NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|547475456|ref|WP_022093800|]
View 

MULTISPECIES: ParA family protein [Collinsella]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 15-265 5.48e-136

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: 383.44  E-value: 5.48e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDLDHCIYDALLNDVPAESLVLDTNCKK 94
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  95 VFVIPATIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKL 174
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 175 LESMKMVKSRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQNKGAKA 254
Cdd:COG1192  161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|.
gi 547475456 255 YMNLAKEVIKR 265
Cdd:COG1192  241 YRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 15-265 5.48e-136

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: 383.44  E-value: 5.48e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDLDHCIYDALLNDVPAESLVLDTNCKK 94
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  95 VFVIPATIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKL 174
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 175 LESMKMVKSRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQNKGAKA 254
Cdd:COG1192  161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|.
gi 547475456 255 YMNLAKEVIKR 265
Cdd:COG1192  241 YRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 15-190 1.54e-86

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: 255.20  E-value: 1.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDLDHCIYDALLNDVPAESLVLDTNCKK 94
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   95 VFVIPATIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKL 174
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*.
gi 547475456  175 LESMKMVKSRLNKGLD 190
Cdd:pfam13614 161 LNTIKLVKKRLNPSLE 176
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 16-214 7.14e-51

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: 162.71  E-value: 7.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFgiekedldhciydallndvpaeslvldtnckkv 95
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  96 fvipatiqlagaeielvsaiaretrlkdllepiqdeFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKLL 175
Cdd:cd02042   48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 547475456 176 ESMKMVKSRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVQ 214
Cdd:cd02042   92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 17-235 2.80e-31

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: 119.31  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   17 IIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKE-DLDH--CIYDALLND---VPAESLVLDT 90
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEfDVGEneTLYGAIRYDderRPISEIIRKT 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   91 NCKKVFVIPATIQLAGAEIELVSAIARE--------TRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQ 162
Cdd:TIGR03453 186 YFPGLDLVPGNLELMEFEHETPRALSRGqggdtiffARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLITVH 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547475456  163 CEYYALEGVTKLLESMKMVKSRLNK-----GLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLIPRTVKISEA 235
Cdd:TIGR03453 266 PQMLDVMSMSQFLLMTGDLLGVVREaggnlSYDFMRYLVTRYEPNDGPQAQMVAFLRSLFGDHVLTNPMLKSTAISDA 343
ParA_partition NF041546
ParA family partition ATPase;
17-261 1.87e-29

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 109.95  E-value: 1.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  17 IIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNStsgfgiekedldhciydallndvpaeslvLDTNckkvf 96
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA-----------------------------LDWA----- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  97 vipatiQLAGAEIEL-VSAIARETRLKDLLEPIQDeFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKLL 175
Cdd:NF041546  47 ------AAREDERPFpVVGLARPTLHRELPSLARD-YDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTV 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 176 EsmkMVKSR--LNKGLDTYGVLmtmydSR----TSLSNQVVEEVQSYfGDKAFKTLIPRTVKISEAPSFGEPVITYAPQN 249
Cdd:NF041546 120 D---LIKEAreYTPGLKAAFVL-----NRaiarTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG 190

                        250
                 ....*....|..
gi 547475456 250 KGAKAYMNLAKE 261
Cdd:NF041546 191 KAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 16-266 5.06e-24

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 96.07  E-value: 5.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGfgiekedldhciydallndvpaeslvldtnckkv 95
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW---------------------------------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  96 fvipatIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQ---CEYYALEGVT 172
Cdd:PHA02518  47 ------AEAREEGEPLIPVVRMGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQpspFDIWAAPDLV 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 173 KLLESMKMVKSRLNKGldtyGVLMTMYDSRTSLSNQvVEEVQSYFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQNKGA 252
Cdd:PHA02518 121 ELIKARQEVTDGLPKF----AFIISRAIKNTQLYRE-ARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAA 195

                        250
                 ....*....|....
gi 547475456 253 KAYMNLAKEVIKRA 266
Cdd:PHA02518 196 EEIIQLVKELFRGI 209
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 13-65 1.44e-04

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: 42.95  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 547475456  13 KDTRIIaIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIE 65
Cdd:NF041417 331 KDTRYL-FFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTE 382
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 11-82 1.56e-04

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: 42.56  E-value: 1.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547475456  11 SAKDTRIIaIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGiekEDLDHCIYDalLNDVP 82
Cdd:NF041417   8 RGEDTEFV-FFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG---QSIGHRVTS--IDDVE 73
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 15-265 5.48e-136

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: 383.44  E-value: 5.48e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDLDHCIYDALLNDVPAESLVLDTNCKK 94
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  95 VFVIPATIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKL 174
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 175 LESMKMVKSRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQNKGAKA 254
Cdd:COG1192  161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|.
gi 547475456 255 YMNLAKEVIKR 265
Cdd:COG1192  241 YRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 15-190 1.54e-86

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: 255.20  E-value: 1.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDLDHCIYDALLNDVPAESLVLDTNCKK 94
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   95 VFVIPATIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKL 174
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*.
gi 547475456  175 LESMKMVKSRLNKGLD 190
Cdd:pfam13614 161 LNTIKLVKKRLNPSLE 176
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 18-242 9.85e-59

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: 186.40  E-value: 9.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   18 IAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKED--LDHCIYDALLNDVPAESLVLDTNCK-- 93
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIapALQALAEGLKGRVNLDPILLKEKSDeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   94 KVFVIPATIQLAGAEIELVSaIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTK 173
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLG-PRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  174 LLESMKMVKSRLN-KGLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKtLIPRTVKISEAPSFGEPV 242
Cdd:pfam01656 160 LGGVIAALVGGYAlLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLG-VIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 16-214 7.14e-51

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: 162.71  E-value: 7.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFgiekedldhciydallndvpaeslvldtnckkv 95
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  96 fvipatiqlagaeielvsaiaretrlkdllepiqdeFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKLL 175
Cdd:cd02042   48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 547475456 176 ESMKMVKSRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVQ 214
Cdd:cd02042   92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 17-235 2.80e-31

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: 119.31  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   17 IIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKE-DLDH--CIYDALLND---VPAESLVLDT 90
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEfDVGEneTLYGAIRYDderRPISEIIRKT 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   91 NCKKVFVIPATIQLAGAEIELVSAIARE--------TRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQ 162
Cdd:TIGR03453 186 YFPGLDLVPGNLELMEFEHETPRALSRGqggdtiffARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLITVH 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547475456  163 CEYYALEGVTKLLESMKMVKSRLNK-----GLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLIPRTVKISEA 235
Cdd:TIGR03453 266 PQMLDVMSMSQFLLMTGDLLGVVREaggnlSYDFMRYLVTRYEPNDGPQAQMVAFLRSLFGDHVLTNPMLKSTAISDA 343
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 31-265 1.87e-30

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: 113.45  E-value: 1.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  31 TTAVNLAAALGEQGRKTLIVDFDPQ-GNSTSGFGIEKEdldHCIYDALLNDVPAESLVLDTNcKKVFVIPAtiqlaGAEI 109
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPK---ATLADVLAGEADLEDAIVQGP-GGLDVLPG-----GSGP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 110 ELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKLLESMkmvksRLNKGL 189
Cdd:COG0455   72 AELAELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLL-----RRRLGV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 190 DTYGVLMTMYDSRTS---LSNQVVEEVQSYFGDKA-FKTLIPRTVKISEAPSFGEPVITYAPQNKGAKAYMNLAKEVIKR 265
Cdd:COG0455  147 RRAGVVVNRVRSEAEardVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 16-262 3.42e-30

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: 113.07  E-value: 3.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDpqgnstsgFGIEKEDL-----DHCIYDalLNDVPA------E 84
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--------IGLRNLDLilgleNRIVYT--LVDVLEgecrleQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  85 SLVLDTNCKKVFVIPATIQLAGAEielvsaiARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCE 164
Cdd:cd02036   71 ALIKDKRWENLYLLPASQTRDKDA-------LTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 165 YYALEG---VTKLLESM-----KMVKSRLNKGLDTYGVLMTMYDSRTSLSNQVVeevqsyfgdkafkTLIPRTVKISEAP 236
Cdd:cd02036  144 ISSVRDadrVIGLLESKgivniGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLL-------------GVIPEDPEVIVAT 210

                        250       260
                 ....*....|....*....|....*.
gi 547475456 237 SFGEPVITYAPQNKGAKAYMNLAKEV 262
Cdd:cd02036  211 NRGEPLVLYKPNSLAAKAFENIARRL 236
ParA_partition NF041546
ParA family partition ATPase;
17-261 1.87e-29

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 109.95  E-value: 1.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  17 IIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNStsgfgiekedldhciydallndvpaeslvLDTNckkvf 96
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA-----------------------------LDWA----- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  97 vipatiQLAGAEIEL-VSAIARETRLKDLLEPIQDeFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEGVTKLL 175
Cdd:NF041546  47 ------AAREDERPFpVVGLARPTLHRELPSLARD-YDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTV 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 176 EsmkMVKSR--LNKGLDTYGVLmtmydSR----TSLSNQVVEEVQSYfGDKAFKTLIPRTVKISEAPSFGEPVITYAPQN 249
Cdd:NF041546 120 D---LIKEAreYTPGLKAAFVL-----NRaiarTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG 190

                        250
                 ....*....|..
gi 547475456 250 KGAKAYMNLAKE 261
Cdd:NF041546 191 KAAREIRALAKE 202
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 4-266 5.05e-26

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: 104.43  E-value: 5.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   4 RDVKRSKSAKDTRIIAIINQKGGVGKSTTAVNLAAALGEQ-GRKTLIVDFDPQ-GNSTSGFGIEKedlDHCIYDAL---- 77
Cdd:COG4963   91 ARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQfGDVALYLDLEP---RRGLADALrnpd 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  78 -LNDVPAESLVLDTNCkKVFVIPATIQLagAEIELVSAiareTRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADS 156
Cdd:COG4963  168 rLDETLLDRALTRHSS-GLSVLAAPADL--ERAEEVSP----EAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADE 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 157 VLIPIQCEYYALEGVTKLLESMKmvksRLNKGLDTYGVLMTMYDSRTSLSnqvVEEVQSYFGDKAFKTlIPRTVK-ISEA 235
Cdd:COG4963  241 VVLVTEPDLPSLRNAKRLLDLLR----ELGLPDDKVRLVLNRVPKRGEIS---AKDIEEALGLPVAAV-LPNDPKaVAEA 312

                        250       260       270
                 ....*....|....*....|....*....|.
gi 547475456 236 PSFGEPVITYAPQNKGAKAYMNLAKEVIKRA 266
Cdd:COG4963  313 ANQGRPLAEVAPKSPLAKAIRKLAARLTGRP 343
PHA02518 PHA02518
ParA-like protein; Provisional
 16-266 5.06e-24

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 96.07  E-value: 5.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGfgiekedldhciydallndvpaeslvldtnckkv 95
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW---------------------------------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  96 fvipatIQLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQ---CEYYALEGVT 172
Cdd:PHA02518  47 ------AEAREEGEPLIPVVRMGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQpspFDIWAAPDLV 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 173 KLLESMKMVKSRLNKGldtyGVLMTMYDSRTSLSNQvVEEVQSYFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQNKGA 252
Cdd:PHA02518 121 ELIKARQEVTDGLPKF----AFIISRAIKNTQLYRE-ARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAA 195

                        250
                 ....*....|....
gi 547475456 253 KAYMNLAKEVIKRA 266
Cdd:PHA02518 196 EEIIQLVKELFRGI 209
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-204 9.94e-23

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: 94.48  E-value: 9.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   3 FRDVKRSKSAKDTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSG-FGIEKEdldHCIYDALLNDV 81
Cdd:COG0489   80 LLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRmLGLENR---PGLSDVLAGEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  82 PAESLVLDTNCKKVFVIPatiqlAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPslGLLTINALTAA---DSVL 158
Cdd:COG0489  157 SLEDVIQPTEVEGLDVLP-----AGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPP--GLGVADATLLAslvDGVL 229

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 547475456 159 IPIQCEYYALEGVTKLLESMKMVKSRLnkgldtYGVLMTMYDSRTS 204
Cdd:COG0489  230 LVVRPGKTALDDVRKALEMLEKAGVPV------LGVVLNMVCPKGE 269
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-185 2.34e-21

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 88.40  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   3 FRDVKR----SKSAKDTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDP-QGNSTSGFGIEKEdldHCIYDAL 77
Cdd:cd05387    3 FRTLRTnllfAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNE---PGLSEVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  78 LNDVPAESLVLDTNCKKVFVIPatiqlAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINAL-TAADS 156
Cdd:cd05387   80 SGQASLEDVIQSTNIPNLDVLP-----AGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILaPLVDG 154

                        170       180
                 ....*....|....*....|....*....
gi 547475456 157 VLIPIQCEYYALEGVTKLLESMKMVKSRL 185
Cdd:cd05387  155 VLLVVRAGKTRRREVKEALERLEQAGAKV 183
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 6-235 2.35e-21

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 92.05  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   6 VKRSKSAKDTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKE-DL--DHCIYDALLNDV- 81
Cdd:PRK13869 112 VPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPEtDVgaNETLYAAIRYDDt 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  82 --PAESLVLDTNCKKVFVIPATIQLAGAEIELVSAIA----RE----TRLKDLLEPIQDEFDFIFIDCPPSLGLLTINAL 151
Cdd:PRK13869 192 rrPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALSdkgtRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGL 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 152 TAADSVLIPIQCEYYALEGVTKLL----ESMKMVK-SRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLI 226
Cdd:PRK13869 272 CAATSMVITVHPQMLDIASMSQFLlmtrDLLGVVKeAGGNLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPM 351


                 ....*....
gi 547475456 227 PRTVKISEA 235
Cdd:PRK13869 352 VKSAAVSDA 360
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 16-259 5.21e-20

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: 85.79  E-value: 5.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQ-GRKTLIVDFD-PQGNSTSGFGIEKedlDHCIYDALLNDVPAESLVLDTNCK 93
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDlPFGDLGLYLNLRP---DYDLADVIQNLDRLDRTLLDSAVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  94 K----VFVIPATiqlagAEIELVSAIaRETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALE 169
Cdd:cd03111   78 RhssgLSLLPAP-----QELEDLEAL-GAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 170 GVTKLLESMKmvksRLNKGLDTYGVLMTMYDSRTSLSNQVVEEVqsyFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQN 249
Cdd:cd03111  152 NARRLLDSLR----ELEGSSDRLRLVLNRYDKKSEISPKDIEEA---LGLEVFATLPNDYKAVSESANTGRPLVEVAPRS 224

                        250
                 ....*....|
gi 547475456 250 KGAKAYMNLA 259
Cdd:cd03111  225 ALVRALQDLA 234
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 16-263 7.87e-20

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: 85.85  E-value: 7.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDpqgnstsgFGIEKEDL-----DHCIYDALlnDV------PAE 84
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD--------IGLRNLDLllgleNRIVYTLV--DVvegecrLQQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   85 SLVLDTNCKKVFVIPAtiqlagAEIELVSAIAREtRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCE 164
Cdd:TIGR01968  72 ALIKDKRLKNLYLLPA------SQTRDKDAVTPE-QMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  165 YYAL---EGVTKLLEsmkmvksrlNKGLDTYGVLMTMYDSRTSLSNQV--VEEVQSYFGDKaFKTLIPRTVKISEAPSFG 239
Cdd:TIGR01968 145 VSAVrdaDRVIGLLE---------AKGIEKIHLIVNRLRPEMVKKGDMlsVDDVLEILSIP-LIGVIPEDEAIIVSTNKG 214

                         250       260
                  ....*....|....*....|....
gi 547475456  240 EPVITyAPQNKGAKAYMNLAKEVI 263
Cdd:TIGR01968 215 EPVVL-NDKSRAGKAFENIARRIL 237
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 17-259 1.27e-17

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: 79.70  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   17 IIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEkEDLDHCIYDALLNDVPAESLVLDTNCKKVF 96
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMD-WSVRDGWARALLNGADWAAAAYRSPDGVLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   97 VIPATIQLAGAEIELVSAIARETRlkdLLEPIQ-DEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCE---YYALegVT 172
Cdd:TIGR03371  82 LPYGDLSADEREAYQAHDAGWLAR---LLQQLDlAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADaacYATL--HQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  173 KLLESMKMVKSRlnkglDTYGVLMTMYDSRTSLSNQVVEEVQSYFGDKAFKTLIPRTVKISEAPSFGEPVITYAPQNKGA 252
Cdd:TIGR03371 157 LALALFAGSGPR-----DGPRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQAA 231


                  ....*..
gi 547475456  253 KAYMNLA 259
Cdd:TIGR03371 232 HDIRTLA 238
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 16-159 4.41e-16

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 74.91  E-value: 4.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFD-PQGNSTSGFGIEKEdldHCIYDALLNDVPAESLVLDTNcKK 94
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPK---KTLGDVLKGRVSLEDIIVEGP-EG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547475456  95 VFVIPATiqlAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLI 159
Cdd:cd02038   77 LDIIPGG---SGMEELANLDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 15-159 6.27e-16

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 75.09  E-value: 6.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDpqgnstsgFGIEKEDL-----DHCIYDALlnDV------PA 83
Cdd:COG2894    2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD--------IGLRNLDLvmgleNRIVYDLV--DViegecrLK 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547475456  84 ESLVLDTNCKKVFVIPAtiqlagAEIELVSAIAREtRLKDLLEPIQDEFDFIFIDCPPSL--GLLtiNALTAADSVLI 159
Cdd:COG2894   72 QALIKDKRFENLYLLPA------SQTRDKDALTPE-QMKKLVEELKEEFDYILIDSPAGIeqGFK--NAIAGADEAIV 140
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-229 2.25e-15

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 75.01  E-value: 2.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   4 RDVKRSKSAK----DTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVD-FDPQGNSTSGFG------IEKEDLDHC 72
Cdd:PRK13705  91 RDVFGTRLRRaedvFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGwvpdlhIHAEDTLLP 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  73 IYDALLNDvpAESLVLDTNCKKVFVIPATIQLAGAEIELVS-------AIARETRLKDLLEPIQDEFDFIFIDCPPSLGL 145
Cdd:PRK13705 171 FYLGEKDD--ATYAIKPTCWPGLDIIPSCLALHRIETELMGkfdegklPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGI 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 146 LTINALTAADSVLIPIQCEYYaleGVTKLLESMKMVKSrLNKGLDTYG------VLMTMYDSRT-SLSNQVVEEVQSYFG 218
Cdd:PRK13705 249 GTINVVCAADVLIVPTPAELF---DYTSALQFFDMLRD-LLKNVDLKGfepdvrILLTKYSNSNgSQSPWMEEQIRDAWG 324

                        250
                 ....*....|.
gi 547475456 219 DKAFKTLIPRT 229
Cdd:PRK13705 325 SMVLKNVVRET 335
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 13-212 1.14e-14

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 72.74  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  13 KDTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVD-FDPQGNSTSGFG------IEKEDLDHCIYDALLNDvpAES 85
Cdd:PHA02519 104 KNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGyvpdlhIHADDTLLPFYLGERDN--AEY 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  86 LVLDTNCKKVFVIPATIQLAGAEIELVSAIARET-------RLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVL 158
Cdd:PHA02519 182 AIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKlphpphlMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIV 261

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 547475456 159 IPIQCEYY----ALEGVTKLLESMKMVKsrLNKGLDTYGVLMTMYDSRTSLSNQVVEE 212
Cdd:PHA02519 262 VATPAELFdyvsVLQFFTMLLDLLATVD--LGGFEPVVRLLLTKYSLTVGNQSRWMEE 317
PRK10818 PRK10818
septum site-determining protein MinD;
16-257 1.89e-14

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 71.12  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFD-PQGNSTSGFGIEKE---DLDHCIY-DALLNdvpaESLVLDT 90
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRvvyDFVNVIQgDATLN----QALIKDK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  91 NCKKVFVIPATiqlagaEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTAADSVLIPIQCEYYALEG 170
Cdd:PRK10818  79 RTENLYILPAS------QTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 171 VTKLLESMKMVKSRLNKGLDTYG--VLMTMYD-SRTS----LSNQVVEEVQSYfgdkAFKTLIPRTVKISEAPSFGEPVI 243
Cdd:PRK10818 153 SDRILGILASKSRRAENGEEPIKehLLLTRYNpGRVSrgdmLSMEDVLEILRI----KLVGVIPEDQSVLRASNQGEPVI 228

                        250
                 ....*....|....
gi 547475456 244 TYAPQNKGaKAYMN 257
Cdd:PRK10818 229 LDIEADAG-KAYAD 241
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 11-194 1.09e-12

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: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   11 SAKDTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDLDHcIYDALLNDVPAESLVLDT 90
Cdd:TIGR01007  13 SGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITG-LTNFLSGTTDLSDAICDT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   91 NCKKVFVIPatiqlAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPsLGLLTINALTA--ADSVLIPIQCEYYAL 168
Cdd:TIGR01007  92 NIENLDVIT-----AGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPP-IGTVTDAAIIAraCDASILVTDAGKIKK 165

                         170       180       190
                  ....*....|....*....|....*....|....
gi 547475456  169 EGVTKLLESMKMVKSR-----LNK---GLDTYGV 194
Cdd:TIGR01007 166 REVKKAKEQLEQAGSNflgvvLNKvdiSVSKYGY 199
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 24-264 4.95e-12

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 64.41  E-value: 4.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEK--EDLDhciydaLLNDVPAESLVLDTNCKKVFVIPAT 101
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKipTVLD------VLREKGIDNLGLEDIIYEGFNGIYC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 102 IQLAGAEIELVSAIARETRLKDLLEPIqDEFDFIFID-----------C-----PPSLGLltinaltaADSVLIPIQCEY 165
Cdd:PRK13230  83 VESGGPEPGYGCAGRGVITAIDLLKKL-GVFEELGPDvviydilgdvvCggfamPLQKGL--------ADDVYIVTTCDP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 166 YALEGVTKLLESMKMVKSRLNKGLDtyGVLmtmYDSRTSLSN-QVVEEVQSYFGDKAFKTlIPRTVKISEAPSFGEPVIT 244
Cdd:PRK13230 154 MAIYAANNICKGIKRFAKRGKSALG--GII---YNGRSVIDApDIVEEFAKKIGTNVIGK-IPMSNIITEAEIYGKTVIE 227

                        250       260
                 ....*....|....*....|
gi 547475456 245 YAPQNKGAKAYMNLAKEVIK 264
Cdd:PRK13230 228 YAPDSEISNIFRELAEAIYE 247
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 16-161 3.46e-11

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


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 61.70  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDP-QGNSTSGFG-----IEKEDLDHCIYDALLNDVPAESLVLD 89
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFEnrsatADRTGLSLPTPEHLNLPDNDVAEVPD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547475456   90 tnckkvfviPATIQLAGAEiELVSAIARetrlkdllepiqdEFDFIFIDCPPSLGLLTINALTAADSVLIPI 161
Cdd:pfam09140  81 ---------GENIDDARLE-EAFADLEA-------------RCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 15-53 5.87e-11

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: 60.93  E-value: 5.87e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 547475456   15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFD 53
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
16-263 1.08e-10

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 60.54  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   16 RIIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTS----GFGIEKedldhcIYDALLNDVPAESLVLDTN 91
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRlllgGKLQPT------VLDTAREKGYVEDVEVEDV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   92 CKKVFVIPATIQLAGAEIE-------LVSAIaretrlkDLLEPI--QDEFDFIFIDCppsLGLLTINALTA------ADS 156
Cdd:pfam00142  74 VYKGYGGVKCVESGGPEPGvgcagrgVITAI-------NLLEELgaYDDLDFVLYDV---LGDVVCGGFAMpiregkAQE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  157 VLIPIQCEYYALEGVTKLLESMKmvKSRLNKGLDTYGVLMT--MYDSRTSLSNQVVEEVQSYFGDKafktlIPRTVKISE 234
Cdd:pfam00142 144 IYIVTSNEMMALYAANNIAKGIQ--KYAKSGGVRLGGIICNsrKVDDERELIDAFAEELGTQVLHF-----VPRDNIVRK 216

                         250       260
                  ....*....|....*....|....*....
gi 547475456  235 APSFGEPVITYAPQNKGAKAYMNLAKEVI 263
Cdd:pfam00142 217 AELRKQTVIEYAPDSEQAQEYRELARKIL 245
minD CHL00175
septum-site determining protein; Validated
 9-177 3.20e-10

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 59.01  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   9 SKSAKDTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDpqgnstsgFGIEKEDL-----DHCIYDALlnDVPA 83
Cdd:CHL00175   9 EKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD--------IGLRNLDLllgleNRVLYTAM--DVLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  84 ESLVLDTNCKKVFVIPATIQLAGAEIELVSAIAREtRLKDLLEPIQDE-FDFIFIDCPPSLGLLTINALTAADSVLIPIQ 162
Cdd:CHL00175  79 GECRLDQALIRDKRWKNLSLLAISKNRQRYNVTRK-NMNMLVDSLKNRgYDYILIDCPAGIDVGFINAIAPAQEAIVVTT 157

                        170
                 ....*....|....*...
gi 547475456 163 CEYYAL---EGVTKLLES 177
Cdd:CHL00175 158 PEITAIrdaDRVAGLLEA 175
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 16-265 7.16e-10

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: 58.15  E-value: 7.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  16 RIIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTsgFGIEKEDLDHCIYDALLNDVPAESLVL-DTNCKK 94
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDST--LLLTGGKVPPTIDEMLTEDGTAEELRReDLLFSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  95 VFVI--------PATIQLAGAEIELVSAIARETRLKDllepiqDEFDFIFIDCppsLGLLTINALTA------ADSVLIP 160
Cdd:cd02117   78 FNGVdcveaggpEPGVGCGGRGIGTMLELLEEHGLLD------DDYDVVIFDV---LGDVVCGGFAAplrrgfAQKVVIV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 161 IQCEYYALEGVTKLLesmKMVKSRLNKGLDTYGVLMTMYDSRTslsnqvVEEVQSYFGDKAFKTL--IPRTVKISEAPSF 238
Cdd:cd02117  149 VSEELMSLYAANNIV---KAVENYSKNGVRLAGLVANLRDPAG------TEEIQAFAAAVGTKILavIPRDPAVRRAELA 219

                        250       260
                 ....*....|....*....|....*..
gi 547475456 239 GEPVITYAPQNKGAKAYMNLAKEVIKR 265
Cdd:cd02117  220 RVTVFEHDPVSPAASEFARLAAKIADA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 16-53 7.80e-10

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: 57.13  E-value: 7.80e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFD 53
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 16-59 1.51e-09

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: 57.14  E-value: 1.51e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 547475456  16 RIIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNST 59
Cdd:cd02040    1 RQIAIYG-KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
17-58 1.54e-09

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 57.75  E-value: 1.54e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 547475456  17 IIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNS 58
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPS 150
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 16-53 1.94e-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: 51.28  E-value: 1.94e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 547475456  16 RIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFD 53
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 14-203 3.54e-08

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: 53.96  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   14 DTRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFD-PQGNSTSGFGiekEDLDHCIYDALLNDVPAESLVLDTNC 92
Cdd:TIGR01005 552 ENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFG---KAPKPGLLDLLAGEASIEAGIHRDQR 628

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   93 KKVFVIPATiqLAGAEIELVSAIARETRLKDLLEPIQDEFDFIFIDCPPSLGLLTINALTA-ADSVLIPIQCEYYALEGV 171
Cdd:TIGR01005 629 PGLAFIAAG--GASHFPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAAlADGILFVTEFERSPLGEI 706

                         170       180       190
                  ....*....|....*....|....*....|..
gi 547475456  172 TKLLESMKMVKSrlnkglDTYGVLMTMYDSRT 203
Cdd:TIGR01005 707 RDLIHQEPHANS------DVLGVIFNALDMNE 732
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 24-54 1.55e-07

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


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 50.97  E-value: 1.55e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 547475456  24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDP 54
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 9-60 4.66e-07

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: 50.22  E-value: 4.66e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 547475456   9 SKSAKDTRIIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTS 60
Cdd:cd02033   25 GPPTKETQIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTS 75
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
13-54 8.86e-07

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 49.05  E-value: 8.86e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 547475456  13 KDTRIIaIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDP 54
Cdd:COG0003    1 DMTRII-FFTGKGGVGKTTVAAATALALAERGKRTLLVSTDP 41
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 17-59 2.42e-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: 47.68  E-value: 2.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 547475456  17 IIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNST 59
Cdd:cd02032    2 VIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 15-59 2.43e-06

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 47.65  E-value: 2.43e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 547475456  15 TRIIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNST 59
Cdd:PRK13185   2 ALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 24-65 8.39e-06

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: 46.62  E-value: 8.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 547475456   24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIE 65
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQT 52
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 18-262 9.83e-06

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 45.94  E-value: 9.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  18 IAIINqKGGVGKSTTAVNLAAALGEQGRkTLIVDFDPQGNSTSGFGIEKEDldhCIYDALL-NDVPAESLVLDTNCKKVF 96
Cdd:PRK13231   5 IAIYG-KGGIGKSTTVSNMAAAYSNDHR-VLVIGCDPKADTTRTLCGKRIP---TVLDTLKdNRKPELEDIIHEGFNGIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  97 VIPATIQLAGAEIELVSAIARETRLkDLLEPIQDEFDFIFIDCppsLGLLTINALTA------ADSVLIPIQCEYYALEG 170
Cdd:PRK13231  80 CVESGGPEPGVGCAGRGVIVAMNLL-ENLGVFDEDIDVVIYDV---LGDVVCGGFSVplredyADEVYIVTSGEYMSLYA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456 171 VTKLLESMKMVKSRLNkgldtyGVLMTMYDSRTSLsnQVVEEVQSYFGDKAFKTlIPRTVKISEAPSFGEPVITYAPQNK 250
Cdd:PRK13231 156 ANNIARGIKKLKGKLG------GIICNCRGIDNEV--EIVSEFASRIGSRIIGV-IPRSNLVQESELDAKTVVETFPESE 226

                        250
                 ....*....|..
gi 547475456 251 GAKAYMNLAKEV 262
Cdd:PRK13231 227 QASVYRKLANNI 238
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 15-161 1.38e-05

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


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 44.84  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  15 TRIIAIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIE-KEDLDHCIY-----DALLNDVpAESLVL 88
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASgRYLMSDHLYtlksrKANLADK-LESCVK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547475456  89 DTNCKKVFVIPATIQLAGAEIELVSAIARETRLKDLlepiqDEFDFIFIDCPPSLGLLTINALTAADSVLIPI 161
Cdd:cd17869   82 QHESGVYYFSPFKSALDILEIKKDDILHMITKLVEA-----HAYDYIIMDLSFEFSSTVCKLLQASHNNVVIA 149
chlL CHL00072
photochlorophyllide reductase subunit L
 24-64 2.42e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 44.73  E-value: 2.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 547475456  24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNST---SGFGI 64
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTftlTGFLI 51
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 24-57 3.30e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 44.00  E-value: 3.30e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 547475456  24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGN 57
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 15-146 6.03e-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: 43.49  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   15 TRIIaIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIE--------KE-------DLDHCIYDALLN 79
Cdd:pfam02374   1 MRWI-FFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKfgheptkvKEnlsameiDPNMELEEYWQE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456   80 DVPAESLVLDTNCKKVFVIPATIQLAGaeIELVSAIARETRLKDllepiQDEFDFIFIDCPP---SLGLL 146
Cdd:pfam02374  80 VQKYMNALLGLRMLEGILAEELASLPG--IDEAASFDEFKKYMD-----EGEYDVVVFDTAPtghTLRLL 142
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 13-65 1.44e-04

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: 42.95  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 547475456  13 KDTRIIaIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIE 65
Cdd:NF041417 331 KDTRYL-FFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTE 382
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 16-69 1.53e-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: 41.91  E-value: 1.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 547475456  16 RIIAIINqKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGIEKEDL 69
Cdd:cd02034    1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKL 53
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 11-82 1.56e-04

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: 42.56  E-value: 1.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547475456  11 SAKDTRIIaIINQKGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGFGiekEDLDHCIYDalLNDVP 82
Cdd:NF041417   8 RGEDTEFV-FFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG---QSIGHRVTS--IDDVE 73
nifH PRK13233
nitrogenase iron protein;
15-59 2.34e-04

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 41.73  E-value: 2.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 547475456  15 TRIIAIINqKGGVGKSTTAVNLAAALGE-QGRKTLIVDFDPQGNST 59
Cdd:PRK13233   2 TRKIAIYG-KGGIGKSTTTQNTAAAMAYfHDKKVFIHGCDPKADST 46
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 24-62 3.87e-04

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 40.01  E-value: 3.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 547475456  24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDPQGNSTSGF 62
Cdd:cd05386    9 KGGVGKSVIASLLAQYLIDKGQPVSCIDTDPVNKTFAGY 47
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 24-54 5.46e-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: 37.76  E-value: 5.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547475456   24 KGGVGKSTTAVNLAAALGEQGRKTLIVDFDP 54
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP 359
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 17-159 6.42e-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: 36.98  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  17 IIAIINQKGGVGKSTTAVNLAAALgeqgRKTLIVDFD-----------PQGNSTSGF-GIEKEDLDH------------C 72
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDvdapnlhlllgPEPEEEEDFvGGKKAFIDQekcircgncervC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547475456  73 IYDALLNDvPAESLVLDTNC-------------------KKVFVIPATIQLAGAEIELVSAIARE------TRLKDLLEP 127
Cdd:cd03110   77 KFGAILEF-FQKLIVDESLCegcgacviicprgaiylkdRDTGKIFISSSDGGPLVHGRLNIGEEnsgklvTELRKKALE 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 547475456 128 IQDEFDFIFIDCPPSLGLLTINALTAADSVLI 159
Cdd:cd03110  156 RSKECDLAIIDGPPGTGCPVVASITGADAVLL 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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