NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|428015306|gb|AFY91400|]
View 

ATPase involved in chromosome partitioning [Chamaesiphon minutus PCC 6605]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 171-346 7.23e-64

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: 203.97  E-value: 7.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLVKFQfeeeddlRDRNVCHLISsgDTNFIHE 250
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNN-------VEKTIYELLI--GECNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  251 IVRESQYfsdPEIAVIPAHINLIDKQGELTTIMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSD 330
Cdd:pfam13614  72 AIIKTVI---ENLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148

                         170
                  ....*....|....*.
gi 428015306  331 LKPFANQGLPTVKKFI 346
Cdd:pfam13614 149 CEYYALEGLSQLLNTI 164
COG2810 super family cl43716
Predicted type IV restriction endonuclease [Defense mechanisms];
9-107 2.98e-10

Predicted type IV restriction endonuclease [Defense mechanisms];


The actual alignment was detected with superfamily member COG2810:

Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 61.53  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306   9 RNESEVESKLIvGYLLPKLGYS---PDTWHQEVRFGKIRLDFLAFTQKLPLklgvpsigLIIEAKHPRKNL-DKHVYQLR 84
Cdd:COG2810   26 ANEAATRQEFI-DPLLEALGWDidnPEEVIPEERVEGGRPDYALRLNGKRK--------LFVEAKKPGVNLkDKPARQAR 96

                         90       100
                 ....*....|....*....|...
gi 428015306  85 SYLTSLDISYGLLTNGKDLRIYH 107
Cdd:COG2810   97 SYAWSSGVRWAILTNGREWRVYD 119
 
Name Accession Description Interval E-value
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 171-346 7.23e-64

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: 203.97  E-value: 7.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLVKFQfeeeddlRDRNVCHLISsgDTNFIHE 250
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNN-------VEKTIYELLI--GECNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  251 IVRESQYfsdPEIAVIPAHINLIDKQGELTTIMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSD 330
Cdd:pfam13614  72 AIIKTVI---ENLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148

                         170
                  ....*....|....*.
gi 428015306  331 LKPFANQGLPTVKKFI 346
Cdd:pfam13614 149 CEYYALEGLSQLLNTI 164
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 171-459 4.74e-58

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: 191.61  E-value: 4.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLvkfqfeEEDDLrDRNVCHLISSGDTnfIHE 250
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL------DPDDL-DPTLYDLLLDDAP--LED 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 251 IVRESQYfsdPEIAVIPAHINLIDKQGELTTIMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSD 330
Cdd:COG1192   72 AIVPTEI---PGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 331 LKPFANQGLPTVKKFITAMDETRsiiaKKPIQLLGVLASKISTNARFieytfpkQREV---IGKRYEMPLMESVIYDRTA 407
Cdd:COG1192  149 PEYLSLEGLAQLLETIEEVREDL----NPKLEILGILLTMVDPRTRL-------SREVleeLREEFGDKVLDTVIPRSVA 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 428015306 408 LSESFNKtvivgdleypdPKSIFKYANEVKssaqvSAMEFEVLAQEVLTKIG 459
Cdd:COG1192  218 LAEAPSA-----------GKPVFEYDPKSK-----GAKAYRALAEELLERLE 253
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 172-376 4.22e-26

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: 102.62  E-value: 4.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglvkfqfeeeddlrdrnvchlissgdtnfihei 251
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 vresQYFsdpeiavipahinlidkqgelttimasrnrlieklkrvennYDIVIFDTPPSRDIYAEVALLTADYLIIPSDL 331
Cdd:cd02042   45 ----SWL-----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQP 79

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 428015306 332 KPFANQGLptvKKFITAMDETRSIIAKKPIqLLGVLASKISTNAR 376
Cdd:cd02042   80 SPFDLDGL---AKLLDTLEELKKQLNPPLL-ILGILLTRVDPRTK 120
ParA_partition NF041546
ParA family partition ATPase;
173-438 1.86e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 91.84  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 173 TIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQAnstfatglvkfqfeeeddlrdrnvchliSSGDTnfiHEiV 252
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG----------------------------SALDW---AA-A 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 253 RESQyfsdPEIAVIPahinlidkqgelttimASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSDLK 332
Cdd:NF041546  49 REDE----RPFPVVG----------------LARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPS 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 333 PFAnqglptvkkfITAMDETRSIIAKKPIQLLGVLA----SKISTNARFieytfpkQREVIG--KRYEMPLMESVIYDRT 406
Cdd:NF041546 109 PYD----------LWASADTVDLIKEAREYTPGLKAafvlNRAIARTAL-------GREVAEalAEYGLPVLKTRIGQRV 171

                        250       260       270
                 ....*....|....*....|....*....|..
gi 428015306 407 ALSESFNKTVIVGDLEypdPKSifKYANEVKS 438
Cdd:NF041546 172 AFAESAAEGLTVFEAE---PDG--KAAREIRA 198
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 171-328 2.89e-17

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 83.10  E-value: 2.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglVKFQFEEEDDLRDrnvchlissGDTNF--- 247
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-----ALFGYQPEFDVGE---------NETLYgai 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  248 --------IHEIVRESqYFsdPEIAVIPAHINLIDKQGELTTIMASRN--------RLIEKLKRVENNYDIVIFDTPPSR 311
Cdd:TIGR03453 170 rydderrpISEIIRKT-YF--PGLDLVPGNLELMEFEHETPRALSRGQggdtiffaRVGEALAEVEDDYDVVVIDCPPQL 246

                         170
                  ....*....|....*..
gi 428015306  312 DIYAEVALLTADYLIIP 328
Cdd:TIGR03453 247 GFLTLSALCAATGVLIT 263
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
173-346 1.77e-12

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 67.86  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 173 TIAIYHNKGGVGKTTVSTNLAAALSKR-GYRVLLIDIDAQANSTFatgLVKFQFEEEDDLRDRNVChlISSGDtnFIHEI 251
Cdd:NF041283   4 VIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATQ---FLSKTFNVPNFPQSFMKC--VEDGD--LEKGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 VRESqyfsdPEIAVIPAHIN-------LIDKQGELTTIMASRNRLIEKLKrveNNYDIVIFDTPPSRDIYAEVALLTADY 324
Cdd:NF041283  77 VHLT-----PNLDLIAGDYDtrelgdfLADKFKSEYDRTFYLKKLLDKIK---DDYDFIFIDVPPSTDIKVDNAMVAADY 148

                        170       180
                 ....*....|....*....|..
gi 428015306 325 LIIPSDLKPFANQGlptVKKFI 346
Cdd:NF041283 149 VIVIQETQQFAFEG---SKKLI 167
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 171-327 5.08e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 67.39  E-value: 5.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLVKfqfeEEDDLRDRNVCHLISSGDTNF-IH 249
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLP----ETDVGANETLYAAIRYDDTRRpLR 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 250 EIVReSQYFSDpeIAVIPAHINLIDKQGELTTIMASR--------NRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLT 321
Cdd:PRK13869 197 DVIR-PTYFDG--LHLVPGNLELMEFEHTTPKALSDKgtrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCA 273


                 ....*.
gi 428015306 322 ADYLII 327
Cdd:PRK13869 274 ATSMVI 279
COG2810 COG2810
Predicted type IV restriction endonuclease [Defense mechanisms];
9-107 2.98e-10

Predicted type IV restriction endonuclease [Defense mechanisms];


Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 61.53  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306   9 RNESEVESKLIvGYLLPKLGYS---PDTWHQEVRFGKIRLDFLAFTQKLPLklgvpsigLIIEAKHPRKNL-DKHVYQLR 84
Cdd:COG2810   26 ANEAATRQEFI-DPLLEALGWDidnPEEVIPEERVEGGRPDYALRLNGKRK--------LFVEAKKPGVNLkDKPARQAR 96

                         90       100
                 ....*....|....*....|...
gi 428015306  85 SYLTSLDISYGLLTNGKDLRIYH 107
Cdd:COG2810   97 SYAWSSGVRWAILTNGREWRVYD 119
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 65-108 1.01e-03

Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.


Pssm-ID: 433331 [Multi-domain]  Cd Length: 110  Bit Score: 38.73  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 428015306   65 LIIEAKHPR-KNLDKHVYQLRSYLTSLDISYGLLTNGKDLRIYHQ 108
Cdd:pfam13588  52 ILVECKAPSiKISQKVFDQLARYNSVLGAPFLVVTNGLQHICFKV 96
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 177-310 1.11e-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: 41.40  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 177 YHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglvkfqfeeedDLRDRNVCHLISSgdtnfIHEIVRESQ 256
Cdd:NF041417  17 FSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLS--------------DIFGQSIGHRVTS-----IDDVENLSA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428015306 257 YFSDPEIA-------VIPAHINLIDKQgELTTI-----------MASRNRLIEKLKRVEnnYDIVIFDTPPS 310
Cdd:NF041417  78 IEIDPDAAaeeyrqrTIEPMRQLLDDE-QLKTVeeqldspcieeIAAFDKFVEFMDEPE--YDVVVFDTAPT 146
 
Name Accession Description Interval E-value
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 171-346 7.23e-64

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: 203.97  E-value: 7.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLVKFQfeeeddlRDRNVCHLISsgDTNFIHE 250
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNN-------VEKTIYELLI--GECNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  251 IVRESQYfsdPEIAVIPAHINLIDKQGELTTIMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSD 330
Cdd:pfam13614  72 AIIKTVI---ENLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148

                         170
                  ....*....|....*.
gi 428015306  331 LKPFANQGLPTVKKFI 346
Cdd:pfam13614 149 CEYYALEGLSQLLNTI 164
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 171-459 4.74e-58

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: 191.61  E-value: 4.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLvkfqfeEEDDLrDRNVCHLISSGDTnfIHE 250
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL------DPDDL-DPTLYDLLLDDAP--LED 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 251 IVRESQYfsdPEIAVIPAHINLIDKQGELTTIMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSD 330
Cdd:COG1192   72 AIVPTEI---PGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 331 LKPFANQGLPTVKKFITAMDETRsiiaKKPIQLLGVLASKISTNARFieytfpkQREV---IGKRYEMPLMESVIYDRTA 407
Cdd:COG1192  149 PEYLSLEGLAQLLETIEEVREDL----NPKLEILGILLTMVDPRTRL-------SREVleeLREEFGDKVLDTVIPRSVA 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 428015306 408 LSESFNKtvivgdleypdPKSIFKYANEVKssaqvSAMEFEVLAQEVLTKIG 459
Cdd:COG1192  218 LAEAPSA-----------GKPVFEYDPKSK-----GAKAYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 174-414 3.60e-29

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: 113.98  E-value: 3.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  174 IAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLVKFQFEEEDDLRDRnvchLISSGDTN-FIheIV 252
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEG----LKGRVNLDpIL--LK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  253 RESQYFSdpeIAVIPAHINLIDKQGELTTIMASrNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSDLK 332
Cdd:pfam01656  75 EKSDEGG---LDLIPGNIDLEKFEKELLGPRKE-ERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  333 PFANQGLptvKKFITAMDETRSIIAKKPIQLLGVLASKISTNArfieyTFPKQREVIGKR-YEMPLMeSVIYDRTALSES 411
Cdd:pfam01656 151 VILVEDA---KRLGGVIAALVGGYALLGLKIIGVVLNKVDGDN-----HGKLLKEALEELlRGLPVL-GVIPRDEAVAEA 221


                  ...
gi 428015306  412 FNK 414
Cdd:pfam01656 222 PAR 224
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 172-376 4.22e-26

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: 102.62  E-value: 4.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglvkfqfeeeddlrdrnvchlissgdtnfihei 251
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 vresQYFsdpeiavipahinlidkqgelttimasrnrlieklkrvennYDIVIFDTPPSRDIYAEVALLTADYLIIPSDL 331
Cdd:cd02042   45 ----SWL-----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQP 79

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 428015306 332 KPFANQGLptvKKFITAMDETRSIIAKKPIqLLGVLASKISTNAR 376
Cdd:cd02042   80 SPFDLDGL---AKLLDTLEELKKQLNPPLL-ILGILLTRVDPRTK 120
ParA_partition NF041546
ParA family partition ATPase;
173-438 1.86e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 91.84  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 173 TIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQAnstfatglvkfqfeeeddlrdrnvchliSSGDTnfiHEiV 252
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG----------------------------SALDW---AA-A 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 253 RESQyfsdPEIAVIPahinlidkqgelttimASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSDLK 332
Cdd:NF041546  49 REDE----RPFPVVG----------------LARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPS 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 333 PFAnqglptvkkfITAMDETRSIIAKKPIQLLGVLA----SKISTNARFieytfpkQREVIG--KRYEMPLMESVIYDRT 406
Cdd:NF041546 109 PYD----------LWASADTVDLIKEAREYTPGLKAafvlNRAIARTAL-------GREVAEalAEYGLPVLKTRIGQRV 171

                        250       260       270
                 ....*....|....*....|....*....|..
gi 428015306 407 ALSESFNKTVIVGDLEypdPKSifKYANEVKS 438
Cdd:NF041546 172 AFAESAAEGLTVFEAE---PDG--KAAREIRA 198
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 171-328 2.89e-17

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 83.10  E-value: 2.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglVKFQFEEEDDLRDrnvchlissGDTNF--- 247
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-----ALFGYQPEFDVGE---------NETLYgai 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  248 --------IHEIVRESqYFsdPEIAVIPAHINLIDKQGELTTIMASRN--------RLIEKLKRVENNYDIVIFDTPPSR 311
Cdd:TIGR03453 170 rydderrpISEIIRKT-YF--PGLDLVPGNLELMEFEHETPRALSRGQggdtiffaRVGEALAEVEDDYDVVVIDCPPQL 246

                         170
                  ....*....|....*..
gi 428015306  312 DIYAEVALLTADYLIIP 328
Cdd:TIGR03453 247 GFLTLSALCAATGVLIT 263
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 172-327 5.01e-16

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: 77.22  E-value: 5.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDaqanstfaTGL----VKFQFEEEDDLRdrnvcHLISSGDTnf 247
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD--------LGLanldILLGLAPKKTLG-----DVLKGRVS-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 248 IHEIVREsqyfsdpeiavIPAHINLIdKQGELTTIMA-----SRNRLIEKLKRVENNYDIVIFDTPP--SRDIYAevALL 320
Cdd:cd02038   66 LEDIIVE-----------GPEGLDII-PGGSGMEELAnldpeQKAKLIEELSSLESNYDYLLIDTGAgiSRNVLD--FLL 131


                 ....*..
gi 428015306 321 TADYLII 327
Cdd:cd02038  132 AADEVIV 138
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 172-331 8.80e-15

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: 75.54  E-value: 8.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKR-GYRVLLIDIDAQanstFATGLVKFQFEEEDDLRDrnVCHLISSGDTNFIHE 250
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQ----FGDVALYLDLEPRRGLAD--ALRNPDRLDETLLDR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 251 IVreSQYfsDPEIAVIPAhinlIDKQGELTTIMASR-NRLIEKLKRvenNYDIVIFDTPPSRDIYAEVALLTADYLIIPS 329
Cdd:COG4963  177 AL--TRH--SSGLSVLAA----PADLERAEEVSPEAvERLLDLLRR---HFDYVVVDLPRGLNPWTLAALEAADEVVLVT 245


                 ..
gi 428015306 330 DL 331
Cdd:COG4963  246 EP 247
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 173-309 9.90e-14

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: 71.37  E-value: 9.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 173 TIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAqANSTFATglvKFQFEEEDDLRDrnvchlISSGDTNFiHEIV 252
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADL-RGPSLHR---MLGLENRPGLSD------VLAGEASL-EDVI 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 253 RESQYfsdPEIAVIPAhinlidkqGELT---TIMASRNRLIEKLKRVENNYDIVIFDTPP 309
Cdd:COG0489  163 QPTEV---EGLDVLPA--------GPLPpnpSELLASKRLKQLLEELRGRYDYVIIDTPP 211
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 172-436 9.45e-13

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: 67.83  E-value: 9.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID-AQANSTFATGlvkfqfeeeddLRDRNVC-HLISSGDTNfih 249
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILG-----------MEDKPVTlHDVLAGEAD--- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  250 eiVRESQYFSDPEIAVIPAHINlidkqgeLTTIMASR-NRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIP 328
Cdd:TIGR01969  67 --IKDAIYEGPFGVKVIPAGVS-------LEGLRKADpDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  329 SDlkpfanqglPTVKKFITAMdETRSIIAKKPIQLLGVLASKISTNARFIeytfpkQREVIGKRYEMPLMESVIYD---- 404
Cdd:TIGR01969 138 VN---------PEISSITDAL-KTKIVAEKLGTAILGVVLNRVTRDKTEL------GREEIETILEVPVLGVVPEDpevr 201

                         250       260       270
                  ....*....|....*....|....*....|..
gi 428015306  405 RTALsesFNKTVIVGDLEYPDPKSIFKYANEV 436
Cdd:TIGR01969 202 RAAA---FGEPVVIYNPNSPAAQAFMELAAEL 230
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 187-428 1.70e-12

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: 66.84  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 187 TVSTNLAAALSKRGYRVLLIDID-AQANSTFATGLVkfqfeeeddlRDRNVCHLISSGDTnfIHEIVREsqyfSDPEIAV 265
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADlGLANLDVLLGLE----------PKATLADVLAGEAD--LEDAIVQ----GPGGLDV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 266 IPAHINLidkqGELTTIMASRnRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSDLKPfanQGLPTVKKF 345
Cdd:COG0455   65 LPGGSGP----AELAELDPEE-RLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEP---TSITDAYAL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 346 ITAMDEtrsiiaKKPIQLLGVLASKISTNARFIEyTFPKQREVIGKRY--EMPLMESVIYDRtALSESFNKTVIVgDLEY 423
Cdd:COG0455  137 LKLLRR------RLGVRRAGVVVNRVRSEAEARD-VFERLEQVAERFLgvRLRVLGVIPEDP-AVREAVRRGRPL-VLAA 207


                 ....*
gi 428015306 424 PDPKS 428
Cdd:COG0455  208 PDSPA 212
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
173-346 1.77e-12

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 67.86  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 173 TIAIYHNKGGVGKTTVSTNLAAALSKR-GYRVLLIDIDAQANSTFatgLVKFQFEEEDDLRDRNVChlISSGDtnFIHEI 251
Cdd:NF041283   4 VIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATQ---FLSKTFNVPNFPQSFMKC--VEDGD--LEKGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 VRESqyfsdPEIAVIPAHIN-------LIDKQGELTTIMASRNRLIEKLKrveNNYDIVIFDTPPSRDIYAEVALLTADY 324
Cdd:NF041283  77 VHLT-----PNLDLIAGDYDtrelgdfLADKFKSEYDRTFYLKKLLDKIK---DDYDFIFIDVPPSTDIKVDNAMVAADY 148

                        170       180
                 ....*....|....*....|..
gi 428015306 325 LIIPSDLKPFANQGlptVKKFI 346
Cdd:NF041283 149 VIVIQETQQFAFEG---SKKLI 167
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 171-327 5.08e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 67.39  E-value: 5.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGLVKfqfeEEDDLRDRNVCHLISSGDTNF-IH 249
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLP----ETDVGANETLYAAIRYDDTRRpLR 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 250 EIVReSQYFSDpeIAVIPAHINLIDKQGELTTIMASR--------NRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLT 321
Cdd:PRK13869 197 DVIR-PTYFDG--LHLVPGNLELMEFEHTTPKALSDKgtrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCA 273


                 ....*.
gi 428015306 322 ADYLII 327
Cdd:PRK13869 274 ATSMVI 279
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 174-209 7.35e-12

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: 64.44  E-value: 7.35e-12
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 428015306 174 IAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:cd02037    3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 158-370 1.64e-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: 62.97  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 158 VSLTISASSPLLDMKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDaqanstfatglvkfqfeeeddLRDRNVC 237
Cdd:cd05387    6 LRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD---------------------LRRPSLH 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 238 HLISS----GDTNFIHEIVRESQYFSDPEI---AVIPAhinlidkqGELT---TIMASRNRLIEKLKRVENNYDIVIFDT 307
Cdd:cd05387   65 RLLGLpnepGLSEVLSGQASLEDVIQSTNIpnlDVLPA--------GTVPpnpSELLSSPRFAELLEELKEQYDYVIIDT 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428015306 308 PPSrdiyaevaLLTADYLIipsdLKPFANQGLPTVKKFIT---AMDETRSIIAKKPIQLLGVLASK 370
Cdd:cd05387  137 PPV--------LAVADALI----LAPLVDGVLLVVRAGKTrrrEVKEALERLEQAGAKVLGVVLNK 190
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 172-209 1.79e-11

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: 64.01  E-value: 1.79e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 428015306  172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 172-327 3.05e-11

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


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 62.99  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID-AQANSTFATGLvkfqfeEEDDLRDrnvCHLISSGDTNFIHE 250
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGL------ENRIVYT---LVDVLEGECRLEQA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 428015306 251 IVRESQYfsdPEIAVIPAHINLiDKqgelttIMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLII 327
Cdd:cd02036   72 LIKDKRW---ENLYLLPASQTR-DK------DALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAII 138
PHA02518 PHA02518
ParA-like protein; Provisional
 172-427 4.66e-11

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 62.17  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATglvkfQFEEEDdlrdrnvchlissgdtnfihei 251
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWA-----EAREEG---------------------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 vresqyfsDPEIAVipahinlidkqgelttiMASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSDL 331
Cdd:PHA02518  54 --------EPLIPV-----------------VRMGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQP 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 332 KPFANQGLPTVKKFITAMDETR------SIIAKKPIQllgvlASKISTNAR-FIEYtfpkqrevigkrYEMPLMESVIYD 404
Cdd:PHA02518 109 SPFDIWAAPDLVELIKARQEVTdglpkfAFIISRAIK-----NTQLYREARkALAG------------YGLPILRNGTTQ 171

                        250       260
                 ....*....|....*....|...
gi 428015306 405 RTALSESFNKTVIVgdLEYPDPK 427
Cdd:PHA02518 172 RVAYADAAEAGGSV--LELPEDD 192
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 171-330 2.61e-10

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 60.44  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQanstfatGLVKFQF----EEEDDLRDRnvchliSSGDTN 246
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ-------NLLRLHFgmdwSVRDGWARA------LLNGAD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  247 FiheivRESQYFSDPEIAVIPAHINLIDkqgELTTIMASR----NRLIEKLKRVENnyDIVIFDTPPSRDIYAEVALLTA 322
Cdd:TIGR03371  68 W-----AAAAYRSPDGVLFLPYGDLSAD---EREAYQAHDagwlARLLQQLDLAAR--DWVLIDLPRGPSPITRQALAAA 137

                         170
                  ....*....|
gi 428015306  323 DYL--IIPSD 330
Cdd:TIGR03371 138 DLVlvVVNAD 147
COG2810 COG2810
Predicted type IV restriction endonuclease [Defense mechanisms];
9-107 2.98e-10

Predicted type IV restriction endonuclease [Defense mechanisms];


Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 61.53  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306   9 RNESEVESKLIvGYLLPKLGYS---PDTWHQEVRFGKIRLDFLAFTQKLPLklgvpsigLIIEAKHPRKNL-DKHVYQLR 84
Cdd:COG2810   26 ANEAATRQEFI-DPLLEALGWDidnPEEVIPEERVEGGRPDYALRLNGKRK--------LFVEAKKPGVNLkDKPARQAR 96

                         90       100
                 ....*....|....*....|...
gi 428015306  85 SYLTSLDISYGLLTNGKDLRIYH 107
Cdd:COG2810   97 SYAWSSGVRWAILTNGREWRVYD 119
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 172-229 5.39e-10

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: 60.00  E-value: 5.39e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428015306 172 KTIAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFA-TG---------LVKFQFEEED 229
Cdd:cd02032    1 LVIAVY-GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTlTGfliptvidvLQSVDFHYEE 67
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 172-306 5.48e-10

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: 60.07  E-value: 5.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFAtglvkfqfeeeddLRDRNVCHLISSGDTNFIH-- 249
Cdd:cd02117    1 ESIVVY-GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLL-------------LTGGKVPPTIDEMLTEDGTae 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428015306 250 EIVRESQYFSD-----------PEIAVIPAhinlidKQGELTTImasrnRLIEKLKRVENNYDIVIFD 306
Cdd:cd02117   67 ELRREDLLFSGfngvdcveaggPEPGVGCG------GRGIGTML-----ELLEEHGLLDDDYDVVIFD 123
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 172-216 5.50e-10

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 59.98  E-value: 5.50e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 428015306 172 KTIAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTF 216
Cdd:PRK13185   3 LVLAVY-GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTF 46
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 172-209 5.80e-10

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 59.69  E-value: 5.80e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
170-311 1.45e-09

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 59.06  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 170 DMKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANstfaTGLVkFQFEEEDDLRDRNVCHLissgdtnFIH 249
Cdd:COG0003    1 DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHS----LGDV-LGTELGNEPTEVAVPNL-------YAL 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428015306 250 EIvresqyfsDPEIAViPAHINLIdkQGELTTIMASRNR--------------LIEKLKRV--ENNYDIVIFDTPPSR 311
Cdd:COG0003   69 EI--------DPEAEL-EEYWERV--RAPLRGLLPSAGVdelaeslpgteelaALDELLELleEGEYDVIVVDTAPTG 135
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 174-215 2.67e-09

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: 57.91  E-value: 2.67e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 428015306 174 IAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANST 215
Cdd:cd02040    3 IAIY-GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 180-328 3.11e-09

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: 57.46  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  180 KGGVGKTTVSTNLAAALSKRGYRVLLIDIdaqanstfatglvkfqfeeedDLRDRnvchlissgdtNFIHEIVRESQYFS 259
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDL---------------------DLRQR-----------TFHRYFENRSATAD 56

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428015306  260 DPEIAV-IPAHINLIDKQGELTTIMAS--RNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIP 328
Cdd:pfam09140  57 RTGLSLpTPEHLNLPDNDVAEVPDGENidDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTP 128
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 180-213 3.67e-09

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 57.10  E-value: 3.67e-09
                         10        20        30
                 ....*....|....*....|....*....|....
gi 428015306 180 KGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQAN 213
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 172-209 4.16e-09

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: 53.97  E-value: 4.16e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 180-309 6.15e-09

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: 56.36  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 180 KGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFATGlVKFQFEEeddlrdrnvchlISSGDTN-FIHEI------- 251
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFG-QKLGGET------------PVKGAPNlWAMEIdpeeale 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428015306 252 -----VRE--SQYFSDPEIAVIpahinlidkQGELTTI------MASRNRLIEKLKrvENNYDIVIFDTPP 309
Cdd:cd02035   75 eyweeVKEllAQYLRLPGLDEV---------YAEELLSlpgmdeAAAFDELREYVE--SGEYDVIVFDTAP 134
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 170-309 8.08e-09

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 55.52  E-value: 8.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  170 DMKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQaNSTfatglVKFQFeeedDLRDRNvchlisSGDTNFIH 249
Cdd:TIGR01007  16 EIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMR-NSV-----MSGTF----KSQNKI------TGLTNFLS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 428015306  250 EIVRESQYFSDPEIA---VIPAhinlidkqGEL----TTIMASRN--RLIEKLKrveNNYDIVIFDTPP 309
Cdd:TIGR01007  80 GTTDLSDAICDTNIEnldVITA--------GPVppnpTELLQSSNfkTLIETLR---KRFDYIIIDTPP 137
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 172-209 4.79e-08

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: 53.88  E-value: 4.79e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 428015306  172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
chlL CHL00072
photochlorophyllide reductase subunit L
 171-219 1.41e-07

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 52.82  E-value: 1.41e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 428015306 171 MKtIAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTFA-TG 219
Cdd:CHL00072   1 MK-LAVY-GKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTlTG 48
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
174-215 3.50e-07

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 51.68  E-value: 3.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 428015306  174 IAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANST 215
Cdd:pfam00142   3 IAIY-GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADST 43
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 171-215 4.02e-07

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 51.31  E-value: 4.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 428015306 171 MKTIAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANST 215
Cdd:PRK13230   1 MRKFCFY-GKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCT 44
minD CHL00175
septum-site determining protein; Validated
 172-209 4.59e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 51.31  E-value: 4.59e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 174-329 6.31e-07

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 51.52  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 174 IAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLID-IDAQANSTFATGLV-KFQFEEEDDLRDRnvcHLISSGDTNFiheI 251
Cdd:PRK13705 109 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVpDLHIHAEDTLLPF---YLGEKDDATY---A 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 VRESQYfsdPEIAVIPAHINL---------IDKQGELTTimASRNRLIEKLKRVENNYDIVIFDTPPSRDIYAEVALLTA 322
Cdd:PRK13705 183 IKPTCW---PGLDIIPSCLALhrietelmgKFDEGKLPT--DPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAA 257


                 ....*..
gi 428015306 323 DYLIIPS 329
Cdd:PRK13705 258 DVLIVPT 264
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 180-309 8.61e-07

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: 50.43  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  180 KGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglvkfqfeeedDLRDRNVCHLISSGDTN-FIHEI---VRES 255
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLS--------------DSFNQKFGHEPTKVKENlSAMEIdpnMELE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428015306  256 QY---FSDPEIAVIPAHInLIDKQGELTTIM------ASRNRLIEKLKrvENNYDIVIFDTPP 309
Cdd:pfam02374  75 EYwqeVQKYMNALLGLRM-LEGILAEELASLpgideaASFDEFKKYMD--EGEYDVVVFDTAP 134
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 171-213 1.71e-06

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


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 49.23  E-value: 1.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 428015306 171 MKtIAIyHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQAN 213
Cdd:cd02034    1 MK-IAV-AGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSN 41
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 134-212 1.80e-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: 47.00  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  134 LIGRDFTRKQFAQNSPTLS-PPPQPVSLTISASSPLLD-----MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLID 207
Cdd:TIGR04291 277 LVGLEALRQLLNDDQPQLSlDITTPQVPDLPSLSRLIDeiaksEKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTT 356


                  ....*
gi 428015306  208 IDAQA 212
Cdd:TIGR04291 357 SDPAA 361
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
182-203 4.25e-05

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 45.89  E-value: 4.25e-05
                         10        20
                 ....*....|....*....|..
gi 428015306 182 GVGKTTVSTNLAAALSKRGYRV 203
Cdd:PRK01077  14 GSGKTTVTLGLMRALRRRGLRV 35
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
174-209 4.32e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 45.42  E-value: 4.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 428015306 174 IAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDID 209
Cdd:PRK11670 110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 174-335 4.52e-05

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: 44.68  E-value: 4.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 174 IAIYHNKGGVGKTTVSTNLAAALskrgYRVLLIDIDAQAnSTFATgLVKFQFEEEDDLR-------DRNVC--------- 237
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDA-PNLHL-LLGPEPEEEEDFVggkkafiDQEKCircgncerv 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 238 ----HLISSGDTNFIHEIV------------RESQYFSDPEIAVIpahinLIDKQGELTTIMA-----SRN------RLI 290
Cdd:cd03110   76 ckfgAILEFFQKLIVDESLcegcgacviicpRGAIYLKDRDTGKI-----FISSSDGGPLVHGrlnigEENsgklvtELR 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 428015306 291 EKLKRVENNYDIVIFDTPPSRDIYAEVALLTADYLIIPSDLKPFA 335
Cdd:cd03110  151 KKALERSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSG 195
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
 181-203 4.52e-05

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 45.49  E-value: 4.52e-05
                         10        20
                 ....*....|....*....|...
gi 428015306 181 GGVGKTTVSTNLAAALSKRGYRV 203
Cdd:COG1797   13 SGSGKTTVTLGLLAALRRRGLKV 35
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 172-433 7.79e-05

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: 43.81  E-value: 7.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKR-GYRVLLIDIDAQanstFATGLVKFqfeeedDLR-DRNVCHLISSGDtNFIH 249
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLP----FGDLGLYL------NLRpDYDLADVIQNLD-RLDR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 250 EIVRESQYFSDPEIAVIPAHIN---LIDKQGELTTimasrnRLIEKLKrveNNYDIVIFDTPPSRDIYAEVALLTADYLI 326
Cdd:cd03111   70 TLLDSAVTRHSSGLSLLPAPQEledLEALGAEQVD------KLLQVLR---AFYDHIIVDLGHFLDEVTLAVLEAADEIL 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 327 IpsdlkpFANQGLPTV---KKFITAMDETRsiIAKKPIQLlgvLASKISTNARfIEytfPKQrevIGKRYEMPLMESVIY 403
Cdd:cd03111  141 L------VTQQDLPSLrnaRRLLDSLRELE--GSSDRLRL---VLNRYDKKSE-IS---PKD---IEEALGLEVFATLPN 202

                        250       260       270
                 ....*....|....*....|....*....|
gi 428015306 404 DRTALSESFNKTVIVGDleyPDPKSIFKYA 433
Cdd:cd03111  203 DYKAVSESANTGRPLVE---VAPRSALVRA 229
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 171-215 1.32e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 43.63  E-value: 1.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 428015306 171 MKTIAIYhNKGGVGKTTVSTNLAAALSKRgYRVLLIDIDAQANST 215
Cdd:PRK13231   2 MKKIAIY-GKGGIGKSTTVSNMAAAYSND-HRVLVIGCDPKADTT 44
PRK10818 PRK10818
septum site-determining protein MinD;
172-370 1.90e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 43.00  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDaqanstfaTGLvkfqfeeeddlrdRNVcHLISSGDTNFIHEI 251
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD--------IGL-------------RNL-DLIMGCERRVVYDF 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 252 VRESQYFSDPEIAVIPahinliDKQGE-LTTIMASRNRLIEKLKR----------VENNYDIVIFDTPPSRDIYAEVALL 320
Cdd:PRK10818  61 VNVIQGDATLNQALIK------DKRTEnLYILPASQTRDKDALTRegvakvlddlKAMDFEFIVCDSPAGIETGALMALY 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 428015306 321 TADYLIIPSDlkpfanqglPTVKkfiTAMDETRsiiakkpiqLLGVLASK 370
Cdd:PRK10818 135 FADEAIITTN---------PEVS---SVRDSDR---------ILGILASK 163
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
182-309 2.29e-04

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 43.60  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 182 GVGKTTVSTNLAAALSKRGYRVLLIDIDAQANstFATGLVKFQfeEEDDLRDrnvchlISSGDTnfihEIVRESQYFSDP 261
Cdd:PRK11519 537 SIGKTFVCANLAAVISQTNKRVLLIDCDMRKG--YTHELLGTN--NVNGLSD------ILIGQG----DITTAAKPTSIA 602

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 428015306 262 EIAVIPAHiNLIDKQGELttIMASrnRLIEKLKRVENNYDIVIFDTPP 309
Cdd:PRK11519 603 NFDLIPRG-QVPPNPSEL--LMSE--RFAELVNWASKNYDLVLIDTPP 645
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 182-241 4.52e-04

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 41.16  E-value: 4.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 428015306 182 GVGKTTVSTNLAAALSKRGYRVLLIDIDAqanstFATGLVK-FQFEEEDdlRDRN------VCHLIS 241
Cdd:PRK00889  14 GAGKTTIARALAEKLREAGYPVEVLDGDA-----VRTNLSKgLGFSKED--RDTNirrigfVANLLT 73
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 159-215 5.71e-04

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: 41.74  E-value: 5.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 428015306 159 SLTISASSPLLDMKTIAIYhNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANST 215
Cdd:cd02033   19 SLEIPTGPPTKETQIIAIY-GKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTT 74
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 180-310 7.13e-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: 42.00  E-value: 7.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  180 KGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQAN--STFAT-------------GLVKFQFEEE---DDLRDRNVchlis 241
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASNvgQVFGQtignkitaiagvpGLFALEIDPQaaaQAYRARIV----- 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 428015306  242 sgdtnfiheivresqyfsDPEIAVIP-AHINLIDKQ--GELTTIMASRNRLIEKL--KRVENNYDIVIFDTPPS 310
Cdd:TIGR04291  86 ------------------DPVRGVLPdDVVSSIEEQlsGACTTEIAAFDEFTGLLtdAELTQDFDHIIFDTAPT 141
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 172-330 8.49e-04

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: 40.60  E-value: 8.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDaqansTFATGLVKFQFEEEDDLRDrnVCHLISSGDTNF---I 248
Cdd:cd17869    4 SVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-----RLQSTDVFFGASGRYLMSD--HLYTLKSRKANLadkL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 249 HEIVRESQ----YFSDPEIAVIPAHINLIDKQgelttimasrnRLIEKLKRVeNNYDIVIFDTPPSRDIYAEVALLTADY 324
Cdd:cd17869   77 ESCVKQHEsgvyYFSPFKSALDILEIKKDDIL-----------HMITKLVEA-HAYDYIIMDLSFEFSSTVCKLLQASHN 144


                 ....*.
gi 428015306 325 LIIPSD 330
Cdd:cd17869  145 NVVIAL 150
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 65-108 1.01e-03

Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.


Pssm-ID: 433331 [Multi-domain]  Cd Length: 110  Bit Score: 38.73  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 428015306   65 LIIEAKHPR-KNLDKHVYQLRSYLTSLDISYGLLTNGKDLRIYHQ 108
Cdd:pfam13588  52 ILVECKAPSiKISQKVFDQLARYNSVLGAPFLVVTNGLQHICFKV 96
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 177-310 1.11e-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: 41.40  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 177 YHNKGGVGKTTVSTNLAAALSKRGYRVLLIDIDAQANSTfatglvkfqfeeedDLRDRNVCHLISSgdtnfIHEIVRESQ 256
Cdd:NF041417  17 FSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLS--------------DIFGQSIGHRVTS-----IDDVENLSA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428015306 257 YFSDPEIA-------VIPAHINLIDKQgELTTI-----------MASRNRLIEKLKRVEnnYDIVIFDTPPS 310
Cdd:NF041417  78 IEIDPDAAaeeyrqrTIEPMRQLLDDE-QLKTVeeqldspcieeIAAFDKFVEFMDEPE--YDVVVFDTAPT 146
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 180-217 1.88e-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: 38.86  E-value: 1.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 428015306 180 KGGVGKTTVSTNLAAALSKRGYRVLLIDIDaQANSTFA 217
Cdd:cd05386    9 KGGVGKSVIASLLAQYLIDKGQPVSCIDTD-PVNKTFA 45
pepcterm_TyrKin TIGR03018
exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are ...
 171-309 2.89e-03

exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are related to a known protein-tyrosine autokinase and to numerous homologs from exopolysaccharide biosynthesis region proteins, many of which are designated as chain length determinants. Most members of this family contain a short region, immediately C-terminal to the region modeled here, with an abundance of Tyr residues. These C-terminal tyrosine residues are likely to be autophosphorylation sites. Some members of this family are fusion proteins.


Pssm-ID: 274392 [Multi-domain]  Cd Length: 207  Bit Score: 38.82  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKR-GYRVLLIDIDAQANSTFATglvkFQFEEEDDLRDrnvchLISSGDTNfIH 249
Cdd:TIGR03018  35 NNLIMVTSSLPGEGKSFTAINLAISLAQEyDKTVLLIDADLRRPSLHRT----LGLEAEPGLSD-----CLLDPVLD-LA 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428015306  250 EIVRESQYfsdPEIAVIPAhinliDKQGELTTIMASRNRLIEKLKRVENNYD--IVIFDTPP 309
Cdd:TIGR03018 105 DVLVPTNI---GRLSLLPA-----GRRHPNPTELLASQRMRSLLHELARRYPdrIIIIDTPP 158
CobB_N cd05388
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ...
 172-203 3.27e-03

N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.


Pssm-ID: 349773 [Multi-domain]  Cd Length: 193  Bit Score: 38.74  E-value: 3.27e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 428015306 172 KTIAIYHNKGGVGKTTVSTNLAAALSKRGYRV 203
Cdd:cd05388    1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRV 32
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 171-207 3.87e-03

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 38.90  E-value: 3.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 428015306  171 MKTIAIYHNKGGVGKTTVSTNLAAALSKRGYRVLLID 207
Cdd:pfam06564   1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLID 37
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 182-203 4.94e-03

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 38.22  E-value: 4.94e-03
                         10        20
                 ....*....|....*....|..
gi 428015306 182 GVGKTTVSTNLAAALSKRGYRV 203
Cdd:COG0132   12 DVGKTVVTAALAAALRAAGLRV 33
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 182-304 5.77e-03

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 37.93  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428015306 182 GVGKTTVSTNLAAALSKRGYRVLLIDIdaqanstFATGLVKfqFEEEDDLRdrnVCHLISSGDTNFIHEIVRESQYFSdP 261
Cdd:cd03109   11 DVGKTVVSAGLARALRKKGIKVGYLKP-------VQTGCPG--LEDSDAEL---LRKLAGLLLDLELINPYRFEAPLS-P 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 428015306 262 EIAvipahinlidkqGELTTIMASRNRLIEKLKRVENNYDIVI 304
Cdd:cd03109   78 HLA------------AELEGRDIDLEEIVRALEELAKSYDVVL 108
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 171-209 7.94e-03

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 37.08  E-value: 7.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 428015306 171 MKTIAI--YHNkggVGKTTVSTNLAAALSKRGYRVLLI-------DID 209
Cdd:COG1763    1 MPVLGIvgYSG---SGKTTLLEKLIPELKARGLRVGTIkhahhdfDID 45
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH