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Conserved domains on  [gi|765459861|ref|WP_044715110|]
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MULTISPECIES: ParA family partition ATPase [Enterobacterales]

Protein Classification

ParA family protein( domain architecture ID 10114212)

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, and to BcsQ, an essential component of the cellulose biosynthesis apparatus

CATH:  3.40.50.300
Gene Ontology:  GO:0005524
PubMed:  28373206|22672910|17161598|2149583
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA_partition super family cl49513
ParA family partition ATPase;
3-200 3.73e-58

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 181.60  E-value: 3.73e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   3 IIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNKA--EKAAFDVYTAASE---KDVYQVRKDlaeYD 77
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAreDERPFPVVGLARPtlhRELPSLARD---YD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  78 FVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVT-VLEAQAYNRPVEARFLITRKIEQATMLNVLKDSIAQ 156
Cdd:NF041546  78 FVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDlIKEAREYTPGLKAAFVLNRAIARTALGREVAEALAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 765459861 157 TGIKPFKTAITQRQSYVKSVMEGESVFDTN-DGAAKGEIAILTRE 200
Cdd:NF041546 158 YGLPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
3-200 3.73e-58

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 181.60  E-value: 3.73e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   3 IIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNKA--EKAAFDVYTAASE---KDVYQVRKDlaeYD 77
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAreDERPFPVVGLARPtlhRELPSLARD---YD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  78 FVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVT-VLEAQAYNRPVEARFLITRKIEQATMLNVLKDSIAQ 156
Cdd:NF041546  78 FVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDlIKEAREYTPGLKAAFVLNRAIARTALGREVAEALAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 765459861 157 TGIKPFKTAITQRQSYVKSVMEGESVFDTN-DGAAKGEIAILTRE 200
Cdd:NF041546 158 YGLPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-155 8.79e-37

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: 124.96  E-value: 8.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNkaekaafdvytaasekdvyqvrkdlaeYDFVII 81
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------YDYILI 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765459861  82 DGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLEA---QAYNRPVEARFLITRKIEQATMLNVLKDSIA 155
Cdd:cd02042   54 DTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEElkkQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-206 4.34e-36

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: 126.90  E-value: 4.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNW---NKAEK------------------------- 52
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGlglDPDDLdptlydlllddapledaivpteipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  53 ----------AAFDVYTAASEKDVYQVRKDLAE----YDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSV 118
Cdd:COG1192   81 ldlipanidlAGAEIELVSRPGRELRLKRALAPladdYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861 119 VTVLEA--QAYNRPVE-ARFLIT----RKIEQATMLNVLKDSIaqtGIKPFKTAITQRQSYVKSVMEGESVFDTnDGAAK 191
Cdd:COG1192  161 LETIEEvrEDLNPKLEiLGILLTmvdpRTRLSREVLEELREEF---GDKVLDTVIPRSVALAEAPSAGKPVFEY-DPKSK 236

                        250
                 ....*....|....*..
gi 765459861 192 GEIAI--LTREILESFE 206
Cdd:COG1192  237 GAKAYraLAEELLERLE 253
PHA02518 PHA02518
ParA-like protein; Provisional
 2-203 4.60e-35

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 123.04  E-value: 4.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWnkAEKAAFDVYTAASEKDVYQVRKDLAE----YD 77
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW--AEAREEGEPLIPVVRMGKSIRADLPKvasgYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  78 FVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLEA-QAY-NRPVEARFLITRKIEQATMLNVLKDSIA 155
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKArQEVtDGLPKFAFIISRAIKNTQLYREARKALA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 765459861 156 QTGIKPFKTAITQRQSYVKSVMEGESVFD-TNDGAAKGEIAILTREILE 203
Cdd:PHA02518 159 GYGLPILRNGTTQRVAYADAAEAGGSVLElPEDDKAAEEIIQLVKELFR 207
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-110 5.89e-22

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: 88.02  E-value: 5.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLT-----NWNKAEKAAFDVY------------TAASE 63
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATsglgiDKNNVEKTIYELLigecnieeaiikTVIEN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765459861   64 KDVYQVRKDLA-------------------------EYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPL 110
Cdd:pfam13614  81 LDLIPSNIDLAgaeieligienrenilkealepvkdNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYY 152
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-139 2.92e-09

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: 55.04  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQ--------MSLTN---WNKAE------KAAFDVYT---- 59
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQnllrlhfgMDWSVrdgWARALlngadwAAAAYRSPdgvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   60 -------AASEKDVYQV-----------RKDLAEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTV 121
Cdd:TIGR03371  81 flpygdlSADEREAYQAhdagwlarllqQLDLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLALA 160

                         170
                  ....*....|....*...
gi 765459861  122 LEAQAYNrPVEARFLITR 139
Cdd:TIGR03371 161 LFAGSGP-RDGPRFLINQ 177
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
3-200 3.73e-58

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 181.60  E-value: 3.73e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   3 IIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNKA--EKAAFDVYTAASE---KDVYQVRKDlaeYD 77
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAreDERPFPVVGLARPtlhRELPSLARD---YD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  78 FVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVT-VLEAQAYNRPVEARFLITRKIEQATMLNVLKDSIAQ 156
Cdd:NF041546  78 FVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDlIKEAREYTPGLKAAFVLNRAIARTALGREVAEALAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 765459861 157 TGIKPFKTAITQRQSYVKSVMEGESVFDTN-DGAAKGEIAILTRE 200
Cdd:NF041546 158 YGLPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-155 8.79e-37

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: 124.96  E-value: 8.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNkaekaafdvytaasekdvyqvrkdlaeYDFVII 81
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------YDYILI 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765459861  82 DGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLEA---QAYNRPVEARFLITRKIEQATMLNVLKDSIA 155
Cdd:cd02042   54 DTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEElkkQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-206 4.34e-36

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: 126.90  E-value: 4.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNW---NKAEK------------------------- 52
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGlglDPDDLdptlydlllddapledaivpteipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  53 ----------AAFDVYTAASEKDVYQVRKDLAE----YDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSV 118
Cdd:COG1192   81 ldlipanidlAGAEIELVSRPGRELRLKRALAPladdYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861 119 VTVLEA--QAYNRPVE-ARFLIT----RKIEQATMLNVLKDSIaqtGIKPFKTAITQRQSYVKSVMEGESVFDTnDGAAK 191
Cdd:COG1192  161 LETIEEvrEDLNPKLEiLGILLTmvdpRTRLSREVLEELREEF---GDKVLDTVIPRSVALAEAPSAGKPVFEY-DPKSK 236

                        250
                 ....*....|....*..
gi 765459861 192 GEIAI--LTREILESFE 206
Cdd:COG1192  237 GAKAYraLAEELLERLE 253
PHA02518 PHA02518
ParA-like protein; Provisional
 2-203 4.60e-35

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 123.04  E-value: 4.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWnkAEKAAFDVYTAASEKDVYQVRKDLAE----YD 77
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW--AEAREEGEPLIPVVRMGKSIRADLPKvasgYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  78 FVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLEA-QAY-NRPVEARFLITRKIEQATMLNVLKDSIA 155
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKArQEVtDGLPKFAFIISRAIKNTQLYREARKALA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 765459861 156 QTGIKPFKTAITQRQSYVKSVMEGESVFD-TNDGAAKGEIAILTREILE 203
Cdd:PHA02518 159 GYGLPILRNGTTQRVAYADAAEAGGSVLElPEDDKAAEEIIQLVKELFR 207
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-110 5.89e-22

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: 88.02  E-value: 5.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLT-----NWNKAEKAAFDVY------------TAASE 63
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATsglgiDKNNVEKTIYELLigecnieeaiikTVIEN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765459861   64 KDVYQVRKDLA-------------------------EYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPL 110
Cdd:pfam13614  81 LDLIPSNIDLAgaeieligienrenilkealepvkdNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYY 152
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-182 6.31e-22

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: 89.33  E-value: 6.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    4 IAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTN------------------------------WNKAEKA 53
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSveglegdiapalqalaeglkgrvnldpillKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   54 AFDVYTAA-----SEKDVYQVRKDLA----------EYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAA--- 115
Cdd:pfam01656  81 GLDLIPGNidlekFEKELLGPRKEERlrealealkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAkrl 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765459861  116 -GSVVTVLEAQAYNRPVEARFLITRkIEQATMLNVLKDSIAQTGIK-PFKTAITQRQSYVKSVMEGESV 182
Cdd:pfam01656 161 gGVIAALVGGYALLGLKIIGVVLNK-VDGDNHGKLLKEALEELLRGlPVLGVIPRDEAVAEAPARGLPV 228
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
1-139 4.15e-15

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 71.03  E-value: 4.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNW--NKAEKAAFD----VYTA---ASEKDVYQvRK 71
Cdd:PRK13849   1 MKLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWkeNALRSNTWDpaceVYAAdelPLLEAAYE-DA 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765459861  72 DLAEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGS----VVTVLeaQAYNRPVEARFLITR 139
Cdd:PRK13849  80 ELQGFDYALADTHGGSSELNNTIIASSNLLLIPTMLTPLDIDEALStyryVIELL--LSENLAIPTAILRQR 149
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 1-115 3.88e-14

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 68.37  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNW--NKAEKAAFD----VYTA---ASEKDVYQvRK 71
Cdd:pfam07015   1 MQLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWreNALRKGTWDpaceIFNAdelPLLEQAYE-HA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 765459861   72 DLAEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAA 115
Cdd:pfam07015  80 EGSGFDYALADTHGGSSELNNTIIASSDLLLIPTMLTPLDIDEA 123
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-118 1.87e-11

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: 61.32  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    3 IIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDP-QMSLTNW--NKAEKAA----------FDVYTAASEKDVYQ- 68
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYfeNRSATADrtglslptpeHLNLPDNDVAEVPDg 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 765459861   69 -----------VRKDLAEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSV 118
Cdd:pfam09140  82 eniddarleeaFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLLGQV 142
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-139 2.92e-09

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: 55.04  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQ--------MSLTN---WNKAE------KAAFDVYT---- 59
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQnllrlhfgMDWSVrdgWARALlngadwAAAAYRSPdgvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   60 -------AASEKDVYQV-----------RKDLAEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTV 121
Cdd:TIGR03371  81 flpygdlSADEREAYQAhdagwlarllqQLDLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLALA 160

                         170
                  ....*....|....*...
gi 765459861  122 LEAQAYNrPVEARFLITR 139
Cdd:TIGR03371 161 LFAGSGP-RDGPRFLINQ 177
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-129 5.08e-09

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: 54.74  E-value: 5.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLA-SSGKKIAVVDTDPQM----SLTNWNKAEKAA---------------------- 54
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFgdvaLYLDLEPRRGLAdalrnpdrldetlldraltrhs 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  55 --FDVYTAA---------SEKDVYQVRKDL-AEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVL 122
Cdd:COG4963  183 sgLSVLAAPadleraeevSPEAVERLLDLLrRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLL 262


                 ....*..
gi 765459861 123 EAQAYNR 129
Cdd:COG4963  263 RELGLPD 269
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-126 5.17e-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: 52.05  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDpqmsltnwnkaekaafdvytaasekdvyqvrkdlaeyDFVII 81
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD-------------------------------------DYVLI 43

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 765459861  82 DGAGSLSVITSA-------AVMVSDLIIIPVTPSPLDFSAAGSVVTVLEAQA 126
Cdd:cd01983   44 DGGGGLETGLLLgtivallALKKADEVIVVVDPELGSLLEAVKLLLALLLLG 95
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 1-139 1.39e-08

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: 53.83  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNKAEkAAFDV------YTA-------ASEKDVY 67
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQ-PEFDVgenetlYGAirydderRPISEII 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   68 Q----------------------------------------VRKDLAE----YDFVIIDGAGSLSVITSAAVMVSDLIII 103
Cdd:TIGR03453 183 RktyfpgldlvpgnlelmefehetpralsrgqggdtiffarVGEALAEveddYDVVVIDCPPQLGFLTLSALCAATGVLI 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 765459861  104 PVTPSPLDFSA-------AGSVVTVLEAQAYNRPVE-ARFLITR 139
Cdd:TIGR03453 263 TVHPQMLDVMSmsqfllmTGDLLGVVREAGGNLSYDfMRYLVTR 306
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-160 1.91e-08

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: 52.59  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDpqMSLTN------------------------WNKA---EKAA 54
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--IGLRNldlilglenrivytlvdvlegecrLEQAlikDKRW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  55 FDVY----------TAASEKDVYQVRKDL-AEYDFVIID-----GAGSLSVITSAavmvsDLIIIPVTPSPLDFSAAGSV 118
Cdd:cd02036   79 ENLYllpasqtrdkDALTPEKLEELVKELkDSFDFILIDspagiESGFINAIAPA-----DEAIIVTNPEISSVRDADRV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 765459861 119 VTVLEAQAynrPVEARFLITR----KIEQATMLNVlKDSIAQTGIK 160
Cdd:cd02036  154 IGLLESKG---IVNIGLIVNRyrpeMVKSGDMLSV-EDIQEILGIP 195
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 17-139 7.13e-08

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: 51.04  E-value: 7.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  17 TATINVSSCLASSGKKIAVVDTDPQMS-----------------LTNWNKAEKAA------FDVYTAAS----------E 63
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLAnldvllglepkatladvLAGEADLEDAIvqgpggLDVLPGGSgpaelaeldpE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765459861  64 KDVYQVRKDLAE-YDFVIID-GAGsLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLEAQAYNRPveARFLITR 139
Cdd:COG0455   81 ERLIRVLEELERfYDVVLVDtGAG-ISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRR--AGVVVNR 155
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-109 1.67e-07

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: 49.88  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTD-------------PQMSLTNWNKAEKAAFDV----------- 57
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSLEDIivegpegldii 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 765459861  58 -----------YTAASEKDVYQ-VRKDLAEYDFVIID-GAGSLSVITSAAVMVSDLIIIpVTPSP 109
Cdd:cd02038   81 pggsgmeelanLDPEQKAKLIEeLSSLESNYDYLLIDtGAGISRNVLDFLLAADEVIVV-TTPEP 144
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 1-45 4.56e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 49.29  E-value: 4.56e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 765459861   1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLT 45
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLS 165
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-39 1.08e-06

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 47.74  E-value: 1.08e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTD 39
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-182 3.29e-06

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: 46.18  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDpqMSLTNW-------NKAEKAAFDVY---------------- 58
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD--IGLRNLdlllgleNRIVYTLVDVVegecrlqqalikdkrl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   59 --------------TAASEKDVYQVRKDL-AEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLE 123
Cdd:TIGR01968  80 knlyllpasqtrdkDAVTPEQMKKLVNELkEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765459861  124 AQAYNRPveaRFLITR----KIEQATMLNVlkDSIAQTGIKPFKTAITQRQSYVKSVMEGESV 182
Cdd:TIGR01968 160 AKGIEKI---HLIVNRlrpeMVKKGDMLSV--DDVLEILSIPLIGVIPEDEAIIVSTNKGEPV 217
PRK10818 PRK10818
septum site-determining protein MinD;
2-191 5.25e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 45.70  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDpqMSLTN------------------------WNKA---EKAA 54
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD--IGLRNldlimgcerrvvydfvnviqgdatLNQAlikDKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  55 FDVYT----------AASEKDVYQVRKDLAE--YDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVL 122
Cdd:PRK10818  81 ENLYIlpasqtrdkdALTREGVAKVLDDLKAmdFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765459861 123 -----EAQAYNRPVEARFLITR----KIEQATMLNvLKDSIAQTGIkPFKTAITQRQSYVKSVMEGESV-FDTNDGAAK 191
Cdd:PRK10818 161 asksrRAENGEEPIKEHLLLTRynpgRVSRGDMLS-MEDVLEILRI-KLVGVIPEDQSVLRASNQGEPViLDIEADAGK 237
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 10-44 6.80e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 45.16  E-value: 6.80e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 765459861  10 KGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSL 44
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANL 42
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 2-45 1.64e-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: 44.28  E-value: 1.64e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 765459861   2 KIIAFLNpKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLT 45
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDST 43
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-107 1.89e-05

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: 43.95  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMS------------------LTNWNKAEKA----AFDVYT 59
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMAnlelilgmedkpvtlhdvLAGEADIKDAiyegPFGVKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   60 AASEKDVYQVRKDLAE------------YDFVIIDGAGSLSVITSAAVMVSDLIIIPVTP 107
Cdd:TIGR01969  81 IPAGVSLEGLRKADPDkledvlkeiiddTDFLLIDAPAGLERDAVTALAAADELLLVVNP 140
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-123 3.47e-05

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: 43.25  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   3 IIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTD-------------PQMSLTNWNKAEKAAFDVYTAASEKDVY-- 67
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgpslhrmlgleNRPGLSDVLAGEASLEDVIQPTEVEGLDvl 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765459861  68 -------------------QVRKDLAE-YDFVIIDGA-GSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVLE 123
Cdd:COG0489  174 pagplppnpsellaskrlkQLLEELRGrYDYVIIDTPpGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLE 250
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
2-65 9.22e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 42.05  E-value: 9.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 765459861    2 KIIAFLNpKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLTNWNKAEKAAFDVYTAASEKD 65
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKG 63
minD CHL00175
septum-site determining protein; Validated
 2-180 9.60e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 42.06  E-value: 9.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDpqMSLTNW-------NKAEKAAFDVY---------------- 58
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD--IGLRNLdlllgleNRVLYTAMDVLegecrldqalirdkrw 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  59 ------TAASEKDVYQV-RKDL---------AEYDFVIIDGAGSLSVITSAAVMVSDLIIIPVTPSPLDFSAAGSVVTVL 122
Cdd:CHL00175  94 knlsllAISKNRQRYNVtRKNMnmlvdslknRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADRVAGLL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765459861 123 EAqayNRPVEARFLITR----KIEQATMLNVlKDSIAQTGIkPFKTAITQRQSYVKSVMEGE 180
Cdd:CHL00175 174 EA---NGIYNVKLLVNRvrpdMIQANDMMSV-RDVQEMLGI-PLLGAIPEDENVIISTNRGE 230
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 1-45 1.85e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 41.29  E-value: 1.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 765459861   1 MKIIAFLNpKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSLT 45
Cdd:PRK13230   1 MRKFCFYG-KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCT 44
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-39 3.11e-04

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: 40.51  E-value: 3.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 765459861    2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTD 39
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-42 5.13e-04

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: 39.41  E-value: 5.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 765459861   2 KIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTD------PQM 42
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADiygpsiPRL 47
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 1-44 5.30e-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: 40.03  E-value: 5.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 765459861    1 MKIIaFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSL 44
Cdd:pfam02374   1 MRWI-FFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSL 43
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 2-44 6.84e-04

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: 39.41  E-value: 6.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 765459861   2 KIIAFLNpKGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSL 44
Cdd:cd02035    1 RIIFFGG-KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSL 42
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-96 7.14e-04

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: 39.09  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   1 MKIIAFLNPKGGSGKTTATINVSSCLASSGKKIAVVDTD-------------PQMSLTNW--NKAE---------KAAFD 56
Cdd:cd05387   19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlrrpslhrllglpNEPGLSEVlsGQASledviqstnIPNLD 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 765459861  57 VYTA-----------ASE--KDVYQVRKdlAEYDFVIIDGAGSLSVITSAAVM 96
Cdd:cd05387   99 VLPAgtvppnpsellSSPrfAELLEELK--EQYDYVIIDTPPVLAVADALILA 149
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 4-40 7.52e-04

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: 39.42  E-value: 7.52e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 765459861   4 IAFLNpKGGSGKTTATINVSSCLASSGKKIAVVDTDP 40
Cdd:cd02040    3 IAIYG-KGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
PRK14494 PRK14494
putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing ...
 1-90 9.10e-04

putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing protein protein; Provisional


Pssm-ID: 237731 [Multi-domain]  Cd Length: 229  Bit Score: 38.81  E-value: 9.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861   1 MKIIAFLNPKGgSGKTTATINVSSCLASSGKKIAVV----------DTDpqmsltNWNKAEKAAFDVYTAASEKDV-YQV 69
Cdd:PRK14494   1 MRAIGVIGFKD-SGKTTLIEKILKNLKERGYRVATAkhthhefdkpDTD------TYRFKKAGAEVVVVSTDETAAfLYD 73

                         90       100
                 ....*....|....*....|....*..
gi 765459861  70 RKDLAE------YDFVIIDGAGSLSVI 90
Cdd:PRK14494  74 RMDLNEilslldADFLLIEGFKELLNI 100
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 6-46 2.01e-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: 38.53  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 765459861    6 FLNPKGGSGKTTATINVSSCLASSGKKIAVVDTDP--------QMSLTN 46
Cdd:TIGR04291   7 FFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPasnvgqvfGQTIGN 55
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 12-85 2.89e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 37.88  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861  12 GSGKTTATINVSSCLASSGKKIAVVDTD---P-------QMsltnwnkAEKAAFDVYTAASEKD-VYQVRKDLAE---YD 77
Cdd:PRK00771 105 GSGKTTTAAKLARYFKKKGLKVGLVAADtyrPaaydqlkQL-------AEKIGVPFYGDPDNKDaVEIAKEGLEKfkkAD 177


                 ....*...
gi 765459861  78 FVIIDGAG 85
Cdd:PRK00771 178 VIIVDTAG 185
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 10-44 4.28e-03

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: 36.91  E-value: 4.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 765459861  10 KGGSGKTTATINVSSCLASSGKKIAVVDTDPQMSL 44
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNL 42
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 2-85 5.18e-03

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 36.93  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    2 KIIAFLNPkGGSGKTTATINVSSCLASS--GKKIAVVDTDP-----QMSLTNWnkAEKAAFDVYTAASEKDVYQVRKDLA 74
Cdd:TIGR03499 195 GVIALVGP-TGVGKTTTLAKLAARFALEhgKKKVALITTDTyrigaVEQLKTY--AEILGIPVKVARDPKELREALDRLR 271

                          90
                  ....*....|.
gi 765459861   75 EYDFVIIDGAG 85
Cdd:TIGR03499 272 DKDLILIDTAG 282
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 2-87 7.55e-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: 35.98  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765459861    2 KIIAFLNPKGgSGKTTATINVSSCLASSGKKIAVVDTD-------PQMSLtnWnkAEKAAFDVYTAASEKDVYQVRKDLA 74
Cdd:pfam00448   1 NVILLVGLQG-SGKTTTIAKLAAYLKKKGKKVLLVAADtfraaaiEQLKQ--L--AEKLGVPVFGSKTGADPAAVAFDAV 75

                          90
                  ....*....|....*....
gi 765459861   75 E------YDFVIIDGAGSL 87
Cdd:pfam00448  76 EkakaenYDVVLVDTAGRL 94
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-44 7.83e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 36.34  E-value: 7.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 765459861   1 MKIIAFLNpKGGSGKTTatinvSSC-----LASSGKKIAVVDTDPQMSL 44
Cdd:COG0003    3 TRIIFFTG-KGGVGKTT-----VAAatalaLAERGKRTLLVSTDPAHSL 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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