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Conserved domains on  [gi|1199647637|ref|WP_087380342|]
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ParA family protein [Anaeromassilibacillus sp. An172]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
SCOP:  4003982

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
11-259 3.36e-86

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: 257.09  E-value: 3.36e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGL-FDDNNPGIYEVMKSEKNPKDCILKTKIENLFL 89
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLdPDDLDPTLYDLLLDDAPLEDAIVPTEIPGLDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  90 LPSKHELRNIETVLMMKTKRqEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAK 169
Cdd:COG1192    84 IPANIDLAGAEIELVSRPGR-ELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 170 EIVEIKQFTNPNLKIMGILICMME-QTKSKKAYADALKTQDIFPCFETVIRKNTTLQEAINAHVPVHRYDKRSNGAKDYM 248
Cdd:COG1192   163 TIEEVREDLNPKLEILGILLTMVDpRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYR 242
                         250
                  ....*....|.
gi 1199647637 249 ALTEEIIKIVK 259
Cdd:COG1192   243 ALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
11-259 3.36e-86

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: 257.09  E-value: 3.36e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGL-FDDNNPGIYEVMKSEKNPKDCILKTKIENLFL 89
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLdPDDLDPTLYDLLLDDAPLEDAIVPTEIPGLDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  90 LPSKHELRNIETVLMMKTKRqEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAK 169
Cdd:COG1192    84 IPANIDLAGAEIELVSRPGR-ELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 170 EIVEIKQFTNPNLKIMGILICMME-QTKSKKAYADALKTQDIFPCFETVIRKNTTLQEAINAHVPVHRYDKRSNGAKDYM 248
Cdd:COG1192   163 TIEEVREDLNPKLEILGILLTMVDpRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYR 242
                         250
                  ....*....|.
gi 1199647637 249 ALTEEIIKIVK 259
Cdd:COG1192   243 ALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
8-184 8.52e-56

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: 177.01  E-value: 8.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   8 STKIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDN-NPGIYEVMKSEKNPKDCILKTKIEN 86
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNvEKTIYELLIGECNIEEAIIKTVIEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  87 LFLLPSKHELRNIETVLMMKTKRqEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLC 166
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENR-ENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQ 159
                         170
                  ....*....|....*...
gi 1199647637 167 IAKEIVEIKQFTNPNLKI 184
Cdd:pfam13614 160 LLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
11-206 1.49e-33

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: 118.41  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYglfddnnpgiyevmkseknpkdcilktkienlfll 90
Cdd:cd02042     3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL----------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 pskhelrnietvlmmktkrqeytlqmalkeieadYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAKE 170
Cdd:cd02042    48 ----------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDT 93
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1199647637 171 IVEIKQFTNPNLKIMGILICMMEQ-TKSKKAYADALK 206
Cdd:cd02042    94 LEELKKQLNPPLLILGILLTRVDPrTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
11-135 1.12e-22

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: 95.43  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGL---FD-DNNPGIYEVMK--SEKNP-KDCILKTK 83
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpeFDvGENETLYGAIRydDERRPiSEIIRKTY 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1199647637  84 IENLFLLPSKHELRNIE--TVLMMKTKRQEYT-----LQMALKEIEADYDFIIFDCPPS 135
Cdd:TIGR03453 187 FPGLDLVPGNLELMEFEheTPRALSRGQGGDTiffarVGEALAEVEDDYDVVVIDCPPQ 245
ParA_partition NF041546
ParA family partition ATPase;
11-253 5.38e-20

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 84.91  E-value: 5.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPGIYEVMKSEKNPKDcilktkienlfll 90
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLARPTLHRE------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 pskhelrnietvlmmktkrqeytlqmaLKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIP---DDYALHGLLCI 167
Cdd:NF041546   69 ---------------------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPspyDLWASADTVDL 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 168 AKEiveiKQFTNPNLKIMGILICMMEQTKSKKAYADALKTQDiFPCFETVIRKNTTLQEAINAHVPVHRYDKRSNGAKDY 247
Cdd:NF041546  122 IKE----AREYTPGLKAAFVLNRAIARTALGREVAEALAEYG-LPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREI 196

                  ....*.
gi 1199647637 248 MALTEE 253
Cdd:NF041546  197 RALAKE 202
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
7-151 2.61e-15

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 74.02  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   7 MSTKIAITYEKGGCGKTTTAVNLSAMLADK-GYKTLLVDLDFQSYATSYYGL-FddNNPGIYEVMKSEKNPKDciLKTKI 84
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATQFLSKtF--NVPNFPQSFMKCVEDGD--LEKGI 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199647637  85 ----ENLFLLPSKHELRNIETVLMMKTKR---QEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVI 151
Cdd:NF041283   77 vhltPNLDLIAGDYDTRELGDFLADKFKSeydRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVI 150
PHA02518 PHA02518
ParA-like protein; Provisional
11-260 4.25e-15

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 71.80  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYyglfddnnpgiyevmkSEKNPKDCILktkienlfll 90
Cdd:PHA02518    3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW----------------AEAREEGEPL---------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 pskhelrnIETVLMMKTKRQEytlqmaLKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAkE 170
Cdd:PHA02518   57 --------IPVVRMGKSIRAD------LPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV-E 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 171 IVEIKQFTNPNLKIMGILIcmMEQTKSKKAYADALKTQD-----IFPCFETviRKNtTLQEAINAHVPVHRYDKRSNGAk 245
Cdd:PHA02518  122 LIKARQEVTDGLPKFAFII--SRAIKNTQLYREARKALAgyglpILRNGTT--QRV-AYADAAEAGGSVLELPEDDKAA- 195
                         250
                  ....*....|....*
gi 1199647637 246 dymaltEEIIKIVKE 260
Cdd:PHA02518  196 ------EEIIQLVKE 204
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
17-56 7.81e-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: 37.55  E-value: 7.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYG 56
Cdd:NF041417  341 KGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFG 380
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
11-259 3.36e-86

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: 257.09  E-value: 3.36e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGL-FDDNNPGIYEVMKSEKNPKDCILKTKIENLFL 89
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLdPDDLDPTLYDLLLDDAPLEDAIVPTEIPGLDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  90 LPSKHELRNIETVLMMKTKRqEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAK 169
Cdd:COG1192    84 IPANIDLAGAEIELVSRPGR-ELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 170 EIVEIKQFTNPNLKIMGILICMME-QTKSKKAYADALKTQDIFPCFETVIRKNTTLQEAINAHVPVHRYDKRSNGAKDYM 248
Cdd:COG1192   163 TIEEVREDLNPKLEILGILLTMVDpRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYR 242
                         250
                  ....*....|.
gi 1199647637 249 ALTEEIIKIVK 259
Cdd:COG1192   243 ALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
8-184 8.52e-56

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: 177.01  E-value: 8.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   8 STKIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDN-NPGIYEVMKSEKNPKDCILKTKIEN 86
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNvEKTIYELLIGECNIEEAIIKTVIEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  87 LFLLPSKHELRNIETVLMMKTKRqEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLC 166
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENR-ENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQ 159
                         170
                  ....*....|....*...
gi 1199647637 167 IAKEIVEIKQFTNPNLKI 184
Cdd:pfam13614 160 LLNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
11-234 1.50e-38

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: 134.40  E-value: 1.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPG---IYEVMKSEKNPKDCILKTKIE-- 85
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPAlqaLAEGLKGRVNLDPILLKEKSDeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  86 NLFLLPSKHELRNIETVLMMKTKrqEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHG-- 163
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRK--EERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDak 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199647637 164 -LLCIAKEIVeiKQFTNPNLKIMGILICMMEQTKSKKAYADALKTQDI-FPCFeTVIRKNTTLQEAINAHVPV 234
Cdd:pfam01656 159 rLGGVIAALV--GGYALLGLKIIGVVLNKVDGDNHGKLLKEALEELLRgLPVL-GVIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
11-206 1.49e-33

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: 118.41  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYglfddnnpgiyevmkseknpkdcilktkienlfll 90
Cdd:cd02042     3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL----------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 pskhelrnietvlmmktkrqeytlqmalkeieadYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAKE 170
Cdd:cd02042    48 ----------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDT 93
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1199647637 171 IVEIKQFTNPNLKIMGILICMMEQ-TKSKKAYADALK 206
Cdd:cd02042    94 LEELKKQLNPPLLILGILLTRVDPrTKLAREVLEELK 130
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
11-198 4.26e-27

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: 106.04  E-value: 4.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDF-QSYATSYYGLfdDNNPGIYEVMKSEKNPKDCILKTKIENLFL 89
Cdd:COG0489    95 IAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGL--ENRPGLSDVLAGEASLEDVIQPTEVEGLDV 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  90 LPSKHELRNIETVLMMKtkrqeyTLQMALKEIEADYDFIIFDCPPSGE----RIkenALTCCDYVILPCIPDDyalhgll 165
Cdd:COG0489   173 LPAGPLPPNPSELLASK------RLKQLLEELRGRYDYVIIDTPPGLGvadaTL---LASLVDGVLLVVRPGK------- 236
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1199647637 166 cIAKEIVE--IKQFTNPNLKIMGILICMMEQTKSK 198
Cdd:COG0489   237 -TALDDVRkaLEMLEKAGVPVLGVVLNMVCPKGER 270
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
11-135 1.12e-22

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: 95.43  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGL---FD-DNNPGIYEVMK--SEKNP-KDCILKTK 83
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpeFDvGENETLYGAIRydDERRPiSEIIRKTY 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1199647637  84 IENLFLLPSKHELRNIE--TVLMMKTKRQEYT-----LQMALKEIEADYDFIIFDCPPS 135
Cdd:TIGR03453 187 FPGLDLVPGNLELMEFEheTPRALSRGQGGDTiffarVGEALAEVEDDYDVVVIDCPPQ 245
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
11-136 2.86e-21

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: 88.01  E-value: 2.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDF-QSYATSYYGLfdDNNPGIYEVMKSEKNPKDCILKTKIENLFL 89
Cdd:cd05387    22 IAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGL--PNEPGLSEVLSGQASLEDVIQSTNIPNLDV 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1199647637  90 LPSKHELRNIETVLmmktkrQEYTLQMALKEIEADYDFIIFDCPPSG 136
Cdd:cd05387   100 LPAGTVPPNPSELL------SSPRFAELLEELKEQYDYVIIDTPPVL 140
ParA_partition NF041546
ParA family partition ATPase;
11-253 5.38e-20

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 84.91  E-value: 5.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPGIYEVMKSEKNPKDcilktkienlfll 90
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLARPTLHRE------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 pskhelrnietvlmmktkrqeytlqmaLKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIP---DDYALHGLLCI 167
Cdd:NF041546   69 ---------------------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPspyDLWASADTVDL 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 168 AKEiveiKQFTNPNLKIMGILICMMEQTKSKKAYADALKTQDiFPCFETVIRKNTTLQEAINAHVPVHRYDKRSNGAKDY 247
Cdd:NF041546  122 IKE----AREYTPGLKAAFVLNRAIARTALGREVAEALAEYG-LPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREI 196

                  ....*.
gi 1199647637 248 MALTEE 253
Cdd:NF041546  197 RALAKE 202
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
11-254 1.86e-16

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: 76.09  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyyGL------FDDNNPGIY---EVMKSEKNPKDCILK 81
Cdd:cd02036     3 IVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADI--------GLrnldliLGLENRIVYtlvDVLEGECRLEQALIK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  82 TK-IENLFLLPSKHELRNIETvlmmkTKRQeytLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVIL------PC 154
Cdd:cd02036    75 DKrWENLYLLPASQTRDKDAL-----TPEK---LEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIvtnpeiSS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 155 IPDDYALHGLLCiAKEIVEIKQFTN---PNLKIMGIlicMMeqtkSKKAYADALKTQDIfpcfeTVIRKNTTLQEAINAH 231
Cdd:cd02036   147 VRDADRVIGLLE-SKGIVNIGLIVNryrPEMVKSGD---ML----SVEDIQEILGIPLL-----GVIPEDPEVIVATNRG 213
                         250       260
                  ....*....|....*....|...
gi 1199647637 232 VPVHRYDKRSNGAKDYMALTEEI 254
Cdd:cd02036   214 EPLVLYKPNSLAAKAFENIARRL 236
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
24-257 1.71e-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: 73.39  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  24 TTAVNLSAMLADKGYKTLLVDLDFQSyAT--SYYGLfdDNNPGIYEVMKSEKNPKDCILKTKiENLFLLPSKHELRNIET 101
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGL-ANldVLLGL--EPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 102 VlmmktkRQEYTLQMALKEIEADYDFIIFDCPP--SGERIkeNALTCCDYVIL------PCIPDDYALHGLLCIAKEIve 173
Cdd:COG0455    77 L------DPEERLIRVLEELERFYDVVLVDTGAgiSDSVL--LFLAAADEVVVvttpepTSITDAYALLKLLRRRLGV-- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 174 ikqftnpnlKIMGILICMMEQTKSKKAYADALKTQ-----DIFPCFETVIRKNTTLQEAINAHVPVHRYDKRSNGAKDYM 248
Cdd:COG0455   147 ---------RRAGVVVNRVRSEAEARDVFERLEQVaerflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIR 217

                  ....*....
gi 1199647637 249 ALTEEIIKI 257
Cdd:COG0455   218 ELAARLAGW 226
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
7-151 2.61e-15

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 74.02  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   7 MSTKIAITYEKGGCGKTTTAVNLSAMLADK-GYKTLLVDLDFQSYATSYYGL-FddNNPGIYEVMKSEKNPKDciLKTKI 84
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATQFLSKtF--NVPNFPQSFMKCVEDGD--LEKGI 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199647637  85 ----ENLFLLPSKHELRNIETVLMMKTKR---QEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVI 151
Cdd:NF041283   77 vhltPNLDLIAGDYDTRELGDFLADKFKSeydRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVI 150
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
7-151 3.39e-15

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 72.78  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   7 MSTKIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyyGL--------------FDdnnpgIYEVMKSE 72
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADI--------GLrnldlvmglenrivYD-----LVDVIEGE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  73 KNPKDCILKTK-IENLFLLPS-----KHELrNIEtvlmmktkrqeytlQMA--LKEIEADYDFIIFDCPPSGERIKENAL 144
Cdd:COG2894    68 CRLKQALIKDKrFENLYLLPAsqtrdKDAL-TPE--------------QMKklVEELKEEFDYILIDSPAGIEQGFKNAI 132

                  ....*..
gi 1199647637 145 TCCDYVI 151
Cdd:COG2894   133 AGADEAI 139
PHA02518 PHA02518
ParA-like protein; Provisional
11-260 4.25e-15

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 71.80  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYyglfddnnpgiyevmkSEKNPKDCILktkienlfll 90
Cdd:PHA02518    3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW----------------AEAREEGEPL---------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 pskhelrnIETVLMMKTKRQEytlqmaLKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIAkE 170
Cdd:PHA02518   57 --------IPVVRMGKSIRAD------LPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV-E 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 171 IVEIKQFTNPNLKIMGILIcmMEQTKSKKAYADALKTQD-----IFPCFETviRKNtTLQEAINAHVPVHRYDKRSNGAk 245
Cdd:PHA02518  122 LIKARQEVTDGLPKFAFII--SRAIKNTQLYREARKALAgyglpILRNGTT--QRV-AYADAAEAGGSVLELPEDDKAA- 195
                         250
                  ....*....|....*
gi 1199647637 246 dymaltEEIIKIVKE 260
Cdd:PHA02518  196 ------EEIIQLVKE 204
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
11-262 5.45e-15

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: 72.46  E-value: 5.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPGIYEVMKSEKNPKDCILKTKiENLFLL 90
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGP-FGVKVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 PSKHELRNIetvlmMKTKRQEytLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYALHGLLCIaKE 170
Cdd:TIGR01969  82 PAGVSLEGL-----RKADPDK--LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKT-KI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 171 IVEikqftNPNLKIMGILICMMEQTK---SKKAYADALKTQDIfpcfeTVIRKNTTLQEAINAHVPVHRYDKRSNGAKDY 247
Cdd:TIGR01969 154 VAE-----KLGTAILGVVLNRVTRDKtelGREEIETILEVPVL-----GVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAF 223
                         250
                  ....*....|....*
gi 1199647637 248 MALTEEIIKIVKEGK 262
Cdd:TIGR01969 224 MELAAELAGIEYEPK 238
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
11-134 5.73e-15

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 73.94  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPGIYEVM-------KSEKNPKDCILKTK 83
Cdd:PRK13869  124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLyaairydDTRRPLRDVIRPTY 203
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1199647637  84 IENLFLLPSKHELRNIE--TVLMMKTKRQEYTL-----QMALKEIEADYDFIIFDCPP 134
Cdd:PRK13869  204 FDGLHLVPGNLELMEFEhtTPKALSDKGTRDGLfftrvAQAFDEVADDYDVVVIDCPP 261
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
11-179 5.51e-14

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: 69.67  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyyGLFDDN------NPGIY---EVMKSEKNPKDCILK 81
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADI--------GLRNLDlllgleNRIVYtlvDVVEGECRLQQALIK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  82 TK-IENLFLLPSKhELRNIETVlmmkTKRQEYTLQMALKEieaDYDFIIFDCPPSGERIKENALTCCDYVILPCIPDDYA 160
Cdd:TIGR01968  76 DKrLKNLYLLPAS-QTRDKDAV----TPEQMKKLVNELKE---EFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSA 147
                         170       180
                  ....*....|....*....|....*
gi 1199647637 161 LH------GLLcIAKEIVEIKQFTN 179
Cdd:TIGR01968 148 VRdadrviGLL-EAKGIEKIHLIVN 171
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
11-201 1.01e-13

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: 67.85  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSyyGLFDDNNP--GIYEVMKSEKNPKDCILKTKIENLF 88
Cdd:TIGR01007  20 LLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMS--GTFKSQNKitGLTNFLSGTTDLSDAICDTNIENLD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  89 LLPSKHELRNIETVLmmktkrQEYTLQMALKEIEADYDFIIFDCPPSGERIKENALT-CCDYVILpcIPDDYAlhgllcI 167
Cdd:TIGR01007  98 VITAGPVPPNPTELL------QSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIArACDASIL--VTDAGK------I 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1199647637 168 AKEIVE--IKQFTNPNLKIMGILICMMEQTKSKKAY 201
Cdd:TIGR01007 164 KKREVKkaKEQLEQAGSNFLGVVLNKVDISVSKYGY 199
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
17-255 2.41e-12

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: 65.91  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLAD-KGYKTLLVDLDFQS-YATSYYGLfdDNNPGIYEVMKSEKNPKDCILK---TKIE-NLFLL 90
Cdd:COG4963   111 KGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFgDVALYLDL--EPRRGLADALRNPDRLDETLLDralTRHSsGLSVL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  91 PSKHELRNIETVlmmkTKRQEYTLQMALKeieADYDFIIFDCPPSGERIKENALTCCDYVILPCIPDdyalhgLLCI--A 168
Cdd:COG4963   189 AAPADLERAEEV----SPEAVERLLDLLR---RHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPD------LPSLrnA 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 169 KEIVE-IKQFTNPNLKImgILICMMEQTK---SKKAYADALKTQDIFpcfetVIRKNT-TLQEAINAHVPVHRYDKRSNG 243
Cdd:COG4963   256 KRLLDlLRELGLPDDKV--RLVLNRVPKRgeiSAKDIEEALGLPVAA-----VLPNDPkAVAEAANQGRPLAEVAPKSPL 328
                         250
                  ....*....|..
gi 1199647637 244 AKDYMALTEEII 255
Cdd:COG4963   329 AKAIRKLAARLT 340
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
11-241 1.44e-10

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: 59.51  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD-----------FQSYATsyyglfddnnpgIYEVMKSEKNPKDCI 79
Cdd:cd02038     3 IAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillgLAPKKT------------LGDVLKGRVSLEDII 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  80 LKTKiENLFLLPSK---HELRNIETVLMMKtkrqeytLQMALKEIEADYDFIIFDCPP--SGERIkeNALTCCDYVIL-- 152
Cdd:cd02038    71 VEGP-EGLDIIPGGsgmEELANLDPEQKAK-------LIEELSSLESNYDYLLIDTGAgiSRNVL--DFLLAADEVIVvt 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 153 ----PCIPDDYALHGLLciakeiveIKQFTNPNLKimgILICMMEQTKSKKAYADALKTQ-----DIFPCFETVIRKNTT 223
Cdd:cd02038   141 tpepTSITDAYALIKVL--------SRRGGKKNFR---LIVNMARSPKEGRATFERLKKVakrflDINLDFVGFIPYDQS 209
                         250
                  ....*....|....*...
gi 1199647637 224 LQEAINAHVPVHRYDKRS 241
Cdd:cd02038   210 VRRAVRSQKPFVLLFPNS 227
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
16-153 6.01e-10

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: 58.23  E-value: 6.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  16 EKGGCGKTTTAVNLSAMLADKGYKTLLVDLDF-QSYATSYYGlfddnnpgiyevmksekNPKDCILKTKIEnlflLPSKh 94
Cdd:pfam09140   8 EKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFE-----------------NRSATADRTGLS----LPTP- 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199647637  95 ELRNIETVLMMKTKRQEYT----LQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILP 153
Cdd:pfam09140  66 EHLNLPDNDVAEVPDGENIddarLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTP 128
minD CHL00175
septum-site determining protein; Validated
7-179 3.80e-09

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 55.93  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   7 MSTKIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyyGLFDDN------NPGIY---EVMKSEKNPKD 77
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI--------GLRNLDlllgleNRVLYtamDVLEGECRLDQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  78 CILKTK-IENLFLLP-SKHELR-NIetvlmmkTKRQEYTLQMALKEIeaDYDFIIFDCPPSGERIKENALTCCDYVILPC 154
Cdd:CHL00175   86 ALIRDKrWKNLSLLAiSKNRQRyNV-------TRKNMNMLVDSLKNR--GYDYILIDCPAGIDVGFINAIAPAQEAIVVT 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1199647637 155 IPDDYALH------GLLcIAKEIVEIKQFTN 179
Cdd:CHL00175  157 TPEITAIRdadrvaGLL-EANGIYNVKLLVN 186
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
10-187 1.11e-08

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: 54.04  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  10 KIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyYGlfddnnPGI--------YEVMKSEKNpkdcILK 81
Cdd:cd02037     2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADI-------YG------PSIprllgvegKPLHQSEEG----IVP 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  82 TKIENL------FLLPSKhelrniETVLM---MKTKrqeyTLQMALKEIE-ADYDFIIFDCPP--SGERIKENALTCCDY 149
Cdd:cd02037    65 VEVGGIkvmsigFLLPED------DAVIWrgpMKSG----AIKQFLKDVDwGELDYLIIDLPPgtGDEHLSLVQLIPIDG 134
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1199647637 150 VILPCIPDDYAlhgLLCIAKEIVEIKQFtnpNLKIMGI 187
Cdd:cd02037   135 AVVVTTPQEVS---LIDVRKAIDMCKKL---NIPVLGI 166
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
11-250 1.53e-08

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: 53.89  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPGIYEVMKSEKNPKDCILKTKIENLFL- 89
Cdd:TIGR03371   4 IAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALLNGADWAAAAYRSPDGVLFLp 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  90 ---LPSKHELRNIETvlmmktkrQEYTLQMALKEIEAD-YDFIIFDCPPSGERIKENALTCCDYV--ILPCIPDDYALhg 163
Cdd:TIGR03371  84 ygdLSADEREAYQAH--------DAGWLARLLQQLDLAaRDWVLIDLPRGPSPITRQALAAADLVlvVVNADAACYAT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637 164 llcIAKEIVEIKQFTNPNLKImGILICMMEQ--TKSKKAYADALKTQDIfPCFETVIRKNTTLQEAINAHVPVHRYDKRS 241
Cdd:TIGR03371 154 ---LHQLALALFAGSGPRDGP-RFLINQFDParQLSRDVRAVLRQTLGS-RLLPFVIHRDEAVSEALARGTPVLNYAPHS 228

                  ....*....
gi 1199647637 242 NGAKDYMAL 250
Cdd:TIGR03371 229 QAAHDIRTL 237
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
11-153 2.69e-08

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 53.83  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVD-LDFQSYATSYYGLFDD-----NNPGIYEVMKSEKNPKDCILKTKI 84
Cdd:PRK13705  109 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDlhihaEDTLLPFYLGEKDDATYAIKPTCW 188
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199647637  85 ENLFLLPSKHELRNIETVLMMKTKRQE------YTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILP 153
Cdd:PRK13705  189 PGLDIIPSCLALHRIETELMGKFDEGKlptdphLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVP 263
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
10-134 3.46e-08

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: 52.84  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  10 KIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyYGlfddnnPGIYEVMKSEKNP----KDCILKTKIE 85
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADI-------YG------PSIPRMLGLEGERpeqsDGGIIPVEAH 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1199647637  86 NL------FLLPSKHelrniETVLM---MKTKrqeyTLQMALKEIE-ADYDFIIFDCPP 134
Cdd:pfam10609  72 GIkvmsigFLLPDED-----DAVIWrgpMKSG----AIKQFLTDVDwGELDYLIIDLPP 121
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
10-46 2.12e-07

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: 48.20  E-value: 2.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1199647637  10 KIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:cd01983     2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
17-137 2.93e-07

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: 50.20  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLADKGYKTLLV--D----LDFqsyatsyygLFDdnnpgiyevMKSEKNPkdcilKTKI-ENLFL 89
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVstDpahsLSD---------AFG---------QKLGGET-----PVKGaPNLWA 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199647637  90 L---PsKHEL-RNIETVLmmKTKRQEYTLQ-------------------MALKEI-----EADYDFIIFDCPPSGE 137
Cdd:cd02035    65 MeidP-EEALeEYWEEVK--ELLAQYLRLPgldevyaeellslpgmdeaAAFDELreyveSGEYDVIVFDTAPTGH 137
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
11-134 8.42e-07

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: 49.72  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQS-YATSYYGlfDDNNPGIYE----------VMKSEKNPKDCI 79
Cdd:TIGR01005 556 IAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKgGLHQMFG--KAPKPGLLDllageasieaGIHRDQRPGLAF 633
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1199647637  80 LKTKIENLFLLPSKHELRNIETVLMMKTKRQEytlqmalkeieadYDFIIFDCPP 134
Cdd:TIGR01005 634 IAAGGASHFPHNPNELLANPAMAELIDNARNA-------------FDLVLVDLAA 675
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
11-153 1.06e-06

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 49.24  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVD-LDFQSYATSYYGLFDDNNpgIYE-------VMKSEKNPKDCILKT 82
Cdd:PHA02519  109 LAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLH--IHAddtllpfYLGERDNAEYAIKPT 186
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199647637  83 KIENLFLLPSKHELRNIETVLMMKTKRQE------YTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILP 153
Cdd:PHA02519  187 CWPGLDIIPSCLALHRIETDLMQYHDAGKlphpphLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVA 263
PRK10818 PRK10818
septum site-determining protein MinD;
7-157 1.33e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 48.40  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   7 MSTKIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyatsyyGLFD-DNNPG-----IYE---VMKSEKNPKD 77
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDI--------GLRNlDLIMGcerrvVYDfvnVIQGDATLNQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  78 CILKTK-IENLFLLPSKhELRNIETVlmmktkRQEYTLQMALKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIP 156
Cdd:PRK10818   73 ALIKDKrTENLYILPAS-QTRDKDAL------TREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNP 145

                  .
gi 1199647637 157 D 157
Cdd:PRK10818  146 E 146
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
10-43 1.45e-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: 48.28  E-value: 1.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1199647637  10 KIAItYEKGGCGKTTTAVNLSAMLADKGYKTLLV 43
Cdd:cd02040     2 QIAI-YGKGGIGKSTTASNLSAALAEMGKKVLHV 34
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
17-137 1.85e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 47.89  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLADKGYKTLLVDLDFqsyATSYYGLFD-DNNPGIYEVmkseknpkdcilktKIENLF------- 88
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDP---AHSLGDVLGtELGNEPTEV--------------AVPNLYaleidpe 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199647637  89 ----------------LLPSKhELRNIETVL--MmktkrQEYTLQMALKEI--EADYDFIIFDCPPSGE 137
Cdd:COG0003    74 aeleeywervraplrgLLPSA-GVDELAESLpgT-----EELAALDELLELleEGEYDVIVVDTAPTGH 136
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
10-46 2.83e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.08  E-value: 2.83e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1199647637  10 KIAITyEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:COG3640     2 KIAVA-GKGGVGKTTLSALLARYLAEKGKPVLAVDAD 37
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
11-157 7.16e-06

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: 45.73  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLS-AMLADKGYKTLLVDLDFQSYATSYYglFDDNNP-GIYEVMKSEKNPKDCILKTKIEN-- 86
Cdd:cd03111     3 VAVVGAKGGVGASTLAVNLAqELAQRAKDKVLLIDLDLPFGDLGLY--LNLRPDyDLADVIQNLDRLDRTLLDSAVTRhs 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199647637  87 --LFLLPSKHELRNIEtvlmmkTKRQEYTLQMaLKEIEADYDFIIFDCPPSGERIKENALTCCDYVILPCIPD 157
Cdd:cd03111    81 sgLSLLPAPQELEDLE------ALGAEQVDKL-LQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQD 146
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
6-134 1.73e-05

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 45.53  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   6 MMSTK---IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDF-QSYATSYYGLfdDNNPGIYEVMKSEKNPKDCILK 81
Cdd:PRK11519  521 MMQAQnnvLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMrKGYTHELLGT--NNVNGLSDILIGQGDITTAAKP 598
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1199647637  82 TKIENLFLLPSKHELRNiETVLMMKTKRQEYtlqmaLKEIEADYDFIIFDCPP 134
Cdd:PRK11519  599 TSIANFDLIPRGQVPPN-PSELLMSERFAEL-----VNWASKNYDLVLIDTPP 645
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
17-140 1.74e-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: 45.46  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNP----GIYEVMKSEKNPKDC--ILKTKIENLF-- 88
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKItaiaGVPGLFALEIDPQAAaqAYRARIVDPVrg 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1199647637  89 LLPSKhELRNIETVLMMKTKRQ-----EYTLQMALKEIEADYDFIIFDCPPSGERIK 140
Cdd:TIGR04291  91 VLPDD-VVSSIEEQLSGACTTEiaafdEFTGLLTDAELTQDFDHIIFDTAPTGHTIR 146
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
10-77 1.94e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 44.74  E-value: 1.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199647637  10 KIAItYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYgLFDDNNPGIYEVMKSEKNPKD 77
Cdd:pfam00142   2 QIAI-YGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLL-LGGKLQPTVLDTAREKGYVED 67
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
9-73 3.37e-05

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: 44.44  E-value: 3.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199647637   9 TKIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYygLFDDNN-PGIYEVMKSEK 73
Cdd:cd02033    31 TQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSL--LFGGKAcPTIIETSTRKK 94
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
11-46 3.93e-05

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: 43.89  E-value: 3.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1199647637  11 IAItYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:cd02117     3 IVV-YGKGGIGKSTTASNLSAALAEGGKKVLHVGCD 37
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
7-41 1.27e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.26  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1199647637   7 MSTKIAItYEKGGCGKTTTAVNLSAMLADKGYKTL 41
Cdd:PRK13185    1 MALVLAV-YGKGGIGKSTTSSNLSAAFAKLGKKVL 34
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
11-46 2.39e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 41.95  E-value: 2.39e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:PRK11670  110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
10-46 3.40e-04

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: 41.13  E-value: 3.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1199647637  10 KIAItYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:cd02032     2 VIAV-YGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCD 37
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
17-140 4.43e-04

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 40.80  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLADKGYKTLLVDLDfqsYATSYYGLFDdnnpgiyevMKSEKNPkdcilkTKI-ENLFLL---PS 92
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTD---PAHSLSDSFN---------QKFGHEP------TKVkENLSAMeidPN 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199647637  93 ------KHELRNIETVLMMkTKRQEYTLQMAL------KEI-----------EADYDFIIFDCPPSGERIK 140
Cdd:pfam02374  71 meleeyWQEVQKYMNALLG-LRMLEGILAEELaslpgiDEAasfdefkkymdEGEYDVVVFDTAPTGHTLR 140
PRK09841 PRK09841
tyrosine-protein kinase;
6-134 5.73e-04

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 41.05  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637   6 MMSTK---IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDF-QSYAtsyYGLFD-DNNPGIYEVMKSEKNPKDCIL 80
Cdd:PRK09841  526 MMETEnniLMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLrRGYS---HNLFTvSNEHGLSEYLAGKDELNKVIQ 602
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1199647637  81 KTKIENLFLLPSKHELRNIETVLMMKTKRQeytlqmALKEIEADYDFIIFDCPP 134
Cdd:PRK09841  603 HFGKGGFDVITRGQVPPNPSELLMRDRMRQ------LLEWANDHYDLVIVDTPP 650
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
10-46 6.14e-04

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


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 40.37  E-value: 6.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1199647637  10 KIAITyEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:cd02034     2 KIAVA-GKGGVGKTTIAALLIRYLAKKGGKVLAVDAD 37
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
10-46 1.09e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.07  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1199647637  10 KIAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
10-46 3.45e-03

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: 37.75  E-value: 3.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1199647637  10 KIAITYEKGGCGKTTTAVNLSAMLadkgYKTLLVDLD 46
Cdd:cd03110     1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCD 33
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
11-133 5.34e-03

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


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 37.13  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199647637  11 IAITYEKGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYGLFDDNNPG-IYEVMKSEKN----PKDCILKTKIE 85
Cdd:cd17869     6 ITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLMSdHLYTLKSRKAnladKLESCVKQHES 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1199647637  86 NLFLLPSkhelrnIETVLMMKTKRQEYTLQMALKEIEAD-YDFIIFDCP 133
Cdd:cd17869    86 GVYYFSP------FKSALDILEIKKDDILHMITKLVEAHaYDYIIMDLS 128
SRP54_G cd17875
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ...
19-46 6.84e-03

GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349784  Cd Length: 193  Bit Score: 36.79  E-value: 6.84e-03
                          10        20
                  ....*....|....*....|....*...
gi 1199647637  19 GCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:cd17875    10 GSGKTTTAAKLAYYYQKKGYKVGLVCAD 37
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
17-56 7.81e-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: 37.55  E-value: 7.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1199647637  17 KGGCGKTTTAVNLSAMLADKGYKTLLVDLDFQSYATSYYG 56
Cdd:NF041417  341 KGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFG 380
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
19-46 9.35e-03

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 36.37  E-value: 9.35e-03
                          10        20
                  ....*....|....*....|....*...
gi 1199647637  19 GCGKTTTAVNLSAMLADKGYKTLLVDLD 46
Cdd:pfam00448  10 GSGKTTTIAKLAAYLKKKGKKVLLVAAD 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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