd02038    81 PGGSGMEELANLDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKVLSRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 192 ENKLSMKVAVNRCRDQKEGLDAFARLSRTIHMFLDVQVQFAGSVSDDVIVSKAVVEQVPFFIKSPQAKAS 261
Cdd:cd02038   161 GGKKNFRLIVNMARSPKEGRATFERLKKVAKRFLDINLDFVGFIPYDQSVRRAVRSQKPFVLLFPNSKAS 230
 
Name Accession Description Interval E-value
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 32-261 3.83e-107

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: 310.66  E-value: 3.83e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSLSIGPKGLRYI 111
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPEGLDII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 112 SGGTGLDVMFQLDQRKWTFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSAVKHLVLT 191
Cdd:cd02038    81 PGGSGMEELANLDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKVLSRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 192 ENKLSMKVAVNRCRDQKEGLDAFARLSRTIHMFLDVQVQFAGSVSDDVIVSKAVVEQVPFFIKSPQAKAS 261
Cdd:cd02038   161 GGKKNFRLIVNMARSPKEGRATFERLKKVAKRFLDINLDFVGFIPYDQSVRRAVRSQKPFVLLFPNSKAS 230
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 47-278 4.77e-69

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: 213.98  E-value: 4.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  47 NITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSLSIGPKGLRYISGGTGLDVMFQLDQR 126
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAELDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 127 KWtfFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSAVKHLVLTENKLSMKVAVNRCRD 206
Cdd:COG0455    81 ER--LIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRRAGVVVNRVRS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119673244 207 QKEGLDAFARLSRTIHMFLDVQVQFAGSVSDDVIVSKAVVEQVPFFIKSPQAKASRSVRILADALFGREETR 278
Cdd:COG0455   159 EAEARDVFERLEQVAERFLGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWPVPE 230
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 32-290 1.89e-33

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


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 122.92  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG-NSSSATIIDVLTDRKPLLQSLSIGPKGLRY 110
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGmEDKPVTLHDVLAGEADIKDAIYEGPFGVKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 111 ISGGTGLDVMFQLDQRKwtfFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDaysAVKHLVL 190
Cdd:TIGR01969  81 IPAGVSLEGLRKADPDK---LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITD---ALKTKIV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 191 TE--NKLSMKVAVNRC-RDQKEgldafarLSR-TIHMFLDVQVqfAGSVSDDVIVSKAVVEQVPFFIKSPQAKASRSVRI 266
Cdd:TIGR01969 155 AEklGTAILGVVLNRVtRDKTE-------LGReEIETILEVPV--LGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFME 225

                         250       260
                  ....*....|....*....|....
gi 1119673244 267 LADALFGREETRHKEDKQTFIEKL 290
Cdd:TIGR01969 226 LAAELAGIEYEPKEPKKEGFIAKV 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 34-251 5.63e-23

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: 94.33  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  34 LAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGN-------IDILIGNSSSATIIDVLTDRKPLLQSLSIGPK 106
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNssvegleGDIAPALQALAEGLKGRVNLDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 107 GLRYISGGTGLDVMFQLDQ--RKWTFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSA 184
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLgpRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119673244 185 ---VKHLVLTENKLSMKVA---VNRCRDQKEGL---DAFARLSRtihmfldvQVQFAGSVSDDVIVSKAVVEQVPF 251
Cdd:pfam01656 161 ggvIAALVGGYALLGLKIIgvvLNKVDGDNHGKllkEALEELLR--------GLPVLGVIPRDEAVAEAPARGLPV 228
minD CHL00175
septum-site determining protein; Validated
 27-207 1.10e-18

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 83.67  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  27 YSQKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG--NSSSATIIDVLT------------ 92
Cdd:CHL00175   11 SATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGleNRVLYTAMDVLEgecrldqalird 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  93 DRKPLLQSLSIGPKGLRYisggtgldvmfQLDQRKWTFFANELshALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITT 172
Cdd:CHL00175   91 KRWKNLSLLAISKNRQRY-----------NVTRKNMNMLVDSL--KNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTT 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1119673244 173 PEPTAILDAySAVKHLVLTENKLSMKVAVNRCRDQ 207
Cdd:CHL00175  158 PEITAIRDA-DRVAGLLEANGIYNVKLLVNRVRPD 191
ParA_partition NF041546
ParA family partition ATPase;
33-69 6.14e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 54.87  E-value: 6.14e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1119673244  33 TLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
 
Name Accession Description Interval E-value
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 32-261 3.83e-107

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: 310.66  E-value: 3.83e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSLSIGPKGLRYI 111
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPEGLDII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 112 SGGTGLDVMFQLDQRKWTFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSAVKHLVLT 191
Cdd:cd02038    81 PGGSGMEELANLDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKVLSRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 192 ENKLSMKVAVNRCRDQKEGLDAFARLSRTIHMFLDVQVQFAGSVSDDVIVSKAVVEQVPFFIKSPQAKAS 261
Cdd:cd02038   161 GGKKNFRLIVNMARSPKEGRATFERLKKVAKRFLDINLDFVGFIPYDQSVRRAVRSQKPFVLLFPNSKAS 230
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 47-278 4.77e-69

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: 213.98  E-value: 4.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  47 NITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSLSIGPKGLRYISGGTGLDVMFQLDQR 126
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAELDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 127 KWtfFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSAVKHLVLTENKLSMKVAVNRCRD 206
Cdd:COG0455    81 ER--LIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRRAGVVVNRVRS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119673244 207 QKEGLDAFARLSRTIHMFLDVQVQFAGSVSDDVIVSKAVVEQVPFFIKSPQAKASRSVRILADALFGREETR 278
Cdd:COG0455   159 EAEARDVFERLEQVAERFLGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWPVPE 230
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 32-290 1.89e-33

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


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 122.92  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG-NSSSATIIDVLTDRKPLLQSLSIGPKGLRY 110
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGmEDKPVTLHDVLAGEADIKDAIYEGPFGVKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 111 ISGGTGLDVMFQLDQRKwtfFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDaysAVKHLVL 190
Cdd:TIGR01969  81 IPAGVSLEGLRKADPDK---LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITD---ALKTKIV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 191 TE--NKLSMKVAVNRC-RDQKEgldafarLSR-TIHMFLDVQVqfAGSVSDDVIVSKAVVEQVPFFIKSPQAKASRSVRI 266
Cdd:TIGR01969 155 AEklGTAILGVVLNRVtRDKTE-------LGReEIETILEVPV--LGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFME 225

                         250       260
                  ....*....|....*....|....
gi 1119673244 267 LADALFGREETRHKEDKQTFIEKL 290
Cdd:TIGR01969 226 LAAELAGIEYEPKEPKKEGFIAKV 249
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 32-271 1.42e-29

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: 112.30  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG--NSSSATIIDVLTDRKPLLQSLSIGP--KG 107
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGleNRIVYTLVDVLEGECRLEQALIKDKrwEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 108 LRYISGGTGLDvMFQLDQRKWTFFANELShalSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDaysAVKH 187
Cdd:cd02036    81 LYLLPASQTRD-KDALTPEKLEELVKELK---DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRD---ADRV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 188 LVLTENK--LSMKVAVNRCRDQkegldaFARLSRTIHMfLDVQ----VQFAGSVSDDVIVSKAVVEQVPFFIKSPQAKAS 261
Cdd:cd02036   154 IGLLESKgiVNIGLIVNRYRPE------MVKSGDMLSV-EDIQeilgIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAA 226

                         250
                  ....*....|
gi 1119673244 262 RSVRILADAL 271
Cdd:cd02036   227 KAFENIARRL 236
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 20-290 3.43e-26

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: 105.97  E-value: 3.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  20 ERVLPMVYSQKAKTLAVISGKGGVGKSNITLNMALAL-QDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLT-----D 93
Cdd:COG4963    91 ARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRnpdrlD 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  94 RKPLLQSLSIGPKGLRYISGGTGLDVMFQLDQRkwtFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTP 173
Cdd:COG4963   171 ETLLDRALTRHSSGLSVLAAPADLERAEEVSPE---AVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 174 EPTAILDAYSAVKHLV-LTENKLSMKVAVNRCrDQKEGLDAfARLSRTIHMFLDVQVQFagsvsDDVIVSKAVVEQVPFF 252
Cdd:COG4963   248 DLPSLRNAKRLLDLLReLGLPDDKVRLVLNRV-PKRGEISA-KDIEEALGLPVAAVLPN-----DPKAVAEAANQGRPLA 320

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1119673244 253 IKSPQAKASRSVRILADALFGREETRHKEDKQTFIEKL 290
Cdd:COG4963   321 EVAPKSPLAKAIRKLAARLTGRPAAAAAKAGGKLLKRL 358
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 34-251 5.63e-23

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: 94.33  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  34 LAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGN-------IDILIGNSSSATIIDVLTDRKPLLQSLSIGPK 106
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNssvegleGDIAPALQALAEGLKGRVNLDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 107 GLRYISGGTGLDVMFQLDQ--RKWTFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSA 184
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLgpRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119673244 185 ---VKHLVLTENKLSMKVA---VNRCRDQKEGL---DAFARLSRtihmfldvQVQFAGSVSDDVIVSKAVVEQVPF 251
Cdd:pfam01656 161 ggvIAALVGGYALLGLKIIgvvLNKVDGDNHGKllkEALEELLR--------GLPVLGVIPRDEAVAEAPARGLPV 228
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 31-294 3.08e-22

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: 93.17  E-value: 3.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  31 AKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG--NSSSATIIDVLTDRKPLLQSLsIGPKGL 108
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGleNRIVYTLVDVVEGECRLQQAL-IKDKRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 109 R--YISGGTGLDVMFQLDQRKWTFFANELshaLSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAySAVK 186
Cdd:TIGR01968  80 KnlYLLPASQTRDKDAVTPEQMKKLVNEL---KEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDA-DRVI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 187 HLVLTENKLSMKVAVNRCRDQKEGLDAFARLSRTIHMfldVQVQFAGSVSDD--VIVSKAVVEQVpffIKSPQAKASRSV 264
Cdd:TIGR01968 156 GLLEAKGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEI---LSIPLIGVIPEDeaIIVSTNKGEPV---VLNDKSRAGKAF 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1119673244 265 RILADALFGREE--TRHKEDKQTFIEKLSSFL 294
Cdd:TIGR01968 230 ENIARRILGEEVpfEDLTTQKKGFFARIKRFF 261
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 19-188 1.78e-19

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: 86.01  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  19 RERVLPMVYSQKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLL 98
Cdd:COG0489    80 LLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  99 QSL-SIGPKGLRYISGG------TGLdvmfqLDQRKWTFFANELShalSQFDYVLFDMGAGLSKDQLPFILSAED-ILII 170
Cdd:COG0489   160 DVIqPTEVEGLDVLPAGplppnpSEL-----LASKRLKQLLEELR---GRYDYVIIDTPPGLGVADATLLASLVDgVLLV 231

                         170
                  ....*....|....*...
gi 1119673244 171 TTPEPTAILDAYSAVKHL 188
Cdd:COG0489   232 VRPGKTALDDVRKALEML 249
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 31-276 1.85e-19

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: 85.29  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  31 AKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDiGMGNIDILIG---NSSSATIIDVLTDRKPLLQSL-SIGPK 106
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLD-PQGNLTSGLGldpDDLDPTLYDLLLDDAPLEDAIvPTEIP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 107 GLRYISGGT---GLDVMFQLDQRKWTFFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAiLDAYS 183
Cdd:COG1192    80 GLDLIPANIdlaGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLS-LEGLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 184 AvkhlvLTENKLSMKVAVNRcRDQKEGL-----DAFARLSR----TIHMFLDVQVqFAGSVSDDVIVSKAVVEQVPFFIK 254
Cdd:COG1192   159 Q-----LLETIEEVREDLNP-KLEILGIlltmvDPRTRLSRevleELREEFGDKV-LDTVIPRSVALAEAPSAGKPVFEY 231

                         250       260
                  ....*....|....*....|..
gi 1119673244 255 SPQAKASRSVRILADALFGREE 276
Cdd:COG1192   232 DPKSKGAKAYRALAEELLERLE 253
minD CHL00175
septum-site determining protein; Validated
 27-207 1.10e-18

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 83.67  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  27 YSQKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG--NSSSATIIDVLT------------ 92
Cdd:CHL00175   11 SATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGleNRVLYTAMDVLEgecrldqalird 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  93 DRKPLLQSLSIGPKGLRYisggtgldvmfQLDQRKWTFFANELshALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITT 172
Cdd:CHL00175   91 KRWKNLSLLAISKNRQRY-----------NVTRKNMNMLVDSL--KNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTT 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1119673244 173 PEPTAILDAySAVKHLVLTENKLSMKVAVNRCRDQ 207
Cdd:CHL00175  158 PEITAIRDA-DRVAGLLEANGIYNVKLLVNRVRPD 191
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 31-181 1.62e-16

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 77.40  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  31 AKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIG--NSSSATIIDVLTDRKPLLQSL------- 101
Cdd:COG2894     2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGleNRIVYDLVDVIEGECRLKQALikdkrfe 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 102 --------------SIGPKGLRYIsggtgldvmfqldqrkwtffANELShalSQFDYVLFDMGAGLSKDQLPFILSAEDI 167
Cdd:COG2894    82 nlyllpasqtrdkdALTPEQMKKL--------------------VEELK---EEFDYILIDSPAGIEQGFKNAIAGADEA 138

                         170
                  ....*....|....
gi 1119673244 168 LIITTPEPTAILDA 181
Cdd:COG2894   139 IVVTTPEVSSVRDA 152
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 35-269 2.48e-15

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: 73.47  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  35 AVISGKGGVGKSNITLNMALALQDKGK-KVLLIDLDIGMGNIDILIGNSSSATIIDVLT-----DRKPLLQSLSIGPKGL 108
Cdd:cd03111     4 AVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQnldrlDRTLLDSAVTRHSSGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 109 RYISGGTGLDVMFQLDqrkwtffANELSHAL----SQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDAYSA 184
Cdd:cd03111    84 SLLPAPQELEDLEALG-------AEQVDKLLqvlrAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 185 VKHLVLTE-NKLSMKVAVNR-CRDQKEGLDAFARLsrtihmfldVQVQFAGSVSDD-VIVSKAVVEQVPFFIKSPQAKAS 261
Cdd:cd03111   157 LDSLRELEgSSDRLRLVLNRyDKKSEISPKDIEEA---------LGLEVFATLPNDyKAVSESANTGRPLVEVAPRSALV 227


                  ....*...
gi 1119673244 262 RSVRILAD 269
Cdd:cd03111   228 RALQDLAA 235
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 32-271 3.35e-15

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: 73.26  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDI-G-----MGNIDILIGNSSSATIIDVLTDRkplLQSLSIGp 105
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIyGpsiprMLGLEGERPEQSDGGIIPVEAHG---IKVMSIG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 106 kglryisggtgldvmFQLDQRkwtffaNE--------LSHALSQF---------DYVLFDM--GAG---LSKDQLpfiLS 163
Cdd:pfam10609  80 ---------------FLLPDE------DDaviwrgpmKSGAIKQFltdvdwgelDYLIIDLppGTGdeqLTLAQL---LP 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 164 AEDILIITTPEPTAILDAYSAV----KH----LVLTENklsMKVAVnrCRDQKEGLDAF-----ARLSRtihmflDVQVQ 230
Cdd:pfam10609 136 LTGAVIVTTPQDVALLDVRKAIdmfkKVnvpvLGVVEN---MSYFV--CPHCGEETYIFgkgggEKLAE------ELGVP 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1119673244 231 FAGSVSDDVIVSKAVVEQVPFFIKSPQAKASRSVRILADAL 271
Cdd:pfam10609 205 FLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 34-199 1.27e-14

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: 71.38  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  34 LAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDI-GMgNIDILIGnsssatiidvlTDRKPLLQSlsigPKGLRYIS 112
Cdd:cd02037     3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIyGP-SIPRLLG-----------VEGKPLHQS----EEGIVPVE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 113 GGtGLDVM---FQLDQRK---WtfFANELSHALSQF---------DYVLFDMGAGLSKDQLPfILSAEDI---LIITTPE 174
Cdd:cd02037    67 VG-GIKVMsigFLLPEDDaviW--RGPMKSGAIKQFlkdvdwgelDYLIIDLPPGTGDEHLS-LVQLIPIdgaVVVTTPQ 142

                         170       180
                  ....*....|....*....|....*
gi 1119673244 175 PTAILDAYSAVKHLvlteNKLSMKV 199
Cdd:cd02037   143 EVSLIDVRKAIDMC----KKLNIPV 163
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 31-148 1.77e-11

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: 61.45  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  31 AKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLD------IGMGnidiLIGNSSSATIIDVLTDRKPlLQSLSIG 104
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDpqgnatSGLG----IDKNNVEKTIYELLIGECN-IEEAIIK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1119673244 105 PK--GLRYISGGTGL----DVMFQLDQRKwTFFANELSHALSQFDYVLFD 148
Cdd:pfam13614  76 TVieNLDLIPSNIDLagaeIELIGIENRE-NILKEALEPVKDNYDYIIID 124
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 32-69 2.20e-11

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: 60.25  E-value: 2.20e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
8-201 4.16e-11

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 62.75  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244   8 QAATLrakmeKRERVLPMVYSQKaKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNsssati 87
Cdd:PRK11670   90 NIATL-----KRVNNQPGVNGVK-NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGA------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  88 idvlTDRKPL--------------LQSLSIGpkglryisggtgldvmFQLDQRKWTFFANEL-SHALSQ---------FD 143
Cdd:PRK11670  158 ----EDQRPTspdgthmapimahgLATNSIG----------------YLVTDDNAMVWRGPMaSKALMQmlqetlwpdLD 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119673244 144 YVLFDMGAGLSKDQLPFilsAEDI-----LIITTPEPTAILDaysAVKHLVLTEnklsmKVAV 201
Cdd:PRK11670  218 YLVLDMPPGTGDIQLTL---AQNIpvtgaVVVTTPQDIALID---AKKGIVMFE-----KVEV 269
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 29-172 9.66e-11

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: 59.89  E-value: 9.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  29 QKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSL-SIGPKG 107
Cdd:cd05387    17 AGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLSGQASLEDVIqSTNIPN 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119673244 108 LRYISGGTGLDVMFQLDQRKWtfFANELSHALSQFDYVLFDmgaglskdqLPFILSAEDILIITT 172
Cdd:cd05387    97 LDVLPAGTVPPNPSELLSSPR--FAELLEELKEQYDYVIID---------TPPVLAVADALILAP 150
PRK10818 PRK10818
septum site-determining protein MinD;
31-181 1.35e-10

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 60.72  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  31 AKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSAT--IIDVLTDRKPLLQSLsIGPKGL 108
Cdd:PRK10818    2 ARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVydFVNVIQGDATLNQAL-IKDKRT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119673244 109 R--YISGGTGLDVMFQLDQRKWTFFANELSHAlsQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEPTAILDA 181
Cdd:PRK10818   81 EnlYILPASQTRDKDALTREGVAKVLDDLKAM--DFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDS 153
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 36-271 3.43e-09

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: 56.60  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  36 VISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVL----TDRKPLLQSLSI-GPKGLRY 110
Cdd:cd02117     4 VVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLtedgTAEELRREDLLFsGFNGVDC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 111 IS----------GGTGLDVMFQLDQrkwtffanELSHALSQFDYVLFDM---------GAGLSKDQlpfilsAEDILIIT 171
Cdd:cd02117    84 VEaggpepgvgcGGRGIGTMLELLE--------EHGLLDDDYDVVIFDVlgdvvcggfAAPLRRGF------AQKVVIVV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 172 TPEPTAILDAYSAVKhLVLTENKLSMKVA---VNRcRDQKEG--LDAFARL--SRTIHMFLDVQVqfagsVSDDVIVSKA 244
Cdd:cd02117   150 SEELMSLYAANNIVK-AVENYSKNGVRLAglvANL-RDPAGTeeIQAFAAAvgTKILAVIPRDPA-----VRRAELARVT 222

                         250       260
                  ....*....|....*....|....*...
gi 1119673244 245 VVEQVPffiKSPQAKA-SRSVRILADAL 271
Cdd:cd02117   223 VFEHDP---VSPAASEfARLAAKIADAV 247
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
37-181 3.94e-09

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 56.30  E-value: 3.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  37 ISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKP-----LLQSLSIGPKGLRYI 111
Cdd:pfam00142   5 IYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYvedveVEDVVYKGYGGVKCV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 112 -SGG-------------TGLDVMFQLDqrkwtffanelshALSQFDYVLFDM---------GAGLSKDQlpfilsAEDIL 168
Cdd:pfam00142  85 eSGGpepgvgcagrgviTAINLLEELG-------------AYDDLDFVLYDVlgdvvcggfAMPIREGK------AQEIY 145

                         170
                  ....*....|...
gi 1119673244 169 IITTPEPTAILDA 181
Cdd:pfam00142 146 IVTSNEMMALYAA 158
ParA_partition NF041546
ParA family partition ATPase;
33-69 6.14e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 54.87  E-value: 6.14e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1119673244  33 TLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 32-69 6.74e-08

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: 49.74  E-value: 6.74e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PHA02518 PHA02518
ParA-like protein; Provisional
 32-175 1.82e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 50.62  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDigmgnidiliGNSSSATIIDVLTDRKPLLQSLSIGPKglryi 111
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD----------PQGSSTDWAEAREEGEPLIPVVRMGKS----- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119673244 112 sggtgldvmfqldqrkwtfFANELSHALSQFDYVLFDMGAGLSKDQLPFILSAEDILIITTPEP 175
Cdd:PHA02518   66 -------------------IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSP 110
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 34-86 5.18e-07

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 49.69  E-value: 5.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1119673244  34 LAVISGKGGVGKSNITLNMALALqdkgKKVLLIDLDIGMGNIDILIGNSSSAT 86
Cdd:cd03110     2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEEE 50
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 7-104 1.24e-06

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 49.06  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244   7 DQAATLRAKM-EKRERVLPMVYSQKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSA 85
Cdd:cd02033     5 SFDARLRDEAaIEPSLEIPTGPPTKETQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFGGKACP 84

                          90
                  ....*....|....*....
gi 1119673244  86 TIIDVLTDRKPLLQSLSIG 104
Cdd:cd02033    85 TIIETSTRKKLAGEEVKIG 103
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 29-171 3.09e-06

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: 47.15  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  29 QKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDiGMGNIDILIGNSSSATIIDVLTDRKP-------LLQS- 100
Cdd:cd17869     1 DATSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-RLQSTDVFFGASGRYLMSDHLYTLKSrkanladKLESc 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119673244 101 LSIGPKGLRYISGGTGLDVMFQLDQRKWTFFANELSHALSqFDYVLFDMGAGLSKDQLPfILSAEDILIIT 171
Cdd:cd17869    80 VKQHESGVYYFSPFKSALDILEIKKDDILHMITKLVEAHA-YDYIIMDLSFEFSSTVCK-LLQASHNNVVI 148
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 25-195 3.28e-06

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: 48.56  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  25 MVYSQKAKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSATIIDVLTDRKPLLQSLSIG 104
Cdd:TIGR01005 547 ALADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRD 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 105 PK-GLRYISggTGLDVMFQLDQRKWTF---FANELSHALSQFDYVLFDMGAGLS-KDQLPFILSAEDILIITTPEPTAIL 179
Cdd:TIGR01005 627 QRpGLAFIA--AGGASHFPHNPNELLAnpaMAELIDNARNAFDLVLVDLAALAAvADAAAFAALADGILFVTEFERSPLG 704

                         170
                  ....*....|....*.
gi 1119673244 180 DAYSAVKHLVLTENKL 195
Cdd:TIGR01005 705 EIRDLIHQEPHANSDV 720
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 36-73 4.13e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.08  E-value: 4.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1119673244  36 VISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMG 73
Cdd:COG3640     4 AVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 31-69 2.16e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.95  E-value: 2.16e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1119673244  31 AKTLAVIsGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:PRK13185    2 ALVLAVY-GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCD 39
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 37-69 3.01e-05

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 44.60  E-value: 3.01e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1119673244  37 ISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:cd02032     5 VYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCD 37
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 37-181 3.35e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 44.38  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  37 ISGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGNSSSaTIIDVLtdRKPLLQSLSIGP---KGLRYI-- 111
Cdd:PRK13230    6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIP-TVLDVL--REKGIDNLGLEDiiyEGFNGIyc 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119673244 112 --SGG-------TGLDVMFQLDQRKWTFFANELSHALSQFDyVLFDMGAGLSKDQLPFILsAEDILIITTPEPTAILDA 181
Cdd:PRK13230   83 veSGGpepgygcAGRGVITAIDLLKKLGVFEELGPDVVIYD-ILGDVVCGGFAMPLQKGL-ADDVYIVTTCDPMAIYAA 159
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 38-69 6.27e-05

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 44.31  E-value: 6.27e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1119673244  38 SGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:TIGR04291   9 TGKGGVGKTSIACATAINLADQGKRVLLVSTD 40
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 38-226 6.38e-05

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: 43.65  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  38 SGKGGVGKSNITLNMALALQDKGKKVLLIDLDIG--MGNI-DILIGNSSSATIID----------VLTDR------KPLL 98
Cdd:cd02035     6 GGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAhsLSDAfGQKLGGETPVKGAPnlwameidpeEALEEyweevkELLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  99 QSLSIGPKGLRYI---SGGTGLDVMFQLdqrkwtffaNELSHAL--SQFDYVLFDmGAG-------LSkdqLPF-----I 161
Cdd:cd02035    86 QYLRLPGLDEVYAeelLSLPGMDEAAAF---------DELREYVesGEYDVIVFD-TAPtghtlrlLS---LPLeqvreL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119673244 162 LSAED---ILIITTPEPTAILDAYSAVKHLvlteNKLSMKVA---VNRCRDQKEGLDAFARLSRTIHMFLD 226
Cdd:cd02035   153 LRDPErttFVLVTIPEKLSIYETERLWGEL----QQYGIPVDgvvVNQVLPEEADDSFFLRRRRQQQKYLD 219
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 37-66 8.49e-05

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 43.27  E-value: 8.49e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1119673244  37 ISGKGGVGKSNITLNMALALQDKGKKVLLI 66
Cdd:cd02040     5 IYGKGGIGKSTTASNLSAALAEMGKKVLHV 34
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 36-69 1.57e-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: 42.30  E-value: 1.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1119673244  36 VISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:cd02034     4 AVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDAD 37
chlL CHL00072
photochlorophyllide reductase subunit L
 34-91 1.98e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 42.03  E-value: 1.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1119673244  34 LAVIsGKGGVGKSNITLNMALALQDKGKKVLLIDLDIGMGNIDILIGnSSSATIIDVL 91
Cdd:CHL00072    3 LAVY-GKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTG-FLIPTIIDTL 58
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 37-69 2.66e-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: 41.95  E-value: 2.66e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1119673244  37 ISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:pfam02374   6 FGGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 32-148 4.57e-04

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: 40.50  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  32 KTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLDI----------------GMGNidILIGNSS-SATIIDVLTDR 94
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMrnsvmsgtfksqnkitGLTN--FLSGTTDlSDAICDTNIEN 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1119673244  95 KPLLQSLSIGPKGLRYISGgtgldvmfqldqrkwTFFANELSHALSQFDYVLFD 148
Cdd:TIGR01007  96 LDVITAGPVPPNPTELLQS---------------SNFKTLIETLRKRFDYIIID 134
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
36-69 8.37e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 40.19  E-value: 8.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1119673244  36 VISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:COG0003     7 FFTGKGGVGKTTVAAATALALAERGKRTLLVSTD 40
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 40-69 1.71e-03

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


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 39.36  E-value: 1.71e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1119673244  40 KGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 36-69 2.25e-03

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 37.70  E-value: 2.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1119673244  36 VISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:cd05386     5 VLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTD 38
PRK13886 PRK13886
conjugal transfer protein TraL; Provisional
 31-69 3.27e-03

conjugal transfer protein TraL; Provisional


Pssm-ID: 184370  Cd Length: 241  Bit Score: 38.17  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1119673244  31 AKTLAVISGKGGVGKSNITLNMALALQDKGKKVLLIDLD 69
Cdd:PRK13886    2 AKIHMVLQGKGGVGKSFIAATIAQYKASKGQKPLCIDTD 40
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 37-294 4.76e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 37.85  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244  37 ISGKGGVGKSNITLNMAlALQDKGKKVLLIDLDIGMGNIDILIGNSSSaTIIDVLTD-RKPLLQSLSI-GPKGLRYI-SG 113
Cdd:PRK13231    7 IYGKGGIGKSTTVSNMA-AAYSNDHRVLVIGCDPKADTTRTLCGKRIP-TVLDTLKDnRKPELEDIIHeGFNGILCVeSG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 114 G-------TGLDVMFQLDQ-RKWTFFANElshalsqFDYVLFDMGAGLSKDQLPFILS---AEDILIITTPEPTAILDAY 182
Cdd:PRK13231   85 GpepgvgcAGRGVIVAMNLlENLGVFDED-------IDVVIYDVLGDVVCGGFSVPLRedyADEVYIVTSGEYMSLYAAN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119673244 183 SAVKHLVLTENKLSMKVAVNR-CRDQKEGLDAFARL--SRTIHMfldvqVQFAGSVSDDVIVSKAVVEQVPffiKSPQAK 259
Cdd:PRK13231  158 NIARGIKKLKGKLGGIICNCRgIDNEVEIVSEFASRigSRIIGV-----IPRSNLVQESELDAKTVVETFP---ESEQAS 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1119673244 260 ASRSvriLADALFGREE--TRHKEDKQTFIEKLSSFL 294
Cdd:PRK13231  230 VYRK---LANNIMNNTEfsTPEPMDDEEFEEFFKSFR 263
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 39-75 9.18e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 36.46  E-value: 9.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1119673244  39 GKGGVGKSNIT---LNMALAlqdKGKKVLLIDLDIGMGNI 75
Cdd:pfam16575   1 GPKDSGKSTLCrilLNYAVR---KGRKPVYVDLDVGQSEI 37
 
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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