NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1361103443|ref|WP_106302863|]
View 

AAA family ATPase [Chamaesiphon polymorphus]

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 ...
 167-348 1.65e-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: 205.51  E-value: 1.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLIKFQfeedddiRDRNVYHAIAssDRDFIEE 246
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNN-------VEKTIYELLI--GECNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 LVRKSSYFNepeIDVLPAHIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSD 326
Cdd:pfam13614  72 AIIKTVIEN---LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148

                         170       180
                  ....*....|....*....|....*.
gi 1361103443 327 LKPFANQGLP----TVKEFIKTINEN 348
Cdd:pfam13614 149 CEYYALEGLSqllnTIKLVKKRLNPS 174
COG2810 super family cl43716
Predicted type IV restriction endonuclease [Defense mechanisms];
9-274 1.62e-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: 62.30  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443   9 RNESEVESKLIvGYLLPKLGYS---PDTWHQEVRFGKIRLDFLaftqklpLKSDDRspLGLVIEAKHPRKNL-DKHVYQI 84
Cdd:COG2810    26 ANEAATRQEFI-DPLLEALGWDidnPEEVIPEERVEGGRPDYA-------LRLNGK--RKLFVEAKKPGVNLkDKPARQA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443  85 QSYLTSLNIAYGLLTNGKELRIYQ-QVAGSARLI-------FRCAVKDIGDRLPELIQLIGRDFLQQRLKDRLSLPQTEI 156
Cdd:COG2810    96 RSYAWSSGVRWAILTNGREWRVYDaQEKTSPRPIeldtaleARLLLLEYEELSSELDLILSRIIVDTDLLARLTLGLLDS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 157 FPTSARK---ISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQaNTTFATGLIKFQFEED-------DD 226
Cdd:COG2810   176 ELKERKLlsdSDPLLLEIDARLKETLGTAIKSTVLSGPILTDLREDRELSVVGL-SKSLDELLEELELKKDadevlkgLG 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1361103443 227 IRDRNVYHaiASSDRDFIEELVRKSSYFNEPEIDVLPAHIDLIKYQEF 274
Cdd:COG2810   255 PPDRKYSG--RSLRRSKSEVLGIKDDIAISIYLLLLPLVTLELVLKLI 300
 
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 ...
 167-348 1.65e-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: 205.51  E-value: 1.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLIKFQfeedddiRDRNVYHAIAssDRDFIEE 246
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNN-------VEKTIYELLI--GECNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 LVRKSSYFNepeIDVLPAHIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSD 326
Cdd:pfam13614  72 AIIKTVIEN---LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148

                         170       180
                  ....*....|....*....|....*.
gi 1361103443 327 LKPFANQGLP----TVKEFIKTINEN 348
Cdd:pfam13614 149 CEYYALEGLSqllnTIKLVKKRLNPS 174
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 167-455 7.95e-62

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: 201.24  E-value: 7.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLikfqfeeDDDIRDRNVYHAIAssDRDFIEE 246
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL-------DPDDLDPTLYDLLL--DDAPLED 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 LVRKSSYfnePEIDVLPAHIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSD 326
Cdd:COG1192    72 AIVPTEI---PGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 327 LKPFANQGLptvKEFIKTINENRETFGRqPLELLGVLASKISTNAqylkySFPKQ-RAVISERYELPLIESVIYDRTALS 405
Cdd:COG1192   149 PEYLSLEGL---AQLLETIEEVREDLNP-KLEILGILLTMVDPRT-----RLSREvLEELREEFGDKVLDTVIPRSVALA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1361103443 406 ACFNqtivvgdieypNPQSIFKYADTHNstsqtSALEFEVLANEILNKVK 455
Cdd:COG1192   220 EAPS-----------AGKPVFEYDPKSK-----GAKAYRALAEELLERLE 253
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 168-375 5.46e-28

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: 107.63  E-value: 5.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTfatglikfqfeedddirdrnvyhaiassdrdfieel 247
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 248 vrkssyfnepeidvlpahidlikyqeflttkmasrnrllaklkriENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDL 327
Cdd:cd02042    45 ---------------------------------------------SWLYDYILIDTPPSLGLLTRNALAAADLVLIPVQP 79

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1361103443 328 KPFANQGLptvKEFIKTINENRETFGRqPLELLGVLASKISTNAQYLK 375
Cdd:cd02042    80 SPFDLDGL---AKLLDTLEELKKQLNP-PLLILGILLTRVDPRTKLAR 123
ParA_partition NF041546
ParA family partition ATPase;
169-324 5.97e-20

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.61  E-value: 5.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 169 TIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTtfatglikfqfeedddiRDrnvYHAIASSDRDFieelv 248
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA-----------------LD---WAAAREDERPF----- 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1361103443 249 rkssyfnePEIDVlpahidlikyqeflttkmaSRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIP 324
Cdd:NF041546   56 --------PVVGL-------------------ARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIP 104
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 138-306 1.11e-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: 84.26  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 138 RDFLQQRLKDRLS-LPQTeifptsaRKISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTtfaTGL 216
Cdd:TIGR03453  81 RRHLAQRGREARRyLPHR-------RGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASL---SAL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 217 IKFQFEEDDDiRDRNVYHAIASSD-RDFIEELVRKsSYFnePEIDVLPAHIDLIKYQEFLTTKMASRN--------RLLA 287
Cdd:TIGR03453 151 FGYQPEFDVG-ENETLYGAIRYDDeRRPISEIIRK-TYF--PGLDLVPGNLELMEFEHETPRALSRGQggdtiffaRVGE 226

                         170
                  ....*....|....*....
gi 1361103443 288 KLKRIENSYDFVIIDTPPS 306
Cdd:TIGR03453 227 ALAEVEDDYDVVVIDCPPQ 245
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
169-344 3.19e-17

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 81.72  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 169 TIAIYHNKGGVGKTTVSTNLA-AAFSRKGYRTLLIDIDGQANTTFatgLIKFQFEedddirDRNVYHAIASS--DRDFIE 245
Cdd:NF041283    4 VIVLANQKGGVGKTTDTVMEAvVASSVFNKKVLVIDTDLQGNATQ---FLSKTFN------VPNFPQSFMKCveDGDLEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 246 ELVRKSsyfnePEIDVLPAHIDLIKYQEFLTTKMAS-RNRLLAKLK---RIENSYDFVIIDTPPSRDIYAEAALITADYL 321
Cdd:NF041283   75 GIVHLT-----PNLDLIAGDYDTRELGDFLADKFKSeYDRTFYLKKlldKIKDDYDFIFIDVPPSTDIKVDNAMVAADYV 149

                         170       180
                  ....*....|....*....|...
gi 1361103443 322 VIPSDLKPFANQGlptVKEFIKT 344
Cdd:NF041283  150 IVIQETQQFAFEG---SKKLILT 169
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 138-323 1.51e-15

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 78.18  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 138 RDFLQQRLKDRLSLPqteiFPTSARKISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLI 217
Cdd:PRK13869   96 RQMLAGSTRGRESID----FVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 218 KfqfeEDDDIRDRNVYHAIA-SSDRDFIEELVRkSSYFNepEIDVLPAHIDLIKYQEFLTTKMASR--------NRLLAK 288
Cdd:PRK13869  172 P----ETDVGANETLYAAIRyDDTRRPLRDVIR-PTYFD--GLHLVPGNLELMEFEHTTPKALSDKgtrdglffTRVAQA 244

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1361103443 289 LKRIENSYDFVIIDTPPSRDIYAEAALITADYLVI 323
Cdd:PRK13869  245 FDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
COG2810 COG2810
Predicted type IV restriction endonuclease [Defense mechanisms];
9-274 1.62e-10

Predicted type IV restriction endonuclease [Defense mechanisms];


Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 62.30  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443   9 RNESEVESKLIvGYLLPKLGYS---PDTWHQEVRFGKIRLDFLaftqklpLKSDDRspLGLVIEAKHPRKNL-DKHVYQI 84
Cdd:COG2810    26 ANEAATRQEFI-DPLLEALGWDidnPEEVIPEERVEGGRPDYA-------LRLNGK--RKLFVEAKKPGVNLkDKPARQA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443  85 QSYLTSLNIAYGLLTNGKELRIYQ-QVAGSARLI-------FRCAVKDIGDRLPELIQLIGRDFLQQRLKDRLSLPQTEI 156
Cdd:COG2810    96 RSYAWSSGVRWAILTNGREWRVYDaQEKTSPRPIeldtaleARLLLLEYEELSSELDLILSRIIVDTDLLARLTLGLLDS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 157 FPTSARK---ISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQaNTTFATGLIKFQFEED-------DD 226
Cdd:COG2810   176 ELKERKLlsdSDPLLLEIDARLKETLGTAIKSTVLSGPILTDLREDRELSVVGL-SKSLDELLEELELKKDadevlkgLG 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1361103443 227 IRDRNVYHaiASSDRDFIEELVRKSSYFNEPEIDVLPAHIDLIKYQEF 274
Cdd:COG2810   255 PPDRKYSG--RSLRRSKSEVLGIKDDIAISIYLLLLPLVTLELVLKLI 300
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 56-118 6.76e-05

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: 41.81  E-value: 6.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1361103443  56 LKSDDRSPLgLVIEAKHPR-KNLDKHVYQIQSYLTSLNIAYGLLTNGKELRIYQQVAGSARLIF 118
Cdd:pfam13588  43 VYNKDGKPY-ILVECKAPSiKISQKVFDQLARYNSVLGAPFLVVTNGLQHICFKVDYDKQQFEF 105
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 173-209 6.55e-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: 39.09  E-value: 6.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1361103443 173 YHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQAN 209
Cdd:NF041417   17 FSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPN 53
 
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 ...
 167-348 1.65e-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: 205.51  E-value: 1.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLIKFQfeedddiRDRNVYHAIAssDRDFIEE 246
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNN-------VEKTIYELLI--GECNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 LVRKSSYFNepeIDVLPAHIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSD 326
Cdd:pfam13614  72 AIIKTVIEN---LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148

                         170       180
                  ....*....|....*....|....*.
gi 1361103443 327 LKPFANQGLP----TVKEFIKTINEN 348
Cdd:pfam13614 149 CEYYALEGLSqllnTIKLVKKRLNPS 174
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 167-455 7.95e-62

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: 201.24  E-value: 7.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLikfqfeeDDDIRDRNVYHAIAssDRDFIEE 246
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL-------DPDDLDPTLYDLLL--DDAPLED 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 LVRKSSYfnePEIDVLPAHIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSD 326
Cdd:COG1192    72 AIVPTEI---PGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 327 LKPFANQGLptvKEFIKTINENRETFGRqPLELLGVLASKISTNAqylkySFPKQ-RAVISERYELPLIESVIYDRTALS 405
Cdd:COG1192   149 PEYLSLEGL---AQLLETIEEVREDLNP-KLEILGILLTMVDPRT-----RLSREvLEELREEFGDKVLDTVIPRSVALA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1361103443 406 ACFNqtivvgdieypNPQSIFKYADTHNstsqtSALEFEVLANEILNKVK 455
Cdd:COG1192   220 EAPS-----------AGKPVFEYDPKSK-----GAKAYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 170-412 5.08e-36

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: 132.47  E-value: 5.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 170 IAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLikfqfEEDDDIRDRNVYHAIASSD--RDFIeeL 247
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGL-----EGDIAPALQALAEGLKGRVnlDPIL--L 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 248 VRKSSYFNepeIDVLPAHIDLIKYqEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDL 327
Cdd:pfam01656  74 KEKSDEGG---LDLIPGNIDLEKF-EKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 328 KPFANQGLptvKEFIKTINENRETFGRQPLELLGVLASKISTNAQYLKYSfpkqRAVISERYELPLIeSVIYDRTALS-- 405
Cdd:pfam01656 150 EVILVEDA---KRLGGVIAALVGGYALLGLKIIGVVLNKVDGDNHGKLLK----EALEELLRGLPVL-GVIPRDEAVAea 221


                  ....*..
gi 1361103443 406 ACFNQTI 412
Cdd:pfam01656 222 PARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 168-375 5.46e-28

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: 107.63  E-value: 5.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTfatglikfqfeedddirdrnvyhaiassdrdfieel 247
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 248 vrkssyfnepeidvlpahidlikyqeflttkmasrnrllaklkriENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDL 327
Cdd:cd02042    45 ---------------------------------------------SWLYDYILIDTPPSLGLLTRNALAAADLVLIPVQP 79

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1361103443 328 KPFANQGLptvKEFIKTINENRETFGRqPLELLGVLASKISTNAQYLK 375
Cdd:cd02042    80 SPFDLDGL---AKLLDTLEELKKQLNP-PLLILGILLTRVDPRTKLAR 123
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 128-410 6.87e-21

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: 93.64  E-value: 6.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 128 RLPELIQLIGRDFLQQRLKDRLSLPQTEIFPTSARKISSM-----KTIAIYHNKGGVGKTTVSTNLAAAFSR-KGYRTLL 201
Cdd:COG4963    58 PTPNLILLEALSESAALLADVLPLSPDELRAALARLLDPGaarrgRVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 202 IDIDGQanttFATGLIKFQFEEDDDIRDrnvyhAIASSDR---DFIEELVRKSSyfnePEIDVLPA-----HIDLIKYQE 273
Cdd:COG4963   138 VDLDLQ----FGDVALYLDLEPRRGLAD-----ALRNPDRldeTLLDRALTRHS----SGLSVLAApadleRAEEVSPEA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 274 FLttkmasrnRLLAKLKRienSYDFVIIDTPPSRDIYAEAALITADYLVIPSDlkpfanQGLPTVKEFIKTINEnretfg 353
Cdd:COG4963   205 VE--------RLLDLLRR---HFDYVVVDLPRGLNPWTLAALEAADEVVLVTE------PDLPSLRNAKRLLDL------ 261

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1361103443 354 rqpLELLGVLASKIST--NaQYLKYSFPKqRAVISERYELPLIESVIYDRTALSACFNQ 410
Cdd:COG4963   262 ---LRELGLPDDKVRLvlN-RVPKRGEIS-AKDIEEALGLPVAAVLPNDPKAVAEAANQ 315
ParA_partition NF041546
ParA family partition ATPase;
169-324 5.97e-20

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.61  E-value: 5.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 169 TIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTtfatglikfqfeedddiRDrnvYHAIASSDRDFieelv 248
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA-----------------LD---WAAAREDERPF----- 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1361103443 249 rkssyfnePEIDVlpahidlikyqeflttkmaSRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIP 324
Cdd:NF041546   56 --------PVVGL-------------------ARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIP 104
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 138-306 1.11e-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: 84.26  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 138 RDFLQQRLKDRLS-LPQTeifptsaRKISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTtfaTGL 216
Cdd:TIGR03453  81 RRHLAQRGREARRyLPHR-------RGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASL---SAL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 217 IKFQFEEDDDiRDRNVYHAIASSD-RDFIEELVRKsSYFnePEIDVLPAHIDLIKYQEFLTTKMASRN--------RLLA 287
Cdd:TIGR03453 151 FGYQPEFDVG-ENETLYGAIRYDDeRRPISEIIRK-TYF--PGLDLVPGNLELMEFEHETPRALSRGQggdtiffaRVGE 226

                         170
                  ....*....|....*....
gi 1361103443 288 KLKRIENSYDFVIIDTPPS 306
Cdd:TIGR03453 227 ALAEVEDDYDVVVIDCPPQ 245
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
169-344 3.19e-17

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 81.72  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 169 TIAIYHNKGGVGKTTVSTNLA-AAFSRKGYRTLLIDIDGQANTTFatgLIKFQFEedddirDRNVYHAIASS--DRDFIE 245
Cdd:NF041283    4 VIVLANQKGGVGKTTDTVMEAvVASSVFNKKVLVIDTDLQGNATQ---FLSKTFN------VPNFPQSFMKCveDGDLEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 246 ELVRKSsyfnePEIDVLPAHIDLIKYQEFLTTKMAS-RNRLLAKLK---RIENSYDFVIIDTPPSRDIYAEAALITADYL 321
Cdd:NF041283   75 GIVHLT-----PNLDLIAGDYDTRELGDFLADKFKSeYDRTFYLKKlldKIKDDYDFIFIDVPPSTDIKVDNAMVAADYV 149

                         170       180
                  ....*....|....*....|...
gi 1361103443 322 VIPSDLKPFANQGlptVKEFIKT 344
Cdd:NF041283  150 IVIQETQQFAFEG---SKKLILT 169
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 168-305 4.68e-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: 4.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGLIKfqfeedddirDRNVYHAIaSSDRDFIEE 246
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAP----------KKTLGDVL-KGRVSLEDI 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1361103443 247 LVRKssyfnEPEIDVLPAHIDlikYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPP 305
Cdd:cd02038    70 IVEG-----PEGLDIIPGGSG---MEELANLDPEQKAKLIEELSSLESNYDYLLIDTGA 120
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 138-323 1.51e-15

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 78.18  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 138 RDFLQQRLKDRLSLPqteiFPTSARKISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGLI 217
Cdd:PRK13869   96 RQMLAGSTRGRESID----FVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 218 KfqfeEDDDIRDRNVYHAIA-SSDRDFIEELVRkSSYFNepEIDVLPAHIDLIKYQEFLTTKMASR--------NRLLAK 288
Cdd:PRK13869  172 P----ETDVGANETLYAAIRyDDTRRPLRDVIR-PTYFD--GLHLVPGNLELMEFEHTTPKALSDKgtrdglffTRVAQA 244

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1361103443 289 LKRIENSYDFVIIDTPPSRDIYAEAALITADYLVI 323
Cdd:PRK13869  245 FDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 183-453 7.16e-15

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: 73.77  E-value: 7.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 183 TVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGLikfqfeedddIRDRNVYHAIASSDRdfIEELVRKSsyfnEPEIDV 261
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADlGLANLDVLLGL----------EPKATLADVLAGEAD--LEDAIVQG----PGGLDV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 262 LPAHIDLIKYQEFLttkmaSRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDLKPfanQGLPTVKEF 341
Cdd:COG0455    65 LPGGSGPAELAELD-----PEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEP---TSITDAYAL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 342 IKTINEnretfgRQPLELLGVLASKISTNAQYLKySFPKQRAVISERY--ELPLIESVIYDRTALSACFNQTIVVgdIEY 419
Cdd:COG0455   137 LKLLRR------RLGVRRAGVVVNRVRSEAEARD-VFERLEQVAERFLgvRLRVLGVIPEDPAVREAVRRGRPLV--LAA 207

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1361103443 420 PNPQsifkyadthnstsqtSALEFEVLANEILNK 453
Cdd:COG0455   208 PDSP---------------AARAIRELAARLAGW 226
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 169-305 6.15e-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: 72.14  E-value: 6.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 169 TIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDidgqANTTFATGLIKFQFEEDDDIRDrnvyhaiASSDRDFIEELV 248
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLID----ADLRGPSLHRMLGLENRPGLSD-------VLAGEASLEDVI 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1361103443 249 RKSSYFNepeIDVLPAHIDLIKYQEFLttkmaSRNRLLAKLKRIENSYDFVIIDTPP 305
Cdd:COG0489   163 QPTEVEG---LDVLPAGPLPPNPSELL-----ASKRLKQLLEELRGRYDYVIIDTPP 211
PHA02518 PHA02518
ParA-like protein; Provisional
 168-418 1.76e-13

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 69.11  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTfatglikfqfeedddirdrnvyhaiassdrDFIEEl 247
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST------------------------------DWAEA- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 248 vRKSsyfNEPEIDVlpahidlikyqeflttkMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDL 327
Cdd:PHA02518   50 -REE---GEPLIPV-----------------VRMGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQP 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 328 KPFANQGLPTVKEFIKTINENREtfgRQPlellgvlaskistnaqylKYSFPKQRAV-----------ISERYELPLIES 396
Cdd:PHA02518  109 SPFDIWAAPDLVELIKARQEVTD---GLP------------------KFAFIISRAIkntqlyrearkALAGYGLPILRN 167

                         250       260
                  ....*....|....*....|..
gi 1361103443 397 VIYDRTALSACFNQTIVVGDIE 418
Cdd:PHA02518  168 GTTQRVAYADAAEAGGSVLELP 189
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 168-323 7.74e-13

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: 68.00  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGLikfqfeedddiRDRNVY--HAIASSDRDFI 244
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGL-----------ENRIVYtlVDVLEGECRLE 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361103443 245 EELVRKSsyfNEPEIDVLPAHIDLIKYqeflttkMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVI 323
Cdd:cd02036    70 QALIKDK---RWENLYLLPASQTRDKD-------ALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAII 138
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 167-326 3.91e-12

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: 65.83  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQanttfatGLIKFQFEEDDDIRDrnVYHAIASSDRDFiee 246
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ-------NLLRLHFGMDWSVRD--GWARALLNGADW--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 lvRKSSYFNEPEIDVLP-AHIDLIKYQEFLTTKMASRNRLLAKLKRieNSYDFVIIDTPPSRDIYAEAALITADYL--VI 323
Cdd:TIGR03371  69 --AAAAYRSPDGVLFLPyGDLSADEREAYQAHDAGWLARLLQQLDL--AARDWVLIDLPRGPSPITRQALAAADLVlvVV 144


                  ...
gi 1361103443 324 PSD 326
Cdd:TIGR03371 145 NAD 147
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 168-323 5.20e-12

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: 65.52  E-value: 5.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGLikfqfeEDDDIRDRNVYHAIASsdrdfiee 246
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGM------EDKPVTLHDVLAGEAD-------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1361103443 247 lVRKSSYFNEPEIDVLPAHIDLIKYqeflttKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVI 323
Cdd:TIGR01969  67 -IKDAIYEGPFGVKVIPAGVSLEGL------RKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLL 136
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 168-429 9.18e-12

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: 64.61  E-value: 9.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFS-RKGYRTLLIDIDGQanttFATGLIKFQFEEDDDIRDrnvyhAIASSDR-DfiE 245
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDLP----FGDLGLYLNLRPDYDLAD-----VIQNLDRlD--R 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 246 ELVRKSSYFNEPEIDVLPAHIDLIKYQEFlttkmaSRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIps 325
Cdd:cd03111    70 TLLDSAVTRHSSGLSLLPAPQELEDLEAL------GAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILL-- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 326 dlkpFANQGLPTVKEFIKTINENRET-FGRQPLELlgvLASKISTNAQYLkysfPKQravISERYELPLIESVIYDRTAL 404
Cdd:cd03111   142 ----VTQQDLPSLRNARRLLDSLRELeGSSDRLRL---VLNRYDKKSEIS----PKD---IEEALGLEVFATLPNDYKAV 207

                         250       260
                  ....*....|....*....|....*
gi 1361103443 405 SACFNQTIVVGDieyPNPQSIFKYA 429
Cdd:cd03111   208 SESANTGRPLVE---VAPRSALVRA 229
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 167-318 2.30e-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: 62.59  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIdgqanttfatglikfqfeeddDIRDRNVYHAI-ASSDRDFIE 245
Cdd:cd05387    19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDA---------------------DLRRPSLHRLLgLPNEPGLSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 246 ELVRKSSY------FNEPEIDVLPAHidliKYQEFLTTKMASRN--RLLAKLKRienSYDFVIIDTPPSrDIYAEAALIT 317
Cdd:cd05387    78 VLSGQASLedviqsTNIPNLDVLPAG----TVPPNPSELLSSPRfaELLEELKE---QYDYVIIDTPPV-LAVADALILA 149


                  .
gi 1361103443 318 A 318
Cdd:cd05387   150 P 150
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 170-205 8.69e-11

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: 61.36  E-value: 8.69e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1361103443 170 IAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID 205
Cdd:cd02037     3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
COG2810 COG2810
Predicted type IV restriction endonuclease [Defense mechanisms];
9-274 1.62e-10

Predicted type IV restriction endonuclease [Defense mechanisms];


Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 62.30  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443   9 RNESEVESKLIvGYLLPKLGYS---PDTWHQEVRFGKIRLDFLaftqklpLKSDDRspLGLVIEAKHPRKNL-DKHVYQI 84
Cdd:COG2810    26 ANEAATRQEFI-DPLLEALGWDidnPEEVIPEERVEGGRPDYA-------LRLNGK--RKLFVEAKKPGVNLkDKPARQA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443  85 QSYLTSLNIAYGLLTNGKELRIYQ-QVAGSARLI-------FRCAVKDIGDRLPELIQLIGRDFLQQRLKDRLSLPQTEI 156
Cdd:COG2810    96 RSYAWSSGVRWAILTNGREWRVYDaQEKTSPRPIeldtaleARLLLLEYEELSSELDLILSRIIVDTDLLARLTLGLLDS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 157 FPTSARK---ISSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQaNTTFATGLIKFQFEED-------DD 226
Cdd:COG2810   176 ELKERKLlsdSDPLLLEIDARLKETLGTAIKSTVLSGPILTDLREDRELSVVGL-SKSLDELLEELELKKDadevlkgLG 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1361103443 227 IRDRNVYHaiASSDRDFIEELVRKSSYFNEPEIDVLPAHIDLIKYQEF 274
Cdd:COG2810   255 PPDRKYSG--RSLRRSKSEVLGIKDDIAISIYLLLLPLVTLELVLKLI 300
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 168-205 1.22e-09

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: 58.62  E-value: 1.22e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID 205
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 167-317 3.61e-09

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 56.68  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANT---TFA-----TGLIKFQFEEDDdirdrnVYHAIAS 238
Cdd:TIGR01007  17 IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVmsgTFKsqnkiTGLTNFLSGTTD------LSDAICD 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361103443 239 SDrdfIEELvrkssyFNEPEIDVLPAHIDLIKYQEFLTTKMASRNRllaklkriensYDFVIIDTPPSrDIYAEAALIT 317
Cdd:TIGR01007  91 TN---IENL------DVITAGPVPPNPTELLQSSNFKTLIETLRKR-----------FDYIIIDTPPI-GTVTDAAIIA 148
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 168-205 9.76e-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: 52.82  E-value: 9.76e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID 205
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 168-323 1.06e-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: 55.81  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGLikfqfeedddiRDRNVYHAIassdrDFIE- 245
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiGLRNLDLLLGL-----------ENRIVYTLV-----DVVEg 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 246 ------ELVRKSSYFNepeIDVLPAHIDLIKYqeflttkMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITAD 319
Cdd:TIGR01968  66 ecrlqqALIKDKRLKN---LYLLPASQTRDKD-------AVTPEQMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPAD 135


                  ....
gi 1361103443 320 YLVI 323
Cdd:TIGR01968 136 EAIV 139
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 176-305 2.27e-08

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: 54.82  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGlIKFQFEEDDDIRDR------NVYHAIASSDRDFIEELVR 249
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFG-QKLGGETPVKGAPNlwameiDPEEALEEYWEEVKELLAQ 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1361103443 250 kssYFNEPEIDVLpahidlikYQEFL-----TTKMASrnrlLAKLKRI--ENSYDFVIIDTPP 305
Cdd:cd02035    87 ---YLRLPGLDEV--------YAEELlslpgMDEAAA----FDELREYveSGEYDVIVFDTAP 134
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 176-324 3.18e-08

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: 54.38  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDIDgqanttfatglikfqfeedddIRDRNVYHaiassdrdFIEElvrKSSYFN 255
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDLD---------------------LRQRTFHR--------YFEN---RSATAD 56

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1361103443 256 EPEIDV-LPAHIDLIKYQEFLTTKMAS--RNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIP 324
Cdd:pfam09140  57 RTGLSLpTPEHLNLPDNDVAEVPDGENidDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTP 128
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
167-307 3.81e-08

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 54.44  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-----GQAnttfatglikFQFEEDDD---IRDRNVY----- 233
Cdd:COG0003     2 MTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDpahslGDV----------LGTELGNEpteVAVPNLYaleid 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 234 --HAIassdRDFIEELVRK-SSYFNEPEIDVLPahidlikyqEFL--TTKMASrnrlLAKLKRI--ENSYDFVIIDTPPS 306
Cdd:COG0003    72 peAEL----EEYWERVRAPlRGLLPSAGVDELA---------ESLpgTEELAA----LDELLELleEGEYDVIVVDTAPT 134


                  .
gi 1361103443 307 R 307
Cdd:COG0003   135 G 135
minD CHL00175
septum-site determining protein; Validated
 168-323 4.49e-08

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 54.39  E-value: 4.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGLikfqfeedddiRDRNVYHA--IASSDRDFI 244
Cdd:CHL00175   16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGL-----------ENRVLYTAmdVLEGECRLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 245 EELVRKSSYfnePEIDVLPAHIDLIKYQeflttkmASRNRLLAKLKRIEN-SYDFVIIDTPPSRDIYAEAALITADYLVI 323
Cdd:CHL00175   85 QALIRDKRW---KNLSLLAISKNRQRYN-------VTRKNMNMLVDSLKNrGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 168-205 4.68e-08

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 53.91  E-value: 4.68e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID 205
Cdd:COG2894     3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 168-246 6.63e-08

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 53.81  E-value: 6.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361103443 168 KTIAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFAtgLIKFQFEEDDDIRDRNVYHAIASSDRDFIEE 246
Cdd:PRK13185    3 LVLAVY-GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFT--LTGKLVPTVIDILEEVDFHSEELRPEDFVYE 78
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 168-246 7.08e-08

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: 53.46  E-value: 7.08e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361103443 168 KTIAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFAtgLIKFQFEEDDDIRDRNVYHAIASSDRDFIEE 246
Cdd:cd02032     1 LVIAVY-GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFT--LTGFLIPTVIDVLQSVDFHYEEVWPEDVIFT 76
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 128-370 8.41e-08

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 54.21  E-value: 8.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 128 RLPEL-IQLIGRdfLQQRLKdrLSLPQT----EIFPTSARKISSMK--TIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTL 200
Cdd:PRK13705   64 RLPHPdMEMRGR--VEQRVG--YTIEQInhmrDVFGTRLRRAEDVFppVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 201 LID-IDGQANTTFATGLIKfqfeeDDDIRDRNVYHAIASSDRDFIEELVRKSSYfnePEIDVLPAHIDLIK-----YQEF 274
Cdd:PRK13705  140 LVEgNDPQGTASMYHGWVP-----DLHIHAEDTLLPFYLGEKDDATYAIKPTCW---PGLDIIPSCLALHRietelMGKF 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 275 LTTKMASRNRLL--AKLKRIENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDLKPF----ANQGLPTVKEFIKTINEN 348
Cdd:PRK13705  212 DEGKLPTDPHLMlrLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFdytsALQFFDMLRDLLKNVDLK 291

                         250       260
                  ....*....|....*....|..
gi 1361103443 349 retfGRQPleLLGVLASKISTN 370
Cdd:PRK13705  292 ----GFEP--DVRILLTKYSNS 307
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 176-209 1.11e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 52.86  E-value: 1.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQAN 209
Cdd:COG3640     8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 168-213 5.18e-07

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: 50.83  E-value: 5.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1361103443 168 KTIAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFA 213
Cdd:cd02117     1 ESIVVY-GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLL 45
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 170-325 6.90e-07

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 51.17  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 170 IAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLID-IDGQANTTFATGLI-KFQFEEDDDIRDRNVyhaiasSDRDFIEEL 247
Cdd:PHA02519  109 LAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVpDLHIHADDTLLPFYL------GERDNAEYA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 248 VRKSSYfnePEIDVLPA-------HIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAALITADY 320
Cdd:PHA02519  183 IKPTCW---PGLDIIPSclalhriETDLMQYHDAGKLPHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADV 259


                  ....*
gi 1361103443 321 LVIPS 325
Cdd:PHA02519  260 IVVAT 264
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 170-211 1.03e-06

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: 49.82  E-value: 1.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1361103443 170 IAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTT 211
Cdd:cd02040     3 IAIY-GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 167-303 3.80e-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: 48.08  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKtIAIyHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTTFATGL---IKFQFEEDDDIRDRnvyhaiASSDRDF 243
Cdd:cd02034     1 MK-IAV-AGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVeveKLPLIKTIGDIRER------TGAKKGE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1361103443 244 IEELVRKSSYFNE--PEIDVLPAHIDLI---KYQEFLTTKMASRNRLLAKLKR--IENSYDFVIIDT 303
Cdd:cd02034    73 PPEGMSLNPYVDDiiKEIIVEPDGIDLLvmgRPEGGGSGCYCPVNALLRELLRhlALKNYEYVVIDM 139
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 165-378 5.60e-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: 48.95  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 165 SSMKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDgqanttfatglikfqfeedddIRDRNVYHAIASSDRD-F 243
Cdd:TIGR01005 551 AENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDAD---------------------IRKGGLHQMFGKAPKPgL 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 244 IEELVRKSSYFNEPEIDVLPAhIDLI-----KYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTPPSRDIYAEAAlita 318
Cdd:TIGR01005 610 LDLLAGEASIEAGIHRDQRPG-LAFIaaggaSHFPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAA---- 684

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1361103443 319 dylvipsdLKPFANQGLPTVKEFIKTINENRETFGRQPL---ELLGVLASKISTNaQYLKYSF 378
Cdd:TIGR01005 685 --------FAALADGILFVTEFERSPLGEIRDLIHQEPHansDVLGVIFNALDMN-ELGKYGD 738
PRK10818 PRK10818
septum site-determining protein MinD;
168-326 1.35e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 46.47  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID-GQANTTFATGL---IKFQFEedddirdrNVYHAIASSDRDF 243
Cdd:PRK10818    3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCerrVVYDFV--------NVIQGDATLNQAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 244 IEELVRKSSYfnepeidVLPAhiDLIKYQEFLTTKMASrnRLLAKLKriENSYDFVIIDTPPSRDIYAEAALITADYLVI 323
Cdd:PRK10818   75 IKDKRTENLY-------ILPA--SQTRDKDALTREGVA--KVLDDLK--AMDFEFIVCDSPAGIETGALMALYFADEAII 141


                  ...
gi 1361103443 324 PSD 326
Cdd:PRK10818  142 TTN 144
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 167-211 1.98e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 46.30  E-value: 1.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1361103443 167 MKTIAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTT 211
Cdd:PRK13230    1 MRKFCFY-GKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCT 44
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 167-211 2.16e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 45.94  E-value: 2.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1361103443 167 MKTIAIYhNKGGVGKTTVSTNLAAAFSRKgYRTLLIDIDGQANTT 211
Cdd:PRK13231    2 MKKIAIY-GKGGIGKSTTVSNMAAAYSND-HRVLVIGCDPKADTT 44
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 168-326 2.18e-05

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: 45.61  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 168 KTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDgqantTFATGLIKFQFEEDDDIRDrnVYHAIASSD---RDFI 244
Cdd:cd17869     4 SVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-----RLQSTDVFFGASGRYLMSD--HLYTLKSRKanlADKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 245 EELVRKS----SYFNEPEIdvlPAHIDLIKYQEFLttkmasrnRLLAKLKRIeNSYDFVIIDTPPSRDIYAEAALITADY 320
Cdd:cd17869    77 ESCVKQHesgvYYFSPFKS---ALDILEIKKDDIL--------HMITKLVEA-HAYDYIIMDLSFEFSSTVCKLLQASHN 144


                  ....*.
gi 1361103443 321 LVIPSD 326
Cdd:cd17869   145 NVVIAL 150
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
170-211 3.30e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 45.51  E-value: 3.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1361103443 170 IAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTT 211
Cdd:pfam00142   3 IAIY-GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADST 43
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 167-337 3.65e-05

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: 45.06  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 167 MKTIAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDgqanttfATGLIKFQFEEddDIRDRNVYHAIASSDRDFiee 246
Cdd:pfam06564   1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLS-------PDNLLRLHFNV--PFEHRQGWARAELDGADW--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 247 lvRKSSYFNEPEIDVLPAHIDLIKYQEFLTTKMASRNRLLAKLKRIENSYDFVIIDTP--PSRDIYAEAALITADYLVIP 324
Cdd:pfam06564  69 --RDAALEYTPGLDLLPFGRLSVEEQENLQQLQPDPGAWCRRLQQLKGRYDWVLFDLPagPSPLTRQLLSLADLSLLVVN 146

                         170
                  ....*....|....*.
gi 1361103443 325 SDLKP---FANQGLPT 337
Cdd:pfam06564 147 PDANChvlLHQQPLPD 162
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 56-118 6.76e-05

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: 41.81  E-value: 6.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1361103443  56 LKSDDRSPLgLVIEAKHPR-KNLDKHVYQIQSYLTSLNIAYGLLTNGKELRIYQQVAGSARLIF 118
Cdd:pfam13588  43 VYNKDGKPY-ILVECKAPSiKISQKVFDQLARYNSVLGAPFLVVTNGLQHICFKVDYDKQQFEF 105
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 176-205 8.44e-05

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: 44.26  E-value: 8.44e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDID 205
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 176-306 1.62e-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: 43.92  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQA--NTTFATGLIKFQF------EEDDDIRDR---NVYHAIASSDRDFI 244
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAhlSVTLTGSLNNLQVsridpkQETERYRQEvlaTKGKELDEDGKAYL 408

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1361103443 245 EELVRksSYFNEpEIDVLPAHIDLIKyqeflttkmasrnrllaklkriENSYDFVIIDTPPS 306
Cdd:TIGR04291 409 EEDLR--SPCTE-EIAVFQAFSRIIR----------------------EAGDRFVVMDTAPT 445
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 141-211 2.05e-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: 43.28  E-value: 2.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1361103443 141 LQQRLKDRLSLPQTEIFPTSARKiSSMKTIAIYhNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQANTT 211
Cdd:cd02033     6 FDARLRDEAAIEPSLEIPTGPPT-KETQIIAIY-GKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTT 74
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 170-331 4.84e-04

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: 41.60  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 170 IAIYHNKGGVGKTTVSTNLAAAFsrkgYRTLLIDIDGQA-NTTFATGlIKFQFEEDddirdrNVYHAIASSDRD-FIE-- 245
Cdd:cd03110     2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDApNLHLLLG-PEPEEEED------FVGGKKAFIDQEkCIRcg 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361103443 246 --ELVRK----SSYFNEPEIDVLPAH-------------IDLIK----YQEFLTTK----------MASRN--RLLAKLK 290
Cdd:cd03110    71 ncERVCKfgaiLEFFQKLIVDESLCEgcgacviicprgaIYLKDrdtgKIFISSSDggplvhgrlnIGEENsgKLVTELR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1361103443 291 RI----ENSYDFVIIDTPPSRDIYAEAALITADYLVIPSDLKPFA 331
Cdd:cd03110   151 KKalerSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSG 195
PRK13886 PRK13886
conjugal transfer protein TraL; Provisional
 176-244 9.63e-04

conjugal transfer protein TraL; Provisional


Pssm-ID: 184370  Cd Length: 241  Bit Score: 40.87  E-value: 9.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDIDgQANTTF----ATGLIKFQFEEDDDIRDRN---VYHAIASSDRDFI 244
Cdd:PRK13886   11 KGGVGKSFIAATIAQYKASKGQKPLCIDTD-PVNATFegykALNVRRLNIMDGDEINTRNfdaLVEMIASTEGDVI 85
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 176-244 1.70e-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: 1.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1361103443 176 KGGVGKTTVSTNLAAAFSRKGYRTLLIDIDgQANTTFAT--GLI--KFQFEEDDDIRDRN---VYHAIASSDRDFI 244
Cdd:cd05386     9 KGGVGKSVIASLLAQYLIDKGQPVSCIDTD-PVNKTFAGykALNvqRINIIDNDEIIQSKfdqLVEQFLAEDGTVV 83
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
 177-198 1.81e-03

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: 40.48  E-value: 1.81e-03
                          10        20
                  ....*....|....*....|..
gi 1361103443 177 GGVGKTTVSTNLAAAFSRKGYR 198
Cdd:COG1797    13 SGSGKTTVTLGLLAALRRRGLK 34
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
178-198 1.89e-03

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 40.50  E-value: 1.89e-03
                          10        20
                  ....*....|....*....|.
gi 1361103443 178 GVGKTTVSTNLAAAFSRKGYR 198
Cdd:PRK01077   14 GSGKTTVTLGLMRALRRRGLR 34
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
170-205 2.91e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 39.64  E-value: 2.91e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1361103443 170 IAIYHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDID 205
Cdd:PRK11670  110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 173-209 6.55e-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: 39.09  E-value: 6.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1361103443 173 YHNKGGVGKTTVSTNLAAAFSRKGYRTLLIDIDGQAN 209
Cdd:NF041417   17 FSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPN 53
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 178-209 8.76e-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: 37.23  E-value: 8.76e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1361103443 178 GVGKTTVSTNLAAAFSRKGYRTLLIDID-GQAN 209
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDvGQSE 36
 
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