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Conserved domains on  [gi|501038728|ref|WP_012090674|]
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MULTISPECIES: ParA family protein [Shewanella]

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 7.09e-131

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: 370.34  E-value: 7.09e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKYEVENTAYELLVEEKSFDEIVIKNTAGKY 82
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 DLIASNGDVTAAEIKLMEFFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:COG1192   82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 163 DTITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLKQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:COG1192  162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                        250
                 ....*....|
gi 501038728 243 LALAGEMIRR 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 7.09e-131

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: 370.34  E-value: 7.09e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKYEVENTAYELLVEEKSFDEIVIKNTAGKY 82
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 DLIASNGDVTAAEIKLMEFFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:COG1192   82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 163 DTITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLKQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:COG1192  162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                        250
                 ....*....|
gi 501038728 243 LALAGEMIRR 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 9.26e-85

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: 250.58  E-value: 9.26e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    2 GKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKYEVENTAYELLVEEKSFDEIVIKNTAGK 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   82 YDLIASNGDVTAAEIKLMEFFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTAL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 501038728  162 IDTITKLAAMVNPGLGI 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 2.01e-50

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: 161.55  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSgvdkyeventayellveeksfdeivikntagky 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 dliasngdvtaaeiklmeffareirlrnalapikdqYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:cd02042   48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 501038728 163 DTITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLK 201
Cdd:cd02042   92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-219 1.01e-31

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 118.32  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   1 MGKVIAVANQKGGVGKTTTCVNLAASLAAT-KRKVLLIDLDPQGNAT--MGSGVDKYEVENTaYELLVEEKSFdEIVIKN 77
Cdd:NF041283   1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATqfLSKTFNVPNFPQS-FMKCVEDGDL-EKGIVH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  78 TAGKYDLIASNGDvtaaEIKLMEFFA--------REIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQ 149
Cdd:NF041283  79 LTPNLDLIAGDYD----TRELGDFLAdkfkseydRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501038728 150 CEYYALEGLTALIDT-----ITKLAAMVNpgLGIEGILRTMYDPRNRLSNDVSDQLKQHFG-DKVYRTVIPRNVRL 219
Cdd:NF041283 155 TQQFAFEGSKKLILTylqtlVDDFGDEIN--VQVAGILPVLLQARRPLQQKIVDETIEYFGkDNVFNNIIKNHARL 228
ParA_partition NF041546
ParA family partition ATPase;
4-248 7.95e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 110.72  E-value: 7.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATmgsgvdkyevenTAYELLVEEKSFDEIVIkntagkyd 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL------------DWAAAREDERPFPVVGL-------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  84 liasngdvtaaeiklmeffAREiRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALID 163
Cdd:NF041546  61 -------------------ARP-TLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 164 TItKLAAMVNPGLGIEGIL-RTmyDPRNRLSNDVSDQLKQhFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:NF041546 121 LI-KEAREYTPGLKAAFVLnRA--IARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREI 196


                 ....*.
gi 501038728 243 LALAGE 248
Cdd:NF041546 197 RALAKE 202
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-147 1.26e-24

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: 100.82  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGV----DKYEVEnTAYELL---VEEKSFDEIVIK 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpefDVGENE-TLYGAIrydDERRPISEIIRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   77 NTAGKYDLIASNgdvtaaeIKLMEF---FAREI------------RLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAA 141
Cdd:TIGR03453 185 TYFPGLDLVPGN-------LELMEFeheTPRALsrgqggdtiffaRVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAA 257


                  ....*.
gi 501038728  142 DSVLVP 147
Cdd:TIGR03453 258 TGVLIT 263
PHA02518 PHA02518
ParA-like protein; Provisional
 3-253 1.95e-21

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 89.14  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSgvdkyeventayellvEEKSFDEIVIKntagky 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWA----------------EAREEGEPLIP------ 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 dLIASNGDVTAaeiklmeffareirlrnALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:PHA02518  59 -VVRMGKSIRA-----------------DLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 163 DtITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLkQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:PHA02518 121 E-LIKARQEVTDGLPKFAFIISRAIKNTQLYREARKAL-AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198

                        250
                 ....*....|.
gi 501038728 243 LALAGEMIRRS 253
Cdd:PHA02518 199 IQLVKELFRGI 209
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-252 7.09e-131

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: 370.34  E-value: 7.09e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKYEVENTAYELLVEEKSFDEIVIKNTAGKY 82
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 DLIASNGDVTAAEIKLMEFFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:COG1192   82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 163 DTITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLKQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:COG1192  162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                        250
                 ....*....|
gi 501038728 243 LALAGEMIRR 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 9.26e-85

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: 250.58  E-value: 9.26e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    2 GKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKYEVENTAYELLVEEKSFDEIVIKNTAGK 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   82 YDLIASNGDVTAAEIKLMEFFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTAL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 501038728  162 IDTITKLAAMVNPGLGI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-228 6.18e-60

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: 189.48  E-value: 6.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    5 IAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATM--GSGVDKYEVENTAYELLVEEKSFDEIVIKN--TAG 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSveGLEGDIAPALQALAEGLKGRVNLDPILLKEksDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   81 KYDLIASNGDVTAAEIKLMEFFAREiRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTA 160
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEE-RLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501038728  161 LIDTITKLAAMVNP-GLGIEGILRTMYDPRNRLSNDVSDQLKQHFGDKVYrTVIPRNVRLAEAPSFGAP 228
Cdd:pfam01656 160 LGGVIAALVGGYALlGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVL-GVIPRDEAVAEAPARGLP 227
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 2.01e-50

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: 161.55  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSgvdkyeventayellveeksfdeivikntagky 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 dliasngdvtaaeiklmeffareirlrnalapikdqYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:cd02042   48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 501038728 163 DTITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLK 201
Cdd:cd02042   92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-219 1.01e-31

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 118.32  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   1 MGKVIAVANQKGGVGKTTTCVNLAASLAAT-KRKVLLIDLDPQGNAT--MGSGVDKYEVENTaYELLVEEKSFdEIVIKN 77
Cdd:NF041283   1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATqfLSKTFNVPNFPQS-FMKCVEDGDL-EKGIVH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  78 TAGKYDLIASNGDvtaaEIKLMEFFA--------REIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQ 149
Cdd:NF041283  79 LTPNLDLIAGDYD----TRELGDFLAdkfkseydRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501038728 150 CEYYALEGLTALIDT-----ITKLAAMVNpgLGIEGILRTMYDPRNRLSNDVSDQLKQHFG-DKVYRTVIPRNVRL 219
Cdd:NF041283 155 TQQFAFEGSKKLILTylqtlVDDFGDEIN--VQVAGILPVLLQARRPLQQKIVDETIEYFGkDNVFNNIIKNHARL 228
ParA_partition NF041546
ParA family partition ATPase;
4-248 7.95e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 110.72  E-value: 7.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATmgsgvdkyevenTAYELLVEEKSFDEIVIkntagkyd 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL------------DWAAAREDERPFPVVGL-------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  84 liasngdvtaaeiklmeffAREiRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALID 163
Cdd:NF041546  61 -------------------ARP-TLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 164 TItKLAAMVNPGLGIEGIL-RTmyDPRNRLSNDVSDQLKQhFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:NF041546 121 LI-KEAREYTPGLKAAFVLnRA--IARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREI 196


                 ....*.
gi 501038728 243 LALAGE 248
Cdd:NF041546 197 RALAKE 202
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-256 1.92e-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: 105.36  E-value: 1.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  18 TTCVNLAASLAATKRKVLLIDLDPqGNATMGSGVDKyEVENTAYELLVEEKSFDEIVIKNTAGkYDLIASNGDVTAaeik 97
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADL-GLANLDVLLGL-EPKATLADVLAGEADLEDAIVQGPGG-LDVLPGGSGPAE---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  98 lMEFFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALIdtitKLAAMVNPGLG 177
Cdd:COG0455   74 -LAELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALL----KLLRRRLGVRR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 178 IeGILRTMYDPRN---RLSNDVSDQLKQHFGDKV-YRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAYLALAGEMIRRS 253
Cdd:COG0455  149 A-GVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWP 227


                 ...
gi 501038728 254 EQQ 256
Cdd:COG0455  228 VPE 230
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-260 4.43e-25

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: 101.73  E-value: 4.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   2 GKVIAVANQKGGVGKTTTCVNLAASLAA-TKRKVLLIDLDPQ-GNATMGSGVDKyevENTAYELLVEEKSFDEIVIKNTA 79
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQfGDVALYLDLEP---RRGLADALRNPDRLDETLLDRAL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  80 GKY----DLIASNGDVTAAEIKLMEFFAREIRLrnalapIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYAL 155
Cdd:COG4963  179 TRHssglSVLAAPADLERAEEVSPEAVERLLDL------LRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSL 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 156 EGLTALIDTitkLAAMVNPGLGIEGILRtMYDPRNRLSndvSDQLKQHFGDKVYrTVIPRNVR-LAEAPSFGAPAMYYDK 234
Cdd:COG4963  253 RNAKRLLDL---LRELGLPDDKVRLVLN-RVPKRGEIS---AKDIEEALGLPVA-AVLPNDPKaVAEAANQGRPLAEVAP 324

                        250       260
                 ....*....|....*....|....*.
gi 501038728 235 SSAGAKAYLALAGEMIRRSEQQTQAK 260
Cdd:COG4963  325 KSPLAKAIRKLAARLTGRPAAAAAKA 350
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-147 1.26e-24

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: 100.82  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGV----DKYEVEnTAYELL---VEEKSFDEIVIK 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpefDVGENE-TLYGAIrydDERRPISEIIRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   77 NTAGKYDLIASNgdvtaaeIKLMEF---FAREI------------RLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAA 141
Cdd:TIGR03453 185 TYFPGLDLVPGN-------LELMEFeheTPRALsrgqggdtiffaRVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAA 257


                  ....*.
gi 501038728  142 DSVLVP 147
Cdd:TIGR03453 258 TGVLIT 263
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-250 1.64e-23

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: 95.57  E-value: 1.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD-PQGNATMGSGVDKYEVenTAYELLVEEKSFDEIVIKNTAGK 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPV--TLHDVLAGEADIKDAIYEGPFGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   82 YdliasngdVTAAEIKLMEFF-AREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEyyalegLTA 160
Cdd:TIGR01969  79 K--------VIPAGVSLEGLRkADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE------ISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  161 LIDTITKLAAMVNPGLGIEGILRTMYdprNRLSNDVSDQLKQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAK 240
Cdd:TIGR01969 145 ITDALKTKIVAEKLGTAILGVVLNRV---TRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQ 221

                         250
                  ....*....|
gi 501038728  241 AYLALAGEMI 250
Cdd:TIGR01969 222 AFMELAAELA 231
PHA02518 PHA02518
ParA-like protein; Provisional
 3-253 1.95e-21

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 89.14  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSgvdkyeventayellvEEKSFDEIVIKntagky 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWA----------------EAREEGEPLIP------ 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  83 dLIASNGDVTAaeiklmeffareirlrnALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALEGLTALI 162
Cdd:PHA02518  59 -VVRMGKSIRA-----------------DLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 163 DtITKLAAMVNPGLGIEGILRTMYDPRNRLSNDVSDQLkQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAGAKAY 242
Cdd:PHA02518 121 E-LIKARQEVTDGLPKFAFIISRAIKNTQLYREARKAL-AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198

                        250
                 ....*....|.
gi 501038728 243 LALAGEMIRRS 253
Cdd:PHA02518 199 IQLVKELFRGI 209
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-246 4.80e-20

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: 85.72  E-value: 4.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD-PQGNATMGSGVDKyEVENTAYELLVEEKSFDEIVI--KNTA 79
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLEN-RIVYTLVDVLEGECRLEQALIkdKRWE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  80 GKYDLIAS-NGDVTAAEIKLMEFFAREirlrnalapIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEyyalegL 158
Cdd:cd02036   80 NLYLLPASqTRDKDALTPEKLEELVKE---------LKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPE------I 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 159 TALIDT---ITKLAAMvnpGLGIEGILRTMYDP-RNRLSNDVS-DQLKQHFGDKVYrTVIPRNVRLAEAPSFGAPAMYYD 233
Cdd:cd02036  145 SSVRDAdrvIGLLESK---GIVNIGLIVNRYRPeMVKSGDMLSvEDIQEILGIPLL-GVIPEDPEVIVATNRGEPLVLYK 220

                        250
                 ....*....|...
gi 501038728 234 KSSAGAKAYLALA 246
Cdd:cd02036  221 PNSLAAKAFENIA 233
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-146 6.49e-20

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: 85.31  E-value: 6.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDpqgnatMG-SGVD-------KYevenTAYELLVEEKSFDEIV 74
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD------LGlANLDillglapKK----TLGDVLKGRVSLEDII 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501038728  75 IKNTAGKYDLIASNGDVTAAEIKlmefFAREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLV 146
Cdd:cd02038   71 VEGPEGLDIIPGGSGMEELANLD----PEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-222 1.21e-19

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 87.42  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKyEVENTAYELLVEEKSFDEI------VIK 76
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLP-ETDVGANETLYAAIRYDDTrrplrdVIR 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  77 NTAgkYDLIasngDVTAAEIKLMEF-----------FARE----IRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAA 141
Cdd:PRK13869 201 PTY--FDGL----HLVPGNLELMEFehttpkalsdkGTRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 142 DSVLVPMQCEYYALEGLTALIDTITKLAAMVNPGLG------IEGILrTMYDPRNRLSNDVSDQLKQHFGDKVYRTVIPR 215
Cdd:PRK13869 275 TSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGnlqydfIRYLL-TRYEPQDAPQTKVAALLRNMFEDHVLTNPMVK 353


                 ....*..
gi 501038728 216 NVRLAEA 222
Cdd:PRK13869 354 SAAVSDA 360
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-213 7.59e-19

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 84.68  E-value: 7.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLID-LDPQGNATMGSG-VDKYEV--ENTAYELLVEEKSFDEIVIKNTA 79
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGyVPDLHIhaDDTLLPFYLGERDNAEYAIKPTC 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  80 -GKYDLIASNGDVTAAEIKLMEFFARE-------IRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCE 151
Cdd:PHA02519 188 wPGLDIIPSCLALHRIETDLMQYHDAGklphpphLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAE 267

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 152 YY----ALEGLTALIDtitkLAAMVNPGlGIEGILR---TMYDPRN-RLSNDVSDQLKQHFGDKVYRTVI 213
Cdd:PHA02519 268 LFdyvsVLQFFTMLLD----LLATVDLG-GFEPVVRlllTKYSLTVgNQSRWMEEQIRNTWGSMVLRQVV 332
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 4-146 5.54e-18

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: 81.39  E-value: 5.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQgnatmGSGVDKY-EVENTA--YELLVEEKSFDEIVIKNTAG 80
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLR-----GPSLHRMlGLENRPglSDVLAGEASLEDVIQPTEVE 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501038728  81 KYDLIASNGDVTAAeiklMEFFAREiRLRNALAPIKDQYDYIFIDCPPSLNM--LTVnAMSAADSVLV 146
Cdd:COG0489  169 GLDVLPAGPLPPNP----SELLASK-RLKQLLEELRGRYDYVIIDTPPGLGVadATL-LASLVDGVLL 230
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-247 6.41e-18

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: 80.47  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMGSGVDKYEVENTAYELLVEEkSFDEIVIKNTAGkY 82
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALLNGA-DWAAAAYRSPDG-V 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   83 DLIASnGDVTAAEikLMEFFAREIR-LRNALAPIK-DQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQC--EYYALegL 158
Cdd:TIGR03371  80 LFLPY-GDLSADE--REAYQAHDAGwLARLLQQLDlAARDWVLIDLPRGPSPITRQALAAADLVLVVVNAdaACYAT--L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  159 TALIDtitKLAAMVNPGLGIeGILRTMYDPRNRLSNDVSDQLKQHFGDKVYRTVIPRNVRLAEAPSFGAPAMYYDKSSAG 238
Cdd:TIGR03371 155 HQLAL---ALFAGSGPRDGP-RFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQA 230


                  ....*....
gi 501038728  239 AKAYLALAG 247
Cdd:TIGR03371 231 AHDIRTLAG 239
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-213 7.91e-18

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 81.95  E-value: 7.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLID-LDPQGNATMGSG-VDKYEV--ENTAYELLVEEKSFDEIVIKNTA 79
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGwVPDLHIhaEDTLLPFYLGEKDDATYAIKPTC 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  80 -GKYDLIASNGDVTAAEIKLMEFF-------AREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCE 151
Cdd:PRK13705 188 wPGLDIIPSCLALHRIETELMGKFdegklptDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 267

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501038728 152 YY----ALEGLTALIDTitklaaMVNPGL-GIEGILRTMYdprNRLSNDV-------SDQLKQHFGDKVYRTVI 213
Cdd:PRK13705 268 LFdytsALQFFDMLRDL------LKNVDLkGFEPDVRILL---TKYSNSNgsqspwmEEQIRDAWGSMVLKNVV 332
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-168 1.00e-15

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: 74.24  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAA-TKRKVLLIDLD-PQGNATMgsgvdkYEVENTAYELLVEEKSFDEI------- 73
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDlPFGDLGL------YLNLRPDYDLADVIQNLDRLdrtllds 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  74 VIKNTAGKYDLIASNGDVTAAEIKlmeffaREIRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYY 153
Cdd:cd03111   75 AVTRHSSGLSLLPAPQELEDLEAL------GAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLP 148

                        170
                 ....*....|....*
gi 501038728 154 ALEGLTALIDTITKL 168
Cdd:cd03111  149 SLRNARRLLDSLREL 163
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-146 1.09e-15

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 74.32  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   1 MGKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLID-------LDpqgnATMGsgvdkyeVENtayellveeksfdEI 73
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDadiglrnLD----LVMG-------LEN-------------RI 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  74 VikntagkYDLIasngDVTAAEIKLMEFFAREIRLRN-------------ALAP---------IKDQYDYIFIDCPPSLN 131
Cdd:COG2894   57 V-------YDLV----DVIEGECRLKQALIKDKRFENlyllpasqtrdkdALTPeqmkklveeLKEEFDYILIDSPAGIE 125

                        170
                 ....*....|....*
gi 501038728 132 MLTVNAMSAADSVLV 146
Cdd:COG2894  126 QGFKNAIAGADEAIV 140
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-146 1.96e-15

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: 72.22  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD---PQGNATMGSgvdkyEVENTAYELLVEEKSFDEIVIKNTA 79
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGL-----PNEPGLSEVLSGQASLEDVIQSTNI 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501038728  80 GKYDLIASNGDVTAAeiklMEFFAREiRLRNALAPIKDQYDYIFIDCPPSLNMLTVNA-MSAADSVLV 146
Cdd:cd05387   95 PNLDVLPAGTVPPNP----SELLSSP-RFAELLEELKEQYDYVIIDTPPVLAVADALIlAPLVDGVLL 157
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-246 4.51e-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: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    2 GKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDpQG--NATMGSGVDKyEVENTAYELLVEEKSFDEIVIKNTA 79
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-IGlrNLDLLLGLEN-RIVYTLVDVVEGECRLQQALIKDKR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   80 GK--YDLIAS-NGDVTAAEIKLMEFFAREirlrnalapIKDQYDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEyyale 156
Cdd:TIGR01968  79 LKnlYLLPASqTRDKDAVTPEQMKKLVNE---------LKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPE----- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  157 gLTALIDTITKLAAMVNPGLGIEGILRTMYDPRNRLSNDV--SDQLKQHFGDKVYrTVIPRNVRLAEAPSFGAPAMYYDK 234
Cdd:TIGR01968 145 -VSAVRDADRVIGLLEAKGIEKIHLIVNRLRPEMVKKGDMlsVDDVLEILSIPLI-GVIPEDEAIIVSTNKGEPVVLNDK 222

                         250
                  ....*....|..
gi 501038728  235 SSAGaKAYLALA 246
Cdd:TIGR01968 223 SRAG-KAFENIA 233
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-148 3.85e-12

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: 64.40  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQgNATMGsgvdKYeVENTA-----YELLVEEKSFDEIVIKNT 78
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFH----RY-FENRSatadrTGLSLPTPEHLNLPDNDV 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   79 AGKYDliasngDVTAAEIKLMEFFAREIRlrnalapikdQYDYIFIDCPPSLNMLTVNAMSAADSVLVPM 148
Cdd:pfam09140  76 AEVPD------GENIDDARLEEAFADLEA----------RCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
minD CHL00175
septum-site determining protein; Validated
 1-146 2.93e-11

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 62.10  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   1 MGKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD-PQGNATMGSGVDKyEVENTAYELLVEEKSFDEIVIKNTA 79
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLEN-RVLYTAMDVLEGECRLDQALIRDKR 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501038728  80 GKyDL----IASNGDVTAAEIKLMEFFAREIRLRNalapikdqYDYIFIDCPPSLNMLTVNAMSAADSVLV 146
Cdd:CHL00175  93 WK-NLsllaISKNRQRYNVTRKNMNMLVDSLKNRG--------YDYILIDCPAGIDVGFINAIAPAQEAIV 154
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-146 1.51e-09

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: 56.29  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQgNATMgSGVDKYEVENTAY-ELLVEEKSFDEIVIKNTAGK 81
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMR-NSVM-SGTFKSQNKITGLtNFLSGTTDLSDAICDTNIEN 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501038728   82 YDLIASnGDVTAAEIKLMEffarEIRLRNALAPIKDQYDYIFIDCPPsLNMLT---VNAMSAADSVLV 146
Cdd:TIGR01007  96 LDVITA-GPVPPNPTELLQ----SSNFKTLIETLRKRFDYIIIDTPP-IGTVTdaaIIARACDASILV 157
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 2.01e-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: 55.97  E-value: 2.01e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD 40
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-40 3.55e-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: 55.54  E-value: 3.55e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 501038728    3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD 40
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-125 9.70e-09

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: 54.68  E-value: 9.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT---MGSGVDKYEVENTAYELLVEEKSFDEIViKNTAGKYDLIAS 87
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTlllTGGKVPPTIDEMLTEDGTAEELRREDLL-FSGFNGVDCVEA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501038728  88 NGD---------VTAAEIKLMEFFAREirlrnalapiKDQYDYIFID 125
Cdd:cd02117   87 GGPepgvgcggrGIGTMLELLEEHGLL----------DDDYDVVIFD 123
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 3-145 1.08e-07

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


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 52.41  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728    3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD-PQGNATMGSGVDKyevENTAYELLVEEKSFDEIVIKNTAGK 81
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFGKAP---KPGLLDLLAGEASIEAGIHRDQRPG 630

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501038728   82 YDLIASnGDVTAAEIKLMEFFAREiRLRNALAPIKDQYDYIFIDCPPSLNMLTVNAMSA-ADSVL 145
Cdd:TIGR01005 631 LAFIAA-GGASHFPHNPNELLANP-AMAELIDNARNAFDLVLVDLAALAAVADAAAFAAlADGIL 693
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 1.27e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 48.97  E-value: 1.27e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501038728   3 KVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD 40
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 3-44 4.46e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 49.39  E-value: 4.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 501038728   3 KVIAVANqKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGN 44
Cdd:COG3640    1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-246 1.04e-06

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 48.61  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNATMG-SGVDKYEVENTAYELLVEEKSFDEIVIKNTAGKYDL----- 84
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNlVGEKIPTVLDVLREKGIDNLGLEDIIYEGFNGIYCVesggp 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  85 -----IASNGDVTAAEI-KLMEFFareirlrNALAPIKDQYDyIFID--CPPSLNMLTvnaMSAADSVLVPMQCEYYALE 156
Cdd:PRK13230  89 epgygCAGRGVITAIDLlKKLGVF-------EELGPDVVIYD-ILGDvvCGGFAMPLQ---KGLADDVYIVTTCDPMAIY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 157 GLTALIDTITKLAAMVNPGLGieGILrtmYDPRNRLSN-DVSDQLKQHFGDKVYRTvIPRNVRLAEAPSFGAPAMYYDKS 235
Cdd:PRK13230 158 AANNICKGIKRFAKRGKSALG--GII---YNGRSVIDApDIVEEFAKKIGTNVIGK-IPMSNIITEAEIYGKTVIEYAPD 231

                        250
                 ....*....|.
gi 501038728 236 SAGAKAYLALA 246
Cdd:PRK13230 232 SEISNIFRELA 242
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-46 1.05e-06

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 48.81  E-value: 1.05e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 501038728   1 MGKVIAVANqKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT 46
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-40 1.16e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 48.89  E-value: 1.16e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 501038728   4 VIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD 40
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
GPN cd17868
GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small ...
 13-127 1.47e-06

GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small GTPases, Gpn1, 2, and 3. They form heterodimers, interact with RNA polymerase II and may function in nuclear import of RNA polymerase II.


Pssm-ID: 349777 [Multi-domain]  Cd Length: 198  Bit Score: 47.70  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  13 GVGKTTTCVNLAASLAATKRKVLLIDLDPqGNatmgsgvdkyevENTAYELLVEEKSFdeIVIKNTAGKYDLiasnGDVT 92
Cdd:cd17868   10 GSGKTTFCKNMKEHLRARKRNPYVINLDP-GN------------INEPLDYDIDIRDL--IKYDDIMEELDL----GPNG 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501038728  93 AAEIKLMEFFAREIRLRNALAPIKDQYDYIFIDCP 127
Cdd:cd17868   71 SIVYSLEYFEKNFDWFEKKLENEDKNPHYILFDCP 105
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-134 2.85e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 47.51  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGN------ATMGSGVDKYEVEN-TAYELLVeEKSFDEIViKNTAGKYD 83
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSlgdvlgTELGNEPTEVAVPNlYALEIDP-EAELEEYW-ERVRAPLR 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501038728  84 LIASNGDVT--------AAEIKLMEFFAREIRlrnalapiKDQYDYIFIDCPPS---LNMLT 134
Cdd:COG0003   89 GLLPSAGVDelaeslpgTEELAALDELLELLE--------EGEYDVIVVDTAPTghtLRLLS 142
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-128 3.74e-06

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: 46.73  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGN------ATMGSGVDKYEVEN-TAYELLVE---EKSFDEivIKNTAG 80
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSlsdafgQKLGGETPVKGAPNlWAMEIDPEealEEYWEE--VKELLA 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501038728  81 KYDLIASNGDVTAAEIKLM----EFFAREiRLRNALApiKDQYDYIFIDCPP 128
Cdd:cd02035   86 QYLRLPGLDEVYAEELLSLpgmdEAAAFD-ELREYVE--SGEYDVIVFDTAP 134
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-254 8.90e-06

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 45.90  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT---MGSGVDKYEVENTAYELLVEEKSFDEIVIKNTAGKYDL--- 84
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrllLGGKLQPTVLDTAREKGYVEDVEVEDVVYKGYGGVKCVesg 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   85 -------IASNGDVTAaeIKLMEffareirlRNAlapIKDQYDYIFID------C-----PPSLNMltvnamsaADSVLV 146
Cdd:pfam00142  88 gpepgvgCAGRGVITA--INLLE--------ELG---AYDDLDFVLYDvlgdvvCggfamPIREGK--------AQEIYI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  147 PMQCEYYALEGLTALIDTITKLAAMvnPGLGIEGILrtmYDPRNRLSN-DVSDQLKQHFGDKVYRtVIPRNVRLAEAPSF 225
Cdd:pfam00142 147 VTSNEMMALYAANNIAKGIQKYAKS--GGVRLGGII---CNSRKVDDErELIDAFAEELGTQVLH-FVPRDNIVRKAELR 220

                         250       260
                  ....*....|....*....|....*....
gi 501038728  226 GAPAMYYDKSSAGAKAYLALAGEMIRRSE 254
Cdd:pfam00142 221 KQTVIEYAPDSEQAQEYRELARKILENPK 249
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 5-83 1.78e-05

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: 44.99  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   5 IAVANqKGGVGKTTTCVNLAASLAATKRKVLLIDLDPqgNATMGS--GVDKYEVENTAYELLVEEKSFDEIVIKNTAGKY 82
Cdd:cd02034    3 IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP--NSNLAEtlGVEVEKLPLIKTIGDIRERTGAKKGEPPEGMSL 79


                 .
gi 501038728  83 D 83
Cdd:cd02034   80 N 80
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 3-46 2.71e-05

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: 44.21  E-value: 2.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 501038728   3 KVIAVANqKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT 46
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
PRK10818 PRK10818
septum site-determining protein MinD;
1-242 3.71e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 44.16  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   1 MGKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD-PQGNATMGSGVDKYEVENTAyELLVEEKSFDEIVIKN-- 77
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRVVYDFV-NVIQGDATLNQALIKDkr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  78 TAGKYDLIASngdvtaaEIKLMEFFAREiRLRNALAPIKDQ-YDYIFIDCPPSLNMLTVNAMSAADSVLVPMQCEYYALE 156
Cdd:PRK10818  80 TENLYILPAS-------QTRDKDALTRE-GVAKVLDDLKAMdFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728 157 GLTALIDTITKLAAMVNPGLGI--EGILRTMYDPrNRLSNdvSDQLKQHFGDKVYRT----VIPRNVRLAEAPSFGAPAM 230
Cdd:PRK10818 152 DSDRILGILASKSRRAENGEEPikEHLLLTRYNP-GRVSR--GDMLSMEDVLEILRIklvgVIPEDQSVLRASNQGEPVI 228

                        250
                 ....*....|..
gi 501038728 231 YYDKSSAGaKAY 242
Cdd:PRK10818 229 LDIEADAG-KAY 239
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-147 6.28e-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: 42.91  E-value: 6.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   2 GKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLD----------PQGNATMGSGVDKYEVENTAYELLVeeksfd 71
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMErlqstdvffgASGRYLMSDHLYTLKSRKANLADKL------ 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501038728  72 EIVIKNTAGKYDLIA---SNGDVTAAEIKLMEFFAREIRLRNAlapikdqYDYIFIDCPPSLNMLTVNAMSAADSVLVP 147
Cdd:cd17869   77 ESCVKQHESGVYYFSpfkSALDILEIKKDDILHMITKLVEAHA-------YDYIIMDLSFEFSSTVCKLLQASHNNVVI 148
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
 13-127 1.37e-04

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


Pssm-ID: 349780  Cd Length: 196  Bit Score: 41.75  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  13 GVGKTTTCVNLAASLAATKRKVLLIDLDPQgnatmgsgvdkyeVENTAYELLVEEKSFdeIVIKNTAGKYDLiASNGdvt 92
Cdd:cd17871   10 GSGKTTYCKGMQQFLSALGRKVAVVNLDPA-------------NEFLPYPCDVDIREL--ITVEDVMEELKL-GPNG--- 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501038728  93 aAEIKLMEFFAREIR-LRNALAPIKDqyDYIFIDCP 127
Cdd:cd17871   71 -GLLYCMEYLEKNIDwLIDKLKKLKD--SYLIFDCP 103
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-44 2.68e-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: 42.00  E-value: 2.68e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 501038728   11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGN 44
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-46 3.56e-04

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


Pssm-ID: 349759  Cd Length: 265  Bit Score: 40.96  E-value: 3.56e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 501038728  11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT 46
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
 13-127 7.80e-04

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 39.66  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728   13 GVGKTTTCVNLAASLAATKRKVLLIDLDPQgnatmgsgvdkyeVENTAYELLVEEKsfDEIVIKNTAGKYDLIaSNGDVT 92
Cdd:pfam03029   6 GSGKTTFVGALSEILPLRGRPVYVVNLDPA-------------AENLPYPADIDIR--ELITVADVMEDYGLG-PNGALT 69

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 501038728   93 AAeiklMEFFAreIRLRNALAPIKDQYDYIFIDCP 127
Cdd:pfam03029  70 VA----MDFGR--ITLDWLDEELKREDDYYLFDTP 98
PRK09841 PRK09841
tyrosine-protein kinase;
15-180 8.95e-04

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 40.28  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  15 GKTTTCVNLAASLAATKRKVLLIDLDPQgnatMGSGVDKYEVENTA--YELLVEEKSFDEIVIKNTAGKYDLIasngdvT 92
Cdd:PRK09841 544 GKTFVSSTLAAVIAQSDQKVLFIDADLR----RGYSHNLFTVSNEHglSEYLAGKDELNKVIQHFGKGGFDVI------T 613

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  93 AAEIKL--MEFFAREiRLRNALAPIKDQYDYIFIDCPPSLNM--LTVNAMSAADSVLVpmqceyyALEGLTALIDTITKL 168
Cdd:PRK09841 614 RGQVPPnpSELLMRD-RMRQLLEWANDHYDLVIVDTPPMLAVsdAAVVGRSVGTSLLV-------ARFGLNTAKEVSLSM 685

                        170
                 ....*....|..
gi 501038728 169 AAMVNPGLGIEG 180
Cdd:PRK09841 686 QRLEQAGVNIKG 697
chlL CHL00072
photochlorophyllide reductase subunit L
 11-46 1.05e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 39.72  E-value: 1.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 501038728  11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT 46
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDST 43
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 11-41 1.55e-03

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: 39.26  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 501038728   11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDP 41
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDP 39
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-41 1.87e-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: 1.87e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 501038728   11 KGGVGKTTTCVNLAASLAATKRKVLLIDLDP 41
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP 359
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
 2-52 3.11e-03

helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.


Pssm-ID: 274798 [Multi-domain]  Cd Length: 322  Bit Score: 38.47  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501038728    2 GKVIAVANQKGGVGKTTTCVNLAASLAATKRKVLLIDLDPqgnatMGSGVD 52
Cdd:TIGR03815  93 GVVVAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADP-----WGGGLD 138
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
13-130 3.31e-03

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 38.59  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  13 GVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT---MGSgvdkyEVENTAYELLVEEKSFDEIVIKNTAGKYDLIaSNG 89
Cdd:PRK11519 537 SIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYThelLGT-----NNVNGLSDILIGQGDITTAAKPTSIANFDLI-PRG 610

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501038728  90 DV--TAAEIKLMEFFAREIrlrnalAPIKDQYDYIFIDCPPSL 130
Cdd:PRK11519 611 QVppNPSELLMSERFAELV------NWASKNYDLVLIDTPPIL 647
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 13-81 4.40e-03

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


Pssm-ID: 349786  Cd Length: 193  Bit Score: 37.19  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038728  13 GVGKTTTCVNLAASLAATKRKVLLIDLDPQGNA------TMGS--GVDKYEVEN------TAYELL--VEEKSFDeIVIK 76
Cdd:cd18539   10 GSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAaieqlqTLGEqvGVPVFESGDgqspvdIAKRALekAKEEGFD-VVIV 88


                 ....*
gi 501038728  77 NTAGK 81
Cdd:cd18539   89 DTAGR 93
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 5-40 6.25e-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: 6.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 501038728   5 IAVANQKGGVGKTTtcvnLAASLAATKRKVLLIDLD 40
Cdd:cd03110    2 IAVLSGKGGTGKTT----ITANLAVLLYNVILVDCD 33
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 3-46 6.40e-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: 37.50  E-value: 6.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 501038728   3 KVIAVANqKGGVGKTTTCVNLAASLAATKRKVLLIDLDPQGNAT 46
Cdd:cd02033   32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTT 74
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 13-40 7.27e-03

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


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 36.75  E-value: 7.27e-03
                          10        20
                  ....*....|....*....|....*...
gi 501038728   13 GVGKTTTCVNLAASLAATKRKVLLIDLD 40
Cdd:pfam00448  10 GSGKTTTIAKLAAYLKKKGKKVLLVAAD 37
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 13-47 9.19e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 36.08  E-value: 9.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 501038728   13 GVGKTTTCVNLAASLAATKRKVLLIDLDP-QGNATM 47
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDVgQSEIGP 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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