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Conserved domains on  [gi|1182607390|pdb|5U1G|C]
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Chain C, ParA

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 1.74e-56

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 177.74  E-value: 1.74e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         3 VISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGKAA--FDVFTAASEkdvyGIRKDL----ADY 76
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDErpFPVVGLARP----TLHRELpslaRDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        77 DFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVT-VLEAQAYSRKVEARFLITRKIEMATMLNVLKESIK 155
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDlIKEAREYTPGLKAAFVLNRAIARTALGREVAEALA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
5U1G_C       156 DTGVKAFRTAITQRQVYVKSILDGDSVFE-SSDGAAKGEIEILTKE 200
Cdd:NF041546 157 EYGLPVLKTRIGQRVAFAESAAEGLTVFEaEPDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
3-200 1.74e-56

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 177.74  E-value: 1.74e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         3 VISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGKAA--FDVFTAASEkdvyGIRKDL----ADY 76
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDErpFPVVGLARP----TLHRELpslaRDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        77 DFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVT-VLEAQAYSRKVEARFLITRKIEMATMLNVLKESIK 155
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDlIKEAREYTPGLKAAFVLNRAIARTALGREVAEALA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
5U1G_C       156 DTGVKAFRTAITQRQVYVKSILDGDSVFE-SSDGAAKGEIEILTKE 200
Cdd:NF041546 157 EYGLPVLKTRIGQRVAFAESAAEGLTVFEaEPDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-155 5.82e-35

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: 120.34  E-value: 5.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSkagkaafdvftaasekdvygirkdladYDFAIV 81
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------YDYILI 53

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5U1G_C       82 DGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTVLEA---QAYSRKVEARFLITRKIEMATMLNVLKESIK 155
Cdd:cd02042  54 DTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEElkkQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PHA02518 PHA02518
ParA-like protein; Provisional
 2-203 3.50e-32

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 115.72  E-value: 3.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGKAAFDVFTAASekdvYG--IRKDL----AD 75
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVR----MGksIRADLpkvaSG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        76 YDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTVLEA-QAYS-RKVEARFLITRKIEMATMLNVLKES 153
Cdd:PHA02518  77 YDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKArQEVTdGLPKFAFIISRAIKNTQLYREARKA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
5U1G_C       154 IKDTGVKAFRTAITQRQVYVKSILDGDSVFE-SSDGAAKGEIEILTKEIVR 203
Cdd:PHA02518 157 LAGYGLPILRNGTTQRVAYADAAEAGGSVLElPEDDKAAEEIIQLVKELFR 207
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-206 3.88e-31

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: 114.18  E-value: 3.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGK---------------------------- 52
Cdd:COG1192   1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPddldptlydlllddapledaivpteipg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C       53 ----------AAFDVFTAASEKDVYGIRKDLA----DYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSV 118
Cdd:COG1192  81 ldlipanidlAGAEIELVSRPGRELRLKRALApladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C      119 VTVLEA--QAYSRKVE-ARFLIT----RKIEMATMLNVLKESIKDtgvKAFRTAITQRQVYVKSILDGDSVFE---SSDG 188
Cdd:COG1192 161 LETIEEvrEDLNPKLEiLGILLTmvdpRTRLSREVLEELREEFGD---KVLDTVIPRSVALAEAPSAGKPVFEydpKSKG 237

                       250
                ....*....|....*...
5U1G_C      189 AAkgEIEILTKEIVRIFE 206
Cdd:COG1192 238 AK--AYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-139 4.19e-19

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: 82.01  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          4 ISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAG-------KAAFDVFT----------------- 59
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEgdiapalQALAEGLKgrvnldpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         60 -----------AASEKDVYGIRKDLA----------DYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAA--- 115
Cdd:pfam01656  81 gldlipgnidlEKFEKELLGPRKEERlrealealkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAkrl 160

                         170       180
                  ....*....|....*....|....*
5U1G_C        116 -GSVVTVLEAQAYSRKVEARFLITR 139
Cdd:pfam01656 161 gGVIAALVGGYALLGLKIIGVVLNK 185
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 1-200 6.59e-10

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: 57.68  E-value: 6.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTnwskagkAAFDV---FTAASEKDVYG--------- 68
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-------ALFGYqpeFDVGENETLYGairydderr 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         69 -----IRK------DL----------------------------------------ADYDFAIVDGAGSLSVITSAAVMV 97
Cdd:TIGR03453 177 piseiIRKtyfpglDLvpgnlelmefehetpralsrgqggdtiffarvgealaeveDDYDVVVIDCPPQLGFLTLSALCA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         98 SDLVIIPVTPSPLDFSA-------AGSVVTVL-EAQAYSRKVEARFLITR-------KIEMATML------NVLKES-IK 155
Cdd:TIGR03453 257 ATGVLITVHPQMLDVMSmsqfllmTGDLLGVVrEAGGNLSYDFMRYLVTRyepndgpQAQMVAFLrslfgdHVLTNPmLK 336

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
5U1G_C        156 DTGVK-AFRTAIT----QRQVYVKSILdgDSVFESSDgAAKGEIEILTKE 200
Cdd:TIGR03453 337 STAISdAGLTKQTlyevERSQFTRSTY--DRAMESLD-AVNAEIEGLIKK 383
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-46 7.00e-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: 36.78  E-value: 7.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
5U1G_C         6 FLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTN 46
Cdd:NF041417  16 FFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSD 56
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
3-200 1.74e-56

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 177.74  E-value: 1.74e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         3 VISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGKAA--FDVFTAASEkdvyGIRKDL----ADY 76
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDErpFPVVGLARP----TLHRELpslaRDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        77 DFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVT-VLEAQAYSRKVEARFLITRKIEMATMLNVLKESIK 155
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDlIKEAREYTPGLKAAFVLNRAIARTALGREVAEALA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
5U1G_C       156 DTGVKAFRTAITQRQVYVKSILDGDSVFE-SSDGAAKGEIEILTKE 200
Cdd:NF041546 157 EYGLPVLKTRIGQRVAFAESAAEGLTVFEaEPDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-155 5.82e-35

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: 120.34  E-value: 5.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSkagkaafdvftaasekdvygirkdladYDFAIV 81
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------YDYILI 53

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5U1G_C       82 DGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTVLEA---QAYSRKVEARFLITRKIEMATMLNVLKESIK 155
Cdd:cd02042  54 DTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEElkkQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PHA02518 PHA02518
ParA-like protein; Provisional
 2-203 3.50e-32

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 115.72  E-value: 3.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGKAAFDVFTAASekdvYG--IRKDL----AD 75
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVR----MGksIRADLpkvaSG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        76 YDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTVLEA-QAYS-RKVEARFLITRKIEMATMLNVLKES 153
Cdd:PHA02518  77 YDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKArQEVTdGLPKFAFIISRAIKNTQLYREARKA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
5U1G_C       154 IKDTGVKAFRTAITQRQVYVKSILDGDSVFE-SSDGAAKGEIEILTKEIVR 203
Cdd:PHA02518 157 LAGYGLPILRNGTTQRVAYADAAEAGGSVLElPEDDKAAEEIIQLVKELFR 207
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-206 3.88e-31

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: 114.18  E-value: 3.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGK---------------------------- 52
Cdd:COG1192   1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPddldptlydlllddapledaivpteipg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C       53 ----------AAFDVFTAASEKDVYGIRKDLA----DYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSV 118
Cdd:COG1192  81 ldlipanidlAGAEIELVSRPGRELRLKRALApladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C      119 VTVLEA--QAYSRKVE-ARFLIT----RKIEMATMLNVLKESIKDtgvKAFRTAITQRQVYVKSILDGDSVFE---SSDG 188
Cdd:COG1192 161 LETIEEvrEDLNPKLEiLGILLTmvdpRTRLSREVLEELREEFGD---KVLDTVIPRSVALAEAPSAGKPVFEydpKSKG 237

                       250
                ....*....|....*...
5U1G_C      189 AAkgEIEILTKEIVRIFE 206
Cdd:COG1192 238 AK--AYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-139 4.19e-19

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: 82.01  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          4 ISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAG-------KAAFDVFT----------------- 59
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEgdiapalQALAEGLKgrvnldpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         60 -----------AASEKDVYGIRKDLA----------DYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAA--- 115
Cdd:pfam01656  81 gldlipgnidlEKFEKELLGPRKEERlrealealkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAkrl 160

                         170       180
                  ....*....|....*....|....*
5U1G_C        116 -GSVVTVLEAQAYSRKVEARFLITR 139
Cdd:pfam01656 161 gGVIAALVGGYALLGLKIIGVVLNK 185
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-110 5.37e-17

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: 75.31  E-value: 5.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTnwskagkAAFDVFTAASEKDVY-----------GI 69
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAT-------SGLGIDKNNVEKTIYelligecnieeAI 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5U1G_C         70 RK-------------DLA-------------------------DYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPL 110
Cdd:pfam13614  74 IKtvienldlipsniDLAgaeieligienrenilkealepvkdNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYY 152
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
1-115 1.63e-12

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 64.09  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSK--AGKAAFD----VFTA---ASEKDVYGiRK 71
Cdd:PRK13849   1 MKLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWKEnaLRSNTWDpaceVYAAdelPLLEAAYE-DA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
5U1G_C        72 DLADYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAA 115
Cdd:PRK13849  80 ELQGFDYALADTHGGSSELNNTIIASSNLLLIPTMLTPLDIDEA 123
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 1-115 4.50e-12

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: 62.97  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSK--AGKAAFD----VFTA---ASEKDVYGiRK 71
Cdd:pfam07015   1 MQLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWREnaLRKGTWDpaceIFNAdelPLLEQAYE-HA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
5U1G_C         72 DLADYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAA 115
Cdd:pfam07015  80 EGSGFDYALADTHGGSSELNNTIIASSDLLLIPTMLTPLDIDEA 123
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 1-200 6.59e-10

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: 57.68  E-value: 6.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTnwskagkAAFDV---FTAASEKDVYG--------- 68
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-------ALFGYqpeFDVGENETLYGairydderr 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         69 -----IRK------DL----------------------------------------ADYDFAIVDGAGSLSVITSAAVMV 97
Cdd:TIGR03453 177 piseiIRKtyfpglDLvpgnlelmefehetpralsrgqggdtiffarvgealaeveDDYDVVVIDCPPQLGFLTLSALCA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         98 SDLVIIPVTPSPLDFSA-------AGSVVTVL-EAQAYSRKVEARFLITR-------KIEMATML------NVLKES-IK 155
Cdd:TIGR03453 257 ATGVLITVHPQMLDVMSmsqfllmTGDLLGVVrEAGGNLSYDFMRYLVTRyepndgpQAQMVAFLrslfgdHVLTNPmLK 336

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
5U1G_C        156 DTGVK-AFRTAIT----QRQVYVKSILdgDSVFESSDgAAKGEIEILTKE 200
Cdd:TIGR03453 337 STAISdAGLTKQTlyevERSQFTRSTY--DRAMESLD-AVNAEIEGLIKK 383
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-118 1.41e-09

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


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 56.31  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          3 VISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDP-QMSLTN-------WSKAGK-----AAFDVFTAASEKDVYG- 68
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRyfenrsaTADRTGlslptPEHLNLPDNDVAEVPDg 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
5U1G_C         69 -----------IRKDLADYDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSV 118
Cdd:pfam09140  82 eniddarleeaFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLLGQV 142
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-126 3.53e-08

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 49.74  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDpqmsltnwskagkaafdvftaasekdvygirkdladyDFAIV 81
Cdd:cd01983   1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD-------------------------------------DYVLI 43

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
5U1G_C       82 DGAGSLSVITSA-------AVMVSDLVIIPVTPSPLDFSAAGSVVTVLEAQA 126
Cdd:cd01983  44 DGGGGLETGLLLgtivallALKKADEVIVVVDPELGSLLEAVKLLLALLLLG 95
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-139 6.94e-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: 51.19  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C          1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQ--------MSLTN---WSKAGKAAFDVFTA--------- 60
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQnllrlhfgMDWSVrdgWARALLNGADWAAAayrspdgvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         61 --------ASEKDVYG------IRKDLADYDFA-----IVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTV 121
Cdd:TIGR03371  81 flpygdlsADEREAYQahdagwLARLLQQLDLAardwvLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLALA 160

                         170
                  ....*....|....*...
5U1G_C        122 LEAQAYSRkVEARFLITR 139
Cdd:TIGR03371 161 LFAGSGPR-DGPRFLINQ 177
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 1-45 4.14e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 49.67  E-value: 4.14e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
5U1G_C         1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLT 45
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLS 165
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-149 2.34e-06

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: 47.03  E-value: 2.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSR-SGYNIAVVDTDPQ-------MSLT---NWSKAGKAA---------------- 54
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQfgdvalyLDLEprrGLADALRNPdrldetlldraltrhs 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C       55 --FDVFTAA---------SEKDVYGIRKDLAD-YDFAIVDGAGSLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTVL 122
Cdd:COG4963 183 sgLSVLAAPadleraeevSPEAVERLLDLLRRhFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLL 262

                       170       180       190
                ....*....|....*....|....*....|....*
5U1G_C      123 EAQAYSR--------KVEARFLITRKiEMATMLNV 149
Cdd:COG4963 263 RELGLPDdkvrlvlnRVPKRGEISAK-DIEEALGL 296
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-157 2.39e-06

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: 46.81  E-value: 2.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDpqMSLTNWSK----------------AGKAAFD--------- 56
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--IGLRNLDLilglenrivytlvdvlEGECRLEqalikdkrw 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C       57 ---VFTAAS---EKDVYGIRK------DLAD-YDFAIVD-----GAGSLSVITSAavmvsDLVIIPVTPSPLDFSAAGSV 118
Cdd:cd02036  79 enlYLLPASqtrDKDALTPEKleelvkELKDsFDFILIDspagiESGFINAIAPA-----DEAIIVTNPEISSVRDADRV 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
5U1G_C      119 VTVLEAQAysrKVEARFLITR-KIEMA---TMLNVlkESIKDT 157
Cdd:cd02036 154 IGLLESKG---IVNIGLIVNRyRPEMVksgDMLSV--EDIQEI 191
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 10-44 2.55e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 46.70  E-value: 2.55e-06
                        10        20        30
                ....*....|....*....|....*....|....*
5U1G_C       10 KGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSL 44
Cdd:COG3640   8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANL 42
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-39 4.10e-06

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 46.20  E-value: 4.10e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTD 39
Cdd:COG2894   3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 17-131 4.81e-06

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: 45.65  E-value: 4.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C       17 TAVINIATALSRSGYNIAVVDTDPQM-----------------------SLTNWSKAGKAAFDVFTAAS----------E 63
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLanldvllglepkatladvlageaDLEDAIVQGPGGLDVLPGGSgpaelaeldpE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C       64 KDVYGIRKDLA-DYDFAIVD-GAGsLSVITSAAVMVSDLVIIPVTPSPLDFSAAGSVVTVLEAQAYSRKV 131
Cdd:COG0455  81 ERLIRVLEELErFYDVVLVDtGAG-ISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRRA 149
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-39 4.58e-05

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: 43.10  E-value: 4.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
5U1G_C          2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTD 39
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-109 5.88e-05

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: 42.56  E-value: 5.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTD-------------PQMSLTNWSKA----------GKAAFDVF 58
Cdd:cd02038   1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGrvslediiveGPEGLDII 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5U1G_C       59 TAAS---------EKDVYGIRKDL----ADYDFAIVD-GAGSLSVITSAAVMVSDLVIIpVTPSP 109
Cdd:cd02038  81 PGGSgmeelanldPEQKAKLIEELssleSNYDYLLIDtGAGISRNVLDFLLAADEVIVV-TTPEP 144
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 1-44 6.76e-05

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 42.72  E-value: 6.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
5U1G_C          1 MKVIsFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSL 44
Cdd:pfam02374   1 MRWI-FFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSL 43
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-39 1.50e-04

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: 41.71  E-value: 1.50e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
5U1G_C        3 VISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTD 39
Cdd:COG0489  94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDAD 130
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 10-39 1.60e-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: 41.28  E-value: 1.60e-04
                          10        20        30
                  ....*....|....*....|....*....|
5U1G_C         10 KGGSGKTTAVINIATALSRSGYNIAVVDTD 39
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-43 2.49e-04

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: 40.87  E-value: 2.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
5U1G_C          2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMS 43
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMA 42
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 1-45 2.94e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 40.91  E-value: 2.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
5U1G_C         1 MKVISFLNpKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLT 45
Cdd:PRK13230   1 MRKFCFYG-KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCT 44
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
10-65 3.12e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 40.50  E-value: 3.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
5U1G_C         10 KGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTNWSKAGKAAFDVFTAASEKD 65
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKG 63
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 12-85 3.34e-04

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 40.96  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        12 GSGKTTAVINIATALSRSGYNIAVVDTD---P-------QMsltnwskAGKAAFDVFTAASEKDVYGIRKD----LADYD 77
Cdd:PRK00771 105 GSGKTTTAAKLARYFKKKGLKVGLVAADtyrPaaydqlkQL-------AEKIGVPFYGDPDNKDAVEIAKEglekFKKAD 177


                 ....*...
5U1G_C        78 FAIVDGAG 85
Cdd:PRK00771 178 VIIVDTAG 185
minD CHL00175
septum-site determining protein; Validated
 2-39 4.12e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.14  E-value: 4.12e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
5U1G_C         2 KVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTD 39
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 10-44 4.46e-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: 39.99  E-value: 4.46e-04
                        10        20        30
                ....*....|....*....|....*....|....*
5U1G_C       10 KGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSL 44
Cdd:cd02034   8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNL 42
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 2-44 5.65e-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: 39.80  E-value: 5.65e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
5U1G_C        2 KVISFLNpKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSL 44
Cdd:cd02035   1 RIIFFGG-KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSL 42
PRK14494 PRK14494
putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing ...
 1-90 1.30e-03

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


Pssm-ID: 237731 [Multi-domain]  Cd Length: 229  Bit Score: 38.42  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C         1 MKVISFLNPKGgSGKTTAVINIATALSRSGYNIAVV----------DTDPQmsltNWSKAGKAAfdVFTAASEKDV-YGI 69
Cdd:PRK14494   1 MRAIGVIGFKD-SGKTTLIEKILKNLKERGYRVATAkhthhefdkpDTDTY----RFKKAGAEV--VVVSTDETAAfLYD 73

                         90       100
                 ....*....|....*....|....*..
5U1G_C        70 RKDLA------DYDFAIVDGAGSLSVI 90
Cdd:PRK14494  74 RMDLNeilsllDADFLLIEGFKELLNI 100
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 1-36 1.41e-03

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


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 37.85  E-value: 1.41e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
5U1G_C        1 MKVISFLNPKGgSGKTTAVINIATALSRSGYNIAVV 36
Cdd:COG1763   1 MPVLGIVGYSG-SGKTTLLEKLIPELKARGLRVGTI 35
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-44 1.84e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 38.26  E-value: 1.84e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
5U1G_C        1 MKVISFLNpKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSL 44
Cdd:COG0003   3 TRIIFFTG-KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSL 45
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-45 2.07e-03

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: 37.80  E-value: 2.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
5U1G_C          1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTD---PQMSLT 45
Cdd:TIGR01007  17 IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDmrnSVMSGT 64
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-96 2.56e-03

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: 37.55  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5U1G_C        1 MKVISFLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSltnwskagkAAFDVFTAASEKDVY-GIRKDLADYDFA 79
Cdd:cd05387  19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRP---------SLHRLLGLPNEPGLSeVLSGQASLEDVI 89

                        90
                ....*....|....*..
5U1G_C       80 IVDGAGSLSVITSAAVM 96
Cdd:cd05387  90 QSTNIPNLDVLPAGTVP 106
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 10-42 2.68e-03

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: 37.48  E-value: 2.68e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
5U1G_C       10 KGGSGKTTAVINIATALSRSGYNIAVVDTD------PQM 42
Cdd:cd02037   9 KGGVGKSTVAVNLALALAKKGYKVGLLDADiygpsiPRL 47
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-46 7.00e-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: 36.78  E-value: 7.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
5U1G_C         6 FLNPKGGSGKTTAVINIATALSRSGYNIAVVDTDPQMSLTN 46
Cdd:NF041417  16 FFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSD 56
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-39 7.83e-03

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: 36.10  E-value: 7.83e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
5U1G_C        2 KVISFLNPKGGSGKTTAVINIATALS-RSGYNIAVVDTD 39
Cdd:cd03111   1 RVVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLD 39
 
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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