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Conserved domains on  [gi|1745905471|gb|KAA5399914|]
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ParA family protein [Phocaeicola dorei]

Protein Classification

ParA family protein( domain architecture ID 11439703)

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-252 1.19e-127

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: 361.87  E-value: 1.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVECSIYECIINEADIREAIYTTDIDGL 82
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 DIVSSHIDLVGAEIEMLNLEDREKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKLL 162
Cdd:COG1192    82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 163 NTIKIIKSKLNPSLEIEGFLLTMFDSRLRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGAKNH 242
Cdd:COG1192   162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                         250
                  ....*....|
gi 1745905471 243 LALAQEIITR 252
Cdd:COG1192   242 RALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-252 1.19e-127

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: 361.87  E-value: 1.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVECSIYECIINEADIREAIYTTDIDGL 82
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 DIVSSHIDLVGAEIEMLNLEDREKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKLL 162
Cdd:COG1192    82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 163 NTIKIIKSKLNPSLEIEGFLLTMFDSRLRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGAKNH 242
Cdd:COG1192   162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                         250
                  ....*....|
gi 1745905471 243 LALAQEIITR 252
Cdd:COG1192   242 RALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 5.50e-93

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: 270.99  E-value: 5.50e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   2 GKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVECSIYECIINEADIREAIYTTDIDG 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  82 LDIVSSHIDLVGAEIEMLNLEDREKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1745905471 162 LNTIKIIKSKLNPSLEI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 1.92e-49

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: 158.86  E-value: 1.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLgvnikevecsiyeciineadireaiyttdidgl 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 divsshidlvgaeiemlnledrekimkkvlapmrdeYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKLL 162
Cdd:cd02042    48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1745905471 163 NTIKIIKSKLNPSLEIEGFLLTMFDSRLRLANQIYDEVK 201
Cdd:cd02042    92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-250 6.21e-27

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: 104.43  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD-PQANASSGLGVNIKEVecSIYECIINEADIREAIYTTDiDG 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPV--TLHDVLAGEADIKDAIYEGP-FG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  82 LDIVSSHIDLvgaeiEMLNLEDREKiMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKl 161
Cdd:TIGR01969  78 VKVIPAGVSL-----EGLRKADPDK-LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALK- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 162 lntIKIIKSKLNpsLEIEGFLLTMFDsrlRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGAKN 241
Cdd:TIGR01969 151 ---TKIVAEKLG--TAILGVVLNRVT---RDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQA 222


                  ....*....
gi 1745905471 242 HLALAQEII 250
Cdd:TIGR01969 223 FMELAAELA 231
ParA_partition NF041546
ParA family partition ATPase;
4-149 2.36e-25

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 99.16  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASsglgvnikevecsiyeciiNEADIREAiyttdidgld 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL-------------------DWAAARED---------- 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745905471  84 ivSSHIDLVGAeiemlnleDREKIMKKvLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQ 149
Cdd:NF041546   52 --ERPFPVVGL--------ARPTLHRE-LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-162 9.42e-22

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 93.20  E-value: 9.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVnIKEVEC----SIYECIINEAD---IREAIY 75
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGV-LPETDVganeTLYAAIRYDDTrrpLRDVIR 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  76 TTDIDGLDIVSSHIDLVgaEIEMLN---LEDRE-------KIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVI 145
Cdd:PRK13869  201 PTYFDGLHLVPGNLELM--EFEHTTpkaLSDKGtrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMV 278

                         170
                  ....*....|....*..
gi 1745905471 146 IPVQCEYFALEGISKLL 162
Cdd:PRK13869  279 ITVHPQMLDIASMSQFL 295
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-252 1.19e-127

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: 361.87  E-value: 1.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVECSIYECIINEADIREAIYTTDIDGL 82
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 DIVSSHIDLVGAEIEMLNLEDREKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKLL 162
Cdd:COG1192    82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 163 NTIKIIKSKLNPSLEIEGFLLTMFDSRLRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGAKNH 242
Cdd:COG1192   162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                         250
                  ....*....|
gi 1745905471 243 LALAQEIITR 252
Cdd:COG1192   242 RALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 5.50e-93

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: 270.99  E-value: 5.50e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   2 GKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVECSIYECIINEADIREAIYTTDIDG 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  82 LDIVSSHIDLVGAEIEMLNLEDREKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1745905471 162 LNTIKIIKSKLNPSLEI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-228 2.30e-55

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: 177.54  E-value: 2.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   5 IALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASS--GLGVNIKEVECSIYECIINEADIREAIYTTDID-- 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSveGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  81 GLDIVSSHIDLVGAEIEMLNLEDREKImKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISK 160
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERL-REALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1745905471 161 LLNTIKIIKSKLNP-SLEIEGFLLTMFDSRlRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIP 228
Cdd:pfam01656 160 LGGVIAALVGGYALlGLKIIGVVLNKVDGD-NHGKLLKEALEELLRGLPVLGVIPRDEAVAEAPARGLP 227
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 1.92e-49

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: 158.86  E-value: 1.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLgvnikevecsiyeciineadireaiyttdidgl 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 divsshidlvgaeiemlnledrekimkkvlapmrdeYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKLL 162
Cdd:cd02042    48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1745905471 163 NTIKIIKSKLNPSLEIEGFLLTMFDSRLRLANQIYDEVK 201
Cdd:cd02042    92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-252 2.91e-27

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: 104.59  E-value: 2.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  18 TTTINLAASLATLEKKVLVIDADPQ-ANASSGLGVnikEVECSIYECIINEADIREAIYTTDiDGLDIVSSHIDLVgaei 96
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGL---EPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPA---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  97 EMLNLEDREKIMKkVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKllnTIKIIKSKLNpsL 176
Cdd:COG0455    73 ELAELDPEERLIR-VLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYA---LLKLLRRRLG--V 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 177 EIEGFLLTMFDSR---LRLANQIYDEVKRHFQ-ELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGAKNHLALAQEIITR 252
Cdd:COG0455   147 RRAGVVVNRVRSEaeaRDVFERLEQVAERFLGvRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-250 6.21e-27

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: 104.43  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD-PQANASSGLGVNIKEVecSIYECIINEADIREAIYTTDiDG 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPV--TLHDVLAGEADIKDAIYEGP-FG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  82 LDIVSSHIDLvgaeiEMLNLEDREKiMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYFALEGISKl 161
Cdd:TIGR01969  78 VKVIPAGVSL-----EGLRKADPDK-LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALK- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 162 lntIKIIKSKLNpsLEIEGFLLTMFDsrlRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGAKN 241
Cdd:TIGR01969 151 ---TKIVAEKLG--TAILGVVLNRVT---RDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQA 222


                  ....*....
gi 1745905471 242 HLALAQEII 250
Cdd:TIGR01969 223 FMELAAELA 231
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-148 8.56e-27

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: 106.60  E-value: 8.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGV----NIKEVEcSIYECIINEA---DIREAIYT 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpefDVGENE-TLYGAIRYDDerrPISEIIRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  77 TDIDGLDIVSSHIDLVGAEIE----MLNLEDREKI----MKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPV 148
Cdd:TIGR03453 185 TYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLITV 264
ParA_partition NF041546
ParA family partition ATPase;
4-149 2.36e-25

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 99.16  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASsglgvnikevecsiyeciiNEADIREAiyttdidgld 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL-------------------DWAAARED---------- 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745905471  84 ivSSHIDLVGAeiemlnleDREKIMKKvLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQ 149
Cdd:NF041546   52 --ERPFPVVGL--------ARPTLHRE-LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-162 9.42e-22

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 93.20  E-value: 9.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVnIKEVEC----SIYECIINEAD---IREAIY 75
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGV-LPETDVganeTLYAAIRYDDTrrpLRDVIR 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  76 TTDIDGLDIVSSHIDLVgaEIEMLN---LEDRE-------KIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVI 145
Cdd:PRK13869  201 PTYFDGLHLVPGNLELM--EFEHTTpkaLSDKGtrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMV 278

                         170
                  ....*....|....*..
gi 1745905471 146 IPVQCEYFALEGISKLL 162
Cdd:PRK13869  279 ITVHPQMLDIASMSQFL 295
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 4-189 3.22e-21

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: 89.86  E-value: 3.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADP-QANASSGLGVnikEVECSIYECIINEADIREAIYTTDIDGL 82
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGL---ENRPGLSDVLAGEASLEDVIQPTEVEGL 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 DIVSShIDLVGAEIEMLNledrEKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTA-ADSVIIPVQCEYFALEGISKL 161
Cdd:COG0489   171 DVLPA-GPLPPNPSELLA----SKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASlVDGVLLVVRPGKTALDDVRKA 245

                         170       180
                  ....*....|....*....|....*...
gi 1745905471 162 LNTIKIIKSKlnpsleIEGFLLTMFDSR 189
Cdd:COG0489   246 LEMLEKAGVP------VLGVVLNMVCPK 267
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-249 4.92e-21

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: 88.41  E-value: 4.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD-PQANASSGLGVNIKEVeCSIYECIINEADIREAIYTTD-ID 80
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIV-YTLVDVLEGECRLEQALIKDKrWE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  81 GLDIVSSHIDLVGAEIemlnleDREKiMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEyfaLEGISK 160
Cdd:cd02036    80 NLYLLPASQTRDKDAL------TPEK-LEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPE---ISSVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 161 LLNTIKIIKSKlnpSLEIEGFLLTMFDS-RLRLANQIYDEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAILYDADSTGA 239
Cdd:cd02036   150 ADRVIGLLESK---GIVNIGLIVNRYRPeMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAA 226

                         250
                  ....*....|
gi 1745905471 240 KNHLALAQEI 249
Cdd:cd02036   227 KAFENIARRL 236
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-214 9.18e-20

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 87.34  E-value: 9.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDA-DPQANASSGLG----VNIKEVECSIYECIINEADIREAIYTTD 78
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHGwvpdLHIHAEDTLLPFYLGEKDDATYAIKPTC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  79 IDGLDIVSSHIDLVGAEIEMLNLEDREKI-------MKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCE 151
Cdd:PRK13705  188 WPGLDIIPSCLALHRIETELMGKFDEGKLptdphlmLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1745905471 152 YF----ALEGISKLLNTIKIIKSK-LNPSLEIegfLLTMFDSRLRLANQIYDE-VKRHFQELVFKTIVQ 214
Cdd:PRK13705  268 LFdytsALQFFDMLRDLLKNVDLKgFEPDVRI---LLTKYSNSNGSQSPWMEEqIRDAWGSMVLKNVVR 333
PHA02518 PHA02518
ParA-like protein; Provisional
 3-254 1.04e-19

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 84.13  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGlgvnikevecsiyeciineADIREaiyttdidgl 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW-------------------AEARE---------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 divssHIDLVGAEIEMlnledrEKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEYF---ALEGIS 159
Cdd:PHA02518   52 -----EGEPLIPVVRM------GKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFdiwAAPDLV 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 160 KLLNTIKIIksklNPSLEIEGFLLtmfdSRLRLANQIYDEVKRHFQEL---VFKTIVQRNVKLSEAPSHGIPAILYDADS 236
Cdd:PHA02518  121 ELIKARQEV----TDGLPKFAFII----SRAIKNTQLYREARKALAGYglpILRNGTTQRVAYADAAEAGGSVLELPEDD 192

                         250
                  ....*....|....*...
gi 1745905471 237 TGAKNHLALAQEIITRNS 254
Cdd:PHA02518  193 KAAEEIIQLVKELFRGIS 210
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-146 1.31e-19

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: 84.54  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD-PQANASSGLGVNIKEvecSIYECIINEADIREAIYTTDiDG 81
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPKK---TLGDVLKGRVSLEDIIVEGP-EG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1745905471  82 LDIVSSHIDLVgaEIEMLNLEDREKIMKKvLAPMRDEYDYILIDCSPSLGLITINALTAADSVII 146
Cdd:cd02038    77 LDIIPGGSGME--ELANLDPEQKAKLIEE-LSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-214 5.56e-18

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 82.37  E-value: 5.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDA-DPQANASSGLG----VNIKEVECSIYECIINEADIREAIYTTD 78
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGnDPQGTASMYHGyvpdLHIHADDTLLPFYLGERDNAEYAIKPTC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  79 IDGLDIVSSHIDLVGAEIEMLNLEDREKI-------MKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCE 151
Cdd:PHA02519  188 WPGLDIIPSCLALHRIETDLMQYHDAGKLphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAE 267

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1745905471 152 YF----ALEGISKLLNTIKIIK-SKLNPSLEIegfLLTMFDsrLRLANQ---IYDEVKRHFQELVFKTIVQ 214
Cdd:PHA02519  268 LFdyvsVLQFFTMLLDLLATVDlGGFEPVVRL---LLTKYS--LTVGNQsrwMEEQIRNTWGSMVLRQVVR 333
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-253 6.88e-18

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: 81.70  E-value: 6.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   2 GKIIALANQKGGVGKTTTTINLAASLATL-EKKVLVIDADPQA-NASSGLGVNikevecsiyeciiNEADIREAIYTTD- 78
Cdd:COG4963   102 GRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFgDVALYLDLE-------------PRRGLADALRNPDr 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  79 IDGLDI------VSSHIDLVGAEIEMLNLED-REKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCE 151
Cdd:COG4963   169 LDETLLdraltrHSSGLSVLAAPADLERAEEvSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPD 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 152 yfaLEGISKLLNTIKIIKSKLNPSLEIEgFLLTMFDSRLRLANQiydEVKRHFQELVFKTIVQRNVKLSEAPSHGIPAIL 231
Cdd:COG4963   249 ---LPSLRNAKRLLDLLRELGLPDDKVR-LVLNRVPKRGEISAK---DIEEALGLPVAAVLPNDPKAVAEAANQGRPLAE 321

                         250       260
                  ....*....|....*....|..
gi 1745905471 232 YDADSTGAKNHLALAQEIITRN 253
Cdd:COG4963   322 VAPKSPLAKAIRKLAARLTGRP 343
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-146 3.00e-17

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 78.56  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   1 MGKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADpqanasSGL-------G---------VNIKEVECSiyeci 64
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD------IGLrnldlvmGlenrivydlVDVIEGECR----- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  65 INEADIREAiyttDIDGLDIvsshidLVGAEI---EMLNLEDrekiMKKVLAPMRDEYDYILIDCsPSlGlitI-----N 136
Cdd:COG2894    70 LKQALIKDK----RFENLYL------LPASQTrdkDALTPEQ----MKKLVEELKEEFDYILIDS-PA-G---IeqgfkN 130

                         170
                  ....*....|
gi 1745905471 137 ALTAADSVII 146
Cdd:COG2894   131 AIAGADEAIV 140
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-146 8.48e-16

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: 73.37  E-value: 8.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD---PQANASSGL----GVNikevecsiyECIINEADIREAIY 75
Cdd:cd05387    20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGLpnepGLS---------EVLSGQASLEDVIQ 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1745905471  76 TTDIDGLDIV-SSHIDLVGAeiEMLNledrEKIMKKVLAPMRDEYDYILIDCSPSLGLITINAL-TAADSVII 146
Cdd:cd05387    91 STNIPNLDVLpAGTVPPNPS--ELLS----SPRFAELLEELKEQYDYVIIDTPPVLAVADALILaPLVDGVLL 157
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-246 4.88e-14

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: 69.30  E-value: 4.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIkEVECSIYECIINEADIREAIYtTDIDGL 82
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDW-SVRDGWARALLNGADWAAAAY-RSPDGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  83 DIVSshidlVGAeiemLNLEDREKIMK-------KVLAPM-RDEYDYILIDCSPSLGLITINALTAADSVIIPVQCE--- 151
Cdd:TIGR03371  80 LFLP-----YGD----LSADEREAYQAhdagwlaRLLQQLdLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADaac 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 152 -------YFALEGISKLLNTIKIIKSKLNPSLE----IEGFLLTMFDSRLrlanqiydevkrhfqelvFKTIVQRNVKLS 220
Cdd:TIGR03371 151 yatlhqlALALFAGSGPRDGPRFLINQFDPARQlsrdVRAVLRQTLGSRL------------------LPFVIHRDEAVS 212

                         250       260
                  ....*....|....*....|....*.
gi 1745905471 221 EAPSHGIPAILYDADSTGAKNHLALA 246
Cdd:TIGR03371 213 EALARGTPVLNYAPHSQAAHDIRTLA 238
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-250 4.71e-13

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: 66.98  E-value: 4.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   2 GKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD-PQANASSGLG---------VNIKEVECSiyeciINEADIR 71
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiGLRNLDLLLGlenrivytlVDVVEGECR-----LQQALIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  72 EAIYttdiDGLDIvsshidLVGAEIEMLNLEDREKiMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCE 151
Cdd:TIGR01968  76 DKRL----KNLYL------LPASQTRDKDAVTPEQ-MKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 152 YFAL------------EGISKllntIKIIKSKLNPSLEIEGFLLTMfdsrlrlanqiyDEVKRHFQeLVFKTIVQRNVKL 219
Cdd:TIGR01968 145 VSAVrdadrviglleaKGIEK----IHLIVNRLRPEMVKKGDMLSV------------DDVLEILS-IPLIGVIPEDEAI 207

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1745905471 220 SEAPSHGIPAILyDADSTGAKNHLALAQEII 250
Cdd:TIGR01968 208 IVSTNKGEPVVL-NDKSRAGKAFENIARRIL 237
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-155 9.92e-13

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 65.15  E-value: 9.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLgVNIKEVECSIYECIINEADIREAIYTTDIDGL 82
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGT-FKSQNKITGLTNFLSGTTDLSDAICDTNIENL 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745905471  83 DIVSShidlvGA----EIEMLnledREKIMKKVLAPMRDEYDYILIDCSPslglitINALTaaDSVIIPVQCEYFAL 155
Cdd:TIGR01007  97 DVITA-----GPvppnPTELL----QSSNFKTLIETLRKRFDYIIIDTPP------IGTVT--DAAIIARACDASIL 156
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-231 1.60e-12

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 64.99  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEK-KVLVIDADPQANassglgvnikevECSIYECIINEADIREAIytTDIDG 81
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPFG------------DLGLYLNLRPDYDLADVI--QNLDR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  82 LDIV---------SSHIDLVGAEIEMLNLED-REKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQce 151
Cdd:cd03111    67 LDRTlldsavtrhSSGLSLLPAPQELEDLEAlGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQ-- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 152 yfalEGISKLLNTIKIIKS-----KLNPSLEIegfLLTMFDSRLRLANqiyDEVKRHFQELVFKTIVQRNVKLSEAPSHG 226
Cdd:cd03111   145 ----QDLPSLRNARRLLDSlreleGSSDRLRL---VLNRYDKKSEISP---KDIEEALGLEVFATLPNDYKAVSESANTG 214


                  ....*
gi 1745905471 227 IPAIL 231
Cdd:cd03111   215 RPLVE 219
minD CHL00175
septum-site determining protein; Validated
 1-146 5.34e-10

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 58.24  E-value: 5.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   1 MGKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD-PQANASSGLGVNIKEVECSIY----ECIINEADIReaiy 75
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRVLYTAMDvlegECRLDQALIR---- 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1745905471  76 ttdidglDIVSSHIDLVGAEIEMLNLEDREKIMKKVLAPMRDE-YDYILIDCSPSLGLITINALTAADSVII 146
Cdd:CHL00175   90 -------DKRWKNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRgYDYILIDCPAGIDVGFINAIAPAQEAIV 154
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 3-172 5.37e-10

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 59.35  E-value: 5.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQanaSSGLGVNI-KEVECSIYECIINEADIREAIYTTDIDG 81
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIR---KGGLHQMFgKAPKPGLLDLLAGEASIEAGIHRDQRPG 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  82 LDIV----SSHIDLVGAEIeMLNledreKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTA-ADSVIIPVQCEYFALE 156
Cdd:TIGR01005 631 LAFIaaggASHFPHNPNEL-LAN-----PAMAELIDNARNAFDLVLVDLAALAAVADAAAFAAlADGILFVTEFERSPLG 704

                         170
                  ....*....|....*.
gi 1745905471 157 GISKLLNTIKIIKSKL 172
Cdd:TIGR01005 705 EIRDLIHQEPHANSDV 720
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-40 2.37e-09

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 56.31  E-value: 2.37e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD 40
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 3-74 2.66e-09

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 55.94  E-value: 2.66e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1745905471   3 KIIALANqKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVnikEVECSIYECIineADIREAI 74
Cdd:COG3640     1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGL---EVEADLIKPL---GEMRELI 65
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 7.65e-09

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 54.43  E-value: 7.65e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD 40
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-128 1.01e-07

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 51.35  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNI-KEVECSIYEciiN----EADIREAIY---------- 75
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLgGETPVKGAP---NlwamEIDPEEALEeyweevkell 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1745905471  76 --TTDIDGLDIVSSHIDLV--GAEiEMLNLedrEKIMKKVLApmrDEYDYILIDCSP 128
Cdd:cd02035    85 aqYLRLPGLDEVYAEELLSlpGMD-EAAAF---DELREYVES---GEYDVIVFDTAP 134
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-148 2.79e-07

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: 50.15  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADP-QANASSGLGVNIKEVECSIYECIINEADIREAIYTTDIDGl 82
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATADRTGLSLPTPEHLNLPDNDVAEVPD- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745905471  83 divsshidlvGAEIEMLNLEdrekimkKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPV 148
Cdd:pfam09140  81 ----------GENIDDARLE-------EAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-50 2.86e-07

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 50.15  E-value: 2.86e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLG 50
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV 48
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 3-247 3.17e-07

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


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 49.68  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPqanaSSGLGVNIkEVECSIYE----CIINEADIREAIYTTd 78
Cdd:pfam06564   2 KILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSP----DNLLRLHF-NVPFEHRQgwarAELDGADWRDAALEY- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  79 IDGLDIVsSHIDLVGAEIEMLN-LEDREKIMKKVLAPMRDEYDYILIDCSPSLGLITINALTAADSVIIPVQCEyfalEG 157
Cdd:pfam06564  76 TPGLDLL-PFGRLSVEEQENLQqLQPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD----AN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471 158 ISKLLNTIkiiksklnpSLEIEGFLLTmfdSRLRLANQIYDEVK---RHFQELVFKTIVQRNVKLSEAPSHGIPAILYDA 234
Cdd:pfam06564 151 CHVLLHQQ---------PLPDADHLLI---NDFRPASQLQQDLLqlwRQSQRRLLPLVIHRDEALAEALAAKQPLGEYRP 218

                         250
                  ....*....|...
gi 1745905471 235 DSTGAKNHLALAQ 247
Cdd:pfam06564 219 DSLAAEEVLTLAN 231
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 6.60e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 46.66  E-value: 6.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1745905471   3 KIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD 40
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-49 1.18e-06

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: 48.52  E-value: 1.18e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGL 49
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-42 1.31e-06

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 48.42  E-value: 1.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1745905471   1 MGKIIALANqKGGVGKTTTTINLAASLATLEKKVLVIDADPQ 42
Cdd:PRK13185    1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 5-74 1.42e-06

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


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 48.08  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   5 IALANqKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVecsiyECIINEADIREAI 74
Cdd:cd02034     3 IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKL-----PLIKTIGDIRERT 66
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-40 1.93e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 48.12  E-value: 1.93e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD 40
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 11-42 3.55e-06

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 46.91  E-value: 3.55e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQ 42
Cdd:cd02032     8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPK 39
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-47 4.19e-06

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 46.67  E-value: 4.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASS 47
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTR 44
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-56 4.26e-06

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 46.74  E-value: 4.26e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGL--GVNIKEV 56
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLlgGKAIPTV 55
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 11-128 9.65e-06

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: 45.80  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNIKEVECSIYECI-INEADIREAIY-----TTDIDGLDI 84
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEPTKVKENLsAMEIDPNMELEeywqeVQKYMNALL 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1745905471  85 VSSHIDLVGAEiEMLNLEDREKIMK--KVLAPMR-DEYDYILIDCSP 128
Cdd:pfam02374  89 GLRMLEGILAE-ELASLPGIDEAASfdEFKKYMDeGEYDVVVFDTAP 134
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-129 2.20e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 44.81  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGVNI--KEVECSIYECIINEADIREAI--YTTDIDGL--DI 84
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELgnEPTEVAVPNLYALEIDPEAELeeYWERVRAPlrGL 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1745905471  85 VSSHIDLVGAEI-----EMLNLEdrekIMKKVLApmRDEYDYILIDCSPS 129
Cdd:COG0003    91 LPSAGVDELAESlpgteELAALD----ELLELLE--EGEYDVIVVDTAPT 134
PRK10818 PRK10818
septum site-determining protein MinD;
1-40 1.14e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 42.62  E-value: 1.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1745905471   1 MGKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDAD 40
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-201 1.31e-04

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


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 42.14  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   2 GKIIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGLGV----NIKEVECSIYECIINEADIREAIYTT 77
Cdd:cd17869     3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGAsgryLMSDHLYTLKSRKANLADKLESCVKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  78 DIDGLDIVSShIDLVGAEIEMLNLEDREKIMKKVLApmrDEYDYILIDCSPSLGLITINALTAADSVIIPVqceyfaLEG 157
Cdd:cd17869    83 HESGVYYFSP-FKSALDILEIKKDDILHMITKLVEA---HAYDYIIMDLSFEFSSTVCKLLQASHNNVVIA------LQD 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1745905471 158 ISKLLNTIKIIKSKLNPSLEIEGFLLTMFDSRLRLANQIYDEVK 201
Cdd:cd17869   153 ANSSYKLNKFLRALEDLFQENFSYIYNKYSNNVEDSLSTNIEKK 196
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-44 4.38e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 41.23  E-value: 4.38e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQAN 44
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
chlL CHL00072
photochlorophyllide reductase subunit L
 11-42 7.08e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 40.11  E-value: 7.08e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQ 42
Cdd:CHL00072    8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPK 39
nifH PRK13233
nitrogenase iron protein;
11-46 1.17e-03

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 39.42  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1745905471  11 KGGVGKTTTTINLAASLATL-EKKVLVIDADPQANAS 46
Cdd:PRK13233   10 KGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADST 46
PRK10037 PRK10037
cellulose biosynthesis protein BcsQ;
4-41 1.39e-03

cellulose biosynthesis protein BcsQ;


Pssm-ID: 182204  Cd Length: 250  Bit Score: 39.09  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1745905471   4 IIALANQKGGVGKTTTTINLAASLATLEKKVLVIDADP 41
Cdd:PRK10037    3 ILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACP 40
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-146 1.46e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 38.91  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471   4 IIALANQKGGVGKTTttinLAASLATLEKKVLVIDADPQA-NASSGLGVNIKE-----------------VECSIYE--C 63
Cdd:cd03110     1 IIAVLSGKGGTGKTT----ITANLAVLLYNVILVDCDVDApNLHLLLGPEPEEeedfvggkkafidqekcIRCGNCErvC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905471  64 ------------IINE---------ADI--REAIYTTDIDGLDIVSSHIDLVGAEIEMLNLEDRE--KI---MKKVLAPM 115
Cdd:cd03110    77 kfgaileffqklIVDEslcegcgacVIIcpRGAIYLKDRDTGKIFISSSDGGPLVHGRLNIGEENsgKLvteLRKKALER 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1745905471 116 RDEYDYILIDCSPSLGLITINALTAADSVII 146
Cdd:cd03110   157 SKECDLAIIDGPPGTGCPVVASITGADAVLL 187
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 3-49 1.72e-03

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 39.04  E-value: 1.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1745905471   3 KIIALANqKGGVGKTTTTINLAASLATLEKKVLVIDADPQANASSGL 49
Cdd:cd02033    32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLL 77
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-46 1.82e-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: 39.30  E-value: 1.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1745905471  11 KGGVGKTTTTINLAASLATLEKKVLVIDADPQANAS 46
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLS 364
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 11-49 4.19e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 37.85  E-value: 4.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1745905471  11 KGGVGKTTTTINLAASLATlEKKVLVIDADPQANASSGL 49
Cdd:PRK13231   10 KGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTRTL 47
 
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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