|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
35-289 |
4.89e-117 |
|
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: 338.37 E-value: 4.89e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 35 TRRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGADHRAGTLSSYEMLIGECAAEEALQQsTASE 114
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVP-TEIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 115 NLFCIPATIDLAGAEIELVSLVRREYRLADALNDAfikEHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALEG 194
Cdd:COG1192 80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPL---ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 195 VGQLLNNIGMIRQHLNQNLHISAILLTMYDGRTKLSEQVTEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVLDYDPGSR 274
Cdd:COG1192 157 LAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSK 236
|
250
....*....|....*
gi 504085602 275 GAMAYLDAARELAQR 289
Cdd:COG1192 237 GAKAYRALAEELLER 251
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
40-215 |
1.22e-73 |
|
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: 225.16 E-value: 1.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 40 VANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGADHRAGTLSSYEMLIGECAAEEALQQsTASENLFCI 119
Cdd:pfam13614 6 IANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIK-TVIENLDLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 120 PATIDLAGAEIELVSLVRREYRLADALNDafIKEHgFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALEGVGQLL 199
Cdd:pfam13614 85 PSNIDLAGAEIELIGIENRENILKEALEP--VKDN-YDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLL 161
|
170
....*....|....*.
gi 504085602 200 NNIGMIRQHLNQNLHI 215
Cdd:pfam13614 162 NTIKLVKKRLNPSLEI 177
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
38-266 |
6.04e-48 |
|
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: 160.97 E-value: 6.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 38 LTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGA--DHRAGTLSSYEMLIGECAAEEALQQSTASE- 114
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLegDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 115 NLFCIPATIDLAGAEIELVSlVRREYRLADALNDAfikEHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALEG 194
Cdd:pfam01656 81 GLDLIPGNIDLEKFEKELLG-PRKEERLREALEAL---KEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVED 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504085602 195 VGQLLNNIGMIRQHLN-QNLHISAILLTMYDGR---TKLSEQVTEEVRGhfgdVVLRTKIPRSVKVSEAPGYGQTV 266
Cdd:pfam01656 157 AKRLGGVIAALVGGYAlLGLKIIGVVLNKVDGDnhgKLLKEALEELLRG----LPVLGVIPRDEAVAEAPARGLPV 228
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
36-238 |
2.37e-40 |
|
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: 138.06 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALgadhragtlssyemligecaaeealqqstasen 115
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 116 lfcipatidlagaeielvslvrreyrladalndafikehgFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALEGV 195
Cdd:cd02042 48 ----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGL 87
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504085602 196 GQLLNNIGMIRQHLNQNLHISAILLTMYDGRTKLSEQVTEEVR 238
Cdd:cd02042 88 AKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
38-288 |
5.24e-27 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 105.33 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 38 LTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTAlgadhragtlssyemliGECAAEEALqqstasenlf 117
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDW-----------------AAAREDERP---------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 118 ciPATIDLAGAEIElvslvrreyRLADALNdafikeHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALEGVGQ 197
Cdd:NF041546 55 --FPVVGLARPTLH---------RELPSLA------RDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASAD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 198 LLNNIGMiRQHLNQNLHiSAILLTMYDGRTKLSEQVTEEVRGhFGDVVLRTKIPRSVKVSEAPGYGQTVLDYDPGSrgam 277
Cdd:NF041546 118 TVDLIKE-AREYTPGLK-AAFVLNRAIARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG---- 190
|
250
....*....|.
gi 504085602 278 aylDAARELAQ 288
Cdd:NF041546 191 ---KAAREIRA 198
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
66-289 |
2.33e-19 |
|
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: 85.33 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 66 KVLVVDLDPQ-GNASTALGADHRAgTLSSYemLIGECAAEEALQQStaSENLFCIPATIDLAGAEielvsLVRREYRLAD 144
Cdd:COG0455 16 RVLLVDADLGlANLDVLLGLEPKA-TLADV--LAGEADLEDAIVQG--PGGLDVLPGGSGPAELA-----ELDPEERLIR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 145 ALNDAfikEHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALEGVGQLLNNIGmiRQHLNQNLHisaILLTMYD 224
Cdd:COG0455 86 VLEEL---ERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLR--RRLGVRRAG---VVVNRVR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504085602 225 GRT---KLSEQVTEEVRGHFG-DVVLRTKIPRSVKVSEAPGYGQTVLDYDPGSRGAMAYLDAARELAQR 289
Cdd:COG0455 158 SEAearDVFERLEQVAERFLGvRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
36-286 |
3.45e-18 |
|
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: 82.25 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLD-PQGNASTALGADHRAG-TLSsyEMLIGECAAEEALQQSTAS 113
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIVyTLV--DVLEGECRLEQALIKDKRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 114 ENLFCIPATIDLAGAEielvslVRREyRLADALNDafIKEHgFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALE 193
Cdd:cd02036 79 ENLYLLPASQTRDKDA------LTPE-KLEELVKE--LKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 194 G---VGQLLNNIGMIRQHLnqnlhisaiLLTMYD-GRTKLSEQVT-EEVRGHFGDVVLRTkIPRSVKVSEAPGYGQTVLD 268
Cdd:cd02036 149 DadrVIGLLESKGIVNIGL---------IVNRYRpEMVKSGDMLSvEDIQEILGIPLLGV-IPEDPEVIVATNRGEPLVL 218
|
250
....*....|....*...
gi 504085602 269 YDPGSRGAMAYLDAAREL 286
Cdd:cd02036 219 YKPNSLAAKAFENIARRL 236
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
33-282 |
2.63e-17 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 82.03 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 33 ERTRRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGADHRAgTLSSYEMLIGECAAEEALQ---- 108
Cdd:PRK13869 119 EHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPET-DVGANETLYAAIRYDDTRRplrd 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 109 --QSTASENLFCIPATIDLAGAE----IELVSLVRRE----YRLADALNDAfikEHGFDYVFIDCPPSLGLLTINAMTAV 178
Cdd:PRK13869 198 viRPTYFDGLHLVPGNLELMEFEhttpKALSDKGTRDglffTRVAQAFDEV---ADDYDVVVIDCPPQLGFLTLSGLCAA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 179 DEVLIPIQCEYYALEGVGQLL----NNIGMIRQhLNQNLHISAI--LLTMYDGRTKLSEQVTEEVRGHFGDVVLRTKIPR 252
Cdd:PRK13869 275 TSMVITVHPQMLDIASMSQFLlmtrDLLGVVKE-AGGNLQYDFIryLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVK 353
|
250 260 270
....*....|....*....|....*....|....*...
gi 504085602 253 SVKVSEAPGYGQTVldYDPGSRG--------AMAYLDA 282
Cdd:PRK13869 354 SAAVSDAGLTKQTL--YEIGRENltrstydrAMESLDA 389
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
36-287 |
4.52e-17 |
|
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: 79.39 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLD-PQGNASTALGADHRAGTLssYEMLIGECAAEEALQQStaSE 114
Cdd:TIGR01969 1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVTL--HDVLAGEADIKDAIYEG--PF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 115 NLFCIPATIDLAG---AEIElvslvrreyRLADALNDafIKEHgFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYA 191
Cdd:TIGR01969 77 GVKVIPAGVSLEGlrkADPD---------KLEDVLKE--IIDD-TDFLLIDAPAGLERDAVTALAAADELLLVVNPEISS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 192 LEGVGQllnnIGMIRQHLNQNLhISAILLTMYDGRTKLSEQVTEEVRghfgDVVLRTKIPRSVKVSEAPGYGQTVLDYDP 271
Cdd:TIGR01969 145 ITDALK----TKIVAEKLGTAI-LGVVLNRVTRDKTELGREEIETIL----EVPVLGVVPEDPEVRRAAAFGEPVVIYNP 215
|
250
....*....|....*.
gi 504085602 272 GSRGAMAYLDAARELA 287
Cdd:TIGR01969 216 NSPAAQAFMELAAELA 231
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
38-285 |
9.88e-17 |
|
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: 80.41 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 38 LTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGA----DHRAG-TLssYEML--------IGEcaae 104
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpefDVGENeTL--YGAIrydderrpISE---- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 105 eaLQQSTASENLFCIPATIDLAGAEIELVSLVRREY--------RLADALNDAfikEHGFDYVFIDCPPSLGLLTINAMT 176
Cdd:TIGR03453 181 --IIRKTYFPGLDLVPGNLELMEFEHETPRALSRGQggdtiffaRVGEALAEV---EDDYDVVVIDCPPQLGFLTLSALC 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 177 AVDEVLIPIQCEYYALEGVGQLLNNIGMIRQHLNQ---NLHISAI--LLTMYDGRTKLSEQVTEEVRGHFGDVVLRTKIP 251
Cdd:TIGR03453 256 AATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREaggNLSYDFMryLVTRYEPNDGPQAQMVAFLRSLFGDHVLTNPML 335
|
250 260 270
....*....|....*....|....*....|....
gi 504085602 252 RSVKVSEAPGYGQTVLDYDPGSRGAMAYlDAARE 285
Cdd:TIGR03453 336 KSTAISDAGLTKQTLYEVERSQFTRSTY-DRAME 368
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
38-289 |
3.83e-14 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 70.26 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 38 LTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTAlgADHRAGTlssyemligecaaEEALQQSTASENLF 117
Cdd:PHA02518 3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW--AEAREEG-------------EPLIPVVRMGKSIR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 118 CipatidlagaEIELVSlvrreyrladalndafikeHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQ---CEYYALEG 194
Cdd:PHA02518 68 A----------DLPKVA-------------------SGYDYVVVDGAPQDSELARAALRIADMVLIPVQpspFDIWAAPD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 195 VGQLLNNigmiRQHLNQNLHISAILLTMYDGRTKLSEQVTEEVRGhFGDVVLRTKIPRSVKVSEAPGYGQTVLDYDPGSR 274
Cdd:PHA02518 119 LVELIKA----RQEVTDGLPKFAFIISRAIKNTQLYREARKALAG-YGLPILRNGTTQRVAYADAAEAGGSVLELPEDDK 193
|
250
....*....|....*
gi 504085602 275 GAMAYLDAARELAQR 289
Cdd:PHA02518 194 AAEEIIQLVKELFRG 208
|
|
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
38-264 |
7.27e-13 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 68.85 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 38 LTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVD-LDPQGNASTALG--AD---HRAGTLSSYEMliGECAAEEALQQST 111
Cdd:PRK13705 109 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGwvPDlhiHAEDTLLPFYL--GEKDDATYAIKPT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 112 ASENLFCIPATIDLAGAEIELVSLvRREYRLADA---LNDAFIKE--HGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQ 186
Cdd:PRK13705 187 CWPGLDIIPSCLALHRIETELMGK-FDEGKLPTDphlMLRLAIETvaHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 187 CEYYALEGVGQLLNnigMIRQhLNQNLHISA------ILLTMY-DGRTKLSEQVTEEVRGHFGDVVLRtkipRSVKVSEA 259
Cdd:PRK13705 266 AELFDYTSALQFFD---MLRD-LLKNVDLKGfepdvrILLTKYsNSNGSQSPWMEEQIRDAWGSMVLK----NVVRETDE 337
|
....*
gi 504085602 260 PGYGQ 264
Cdd:PRK13705 338 VGKGQ 342
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
38-264 |
1.01e-11 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 65.42 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 38 LTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVD-LDPQGNASTALG--AD---HRAGTLSSYemLIGECAAEEALQQST 111
Cdd:PHA02519 109 LAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGyvPDlhiHADDTLLPF--YLGERDNAEYAIKPT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 112 ASENLFCIPATIDLAGAEIELVSLVRRE-------YRLADALNDAFikeHGFDYVFIDCPPSLGLLTINAMTAVDEVLIP 184
Cdd:PHA02519 187 CWPGLDIIPSCLALHRIETDLMQYHDAGklphpphLMLRAAIESVW---DNYDIIVIDSAPNLGTGTINVVCAADVIVVA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 185 IQCEYYALEGVGQLLNnigMIRQhLNQNLHISA------ILLTMYDGRT-KLSEQVTEEVRGHFGDVVLRtkipRSVKVS 257
Cdd:PHA02519 264 TPAELFDYVSVLQFFT---MLLD-LLATVDLGGfepvvrLLLTKYSLTVgNQSRWMEEQIRNTWGSMVLR----QVVRVT 335
|
....*..
gi 504085602 258 EAPGYGQ 264
Cdd:PHA02519 336 DEVGKGQ 342
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
30-311 |
5.35e-11 |
|
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: 62.82 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 30 PRPERTRRLTVANQKGGVGKTTSSVNL-AAGLALGGLKVLVVDLDPQ-GNASTALGADHRAGtlssyemlIGECAA---- 103
Cdd:COG4963 97 GAARRGRVIAVVGAKGGVGATTLAVNLaWALARESGRRVLLVDLDLQfGDVALYLDLEPRRG--------LADALRnpdr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 104 --EEALQQ--STASENLFCIPATIDLAGAEI-------ELVSLVRREyrladalndafikehgFDYVFIDCPPSLGLLTI 172
Cdd:COG4963 169 ldETLLDRalTRHSSGLSVLAAPADLERAEEvspeaveRLLDLLRRH----------------FDYVVVDLPRGLNPWTL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 173 NAMTAVDEVLIPIQCEYYALEGVGQLLNNIGMIRqHLNQNLHisaILLTMYDGRTKLSEqvtEEVRGHFGDVVLRTkIPR 252
Cdd:COG4963 233 AALEAADEVVLVTEPDLPSLRNAKRLLDLLRELG-LPDDKVR---LVLNRVPKRGEISA---KDIEEALGLPVAAV-LPN 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 253 SVK-VSEAPGYGQTVLDYDPGSRgamaYLDAARELAQRgdYLPIEASGAVGMSPESARRL 311
Cdd:COG4963 305 DPKaVAEAANQGRPLAEVAPKSP----LAKAIRKLAAR--LTGRPAAAAAKAGGKLLKRL 358
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
33-183 |
8.64e-11 |
|
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: 60.28 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 33 ERTRRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDP-QGNASTALGADHRAGtLSSYemLIGECAAEEALQQsT 111
Cdd:cd05387 17 AGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNEPG-LSEV--LSGQASLEDVIQS-T 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504085602 112 ASENLFCIPatidlAGAEIELVSLVRREYRLADALNDAfiKEHgFDYVFIDCPPSLGLL-TINAMTAVDEVLI 183
Cdd:cd05387 93 NIPNLDVLP-----AGTVPPNPSELLSSPRFAELLEEL--KEQ-YDYVIIDTPPVLAVAdALILAPLVDGVLL 157
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
27-224 |
3.60e-10 |
|
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: 59.82 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 27 LHLPRPERTRRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQG-NASTALGADHRAGtLSSYemLIGECAAEE 105
Cdd:COG0489 84 LLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGpSLHRMLGLENRPG-LSDV--LAGEASLED 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 106 ALQQsTASENLFCIPA-TIDLAGAEIelvsLVRReyRLADALNDAfikEHGFDYVFIDCPPSLGL--LTInAMTAVDEVL 182
Cdd:COG0489 161 VIQP-TEVEGLDVLPAgPLPPNPSEL----LASK--RLKQLLEEL---RGRYDYVIIDTPPGLGVadATL-LASLVDGVL 229
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504085602 183 IPIQCEYYALEGVGQLLNnigMIRQHlnqNLHISAILLTMYD 224
Cdd:COG0489 230 LVVRPGKTALDDVRKALE---MLEKA---GVPVLGVVLNMVC 265
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
36-294 |
7.33e-10 |
|
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: 58.89 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDpQG--NASTALGADHRAgTLSSYEMLIGECAAEEALQQSTAS 113
Cdd:TIGR01968 2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-IGlrNLDLLLGLENRI-VYTLVDVVEGECRLQQALIKDKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 114 ENLFCIPAtidlagAEIELVSLVRREyRLADALNDafIKEHgFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYALE 193
Cdd:TIGR01968 80 KNLYLLPA------SQTRDKDAVTPE-QMKKLVNE--LKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 194 GVGQLlnnIGMIRQhlNQNLHISAILLTMYDGRTKLSEQVT-EEVRGHFGdVVLRTKIPRSVKVSEAPGYGQTVLdYDPG 272
Cdd:TIGR01968 150 DADRV---IGLLEA--KGIEKIHLIVNRLRPEMVKKGDMLSvDDVLEILS-IPLIGVIPEDEAIIVSTNKGEPVV-LNDK 222
|
250 260
....*....|....*....|..
gi 504085602 273 SRGAMAYLDAARELAQRGDYLP 294
Cdd:TIGR01968 223 SRAGKAFENIARRILGEEVPFE 244
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
36-183 |
3.29e-09 |
|
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: 56.42 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLD-PQGNASTALGADHRAgTLSSYemLIGECAAEEALQQSTasE 114
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPKK-TLGDV--LKGRVSLEDIIVEGP--E 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 115 NLFCIPATIDLAgaeiELVSL-VRREYRLADALNDAFIKehgFDYVFIDCPPSLGLLTINAMTAVDEVLI 183
Cdd:cd02038 76 GLDIIPGGSGME----ELANLdPEQKAKLIEELSSLESN---YDYLLIDTGAGISRNVLDFLLAADEVIV 138
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
35-183 |
3.32e-09 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 57.09 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 35 TRRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLD-PQGNASTALGADHRAgTLSSYEMLIGECAAEEALQQSTAS 113
Cdd:CHL00175 15 SRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRV-LYTAMDVLEGECRLDQALIRDKRW 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504085602 114 ENLFCIPAtidlagaeielvSLVRREYRLA----DALNDAfIKEHGFDYVFIDCPPSLGLLTINAMTAVDEVLI 183
Cdd:CHL00175 94 KNLSLLAI------------SKNRQRYNVTrknmNMLVDS-LKNRGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
36-286 |
1.59e-08 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 54.95 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLD-PQGNASTALGADHRAgTLSSYEMLIGECAAEEALQQSTASE 114
Cdd:PRK10818 3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRV-VYDFVNVIQGDATLNQALIKDKRTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 115 NLFCIPA--TIDLAGAEIELVSLVrreyrladaLNDafIKEHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPIQCEYYAL 192
Cdd:PRK10818 82 NLYILPAsqTRDKDALTREGVAKV---------LDD--LKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 193 EGVGQLL-----------NNIGMIRQHLnqnlhisaiLLTMYD-GRTKLSEQVTEEVRGHFGDVVLRTKIPRSVKVSEAP 260
Cdd:PRK10818 151 RDSDRILgilasksrraeNGEEPIKEHL---------LLTRYNpGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRAS 221
|
250 260
....*....|....*....|....*.
gi 504085602 261 GYGQTVLdYDPGSRGAMAYLDAAREL 286
Cdd:PRK10818 222 NQGEPVI-LDIEADAGKAYADTVDRL 246
|
|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
37-276 |
3.69e-08 |
|
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274549 [Multi-domain] Cd Length: 246 Bit Score: 53.50 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 37 RLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGAD--HRAGtLSSYeMLIGECAAeEALQQSTASE 114
Cdd:TIGR03371 3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDwsVRDG-WARA-LLNGADWA-AAAYRSPDGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 115 NLfcIP-ATIDLAGAEIELVSLVRREYRLADALNDAfikehGFDYVFIDCPPSLGLLTINAMTAVDEVLIPI----QCEY 189
Cdd:TIGR03371 80 LF--LPyGDLSADEREAYQAHDAGWLARLLQQLDLA-----ARDWVLIDLPRGPSPITRQALAAADLVLVVVnadaACYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 190 YALEGVGQLLNNIGMIRQHlnqnlhisAILLTMYDGRTKLSEQVTEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVLDY 269
Cdd:TIGR03371 153 TLHQLALALFAGSGPRDGP--------RFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNY 224
|
....*..
gi 504085602 270 DPGSRGA 276
Cdd:TIGR03371 225 APHSQAA 231
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
44-294 |
2.71e-07 |
|
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: 51.21 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 44 KGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGADHRAGTLSsyEMLIGECAAEEALQQS---TASENLFCI- 119
Cdd:cd02117 8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTID--EMLTEDGTAEELRREDllfSGFNGVDCVe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 120 ----PATIDLAGAEI-ELVSLVRREYRLADalndafikehGFDYVFIDCppsLGLLTINAMTA------VDEVLIPIQCE 188
Cdd:cd02117 86 aggpEPGVGCGGRGIgTMLELLEEHGLLDD----------DYDVVIFDV---LGDVVCGGFAAplrrgfAQKVVIVVSEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 189 YYALEGVgqllNNI-GMIRQHLNQNLHISAILLTMYD-GRTKLSEQVTEEVrghfgdvvlRTKI----PRSVKVSEAPGY 262
Cdd:cd02117 153 LMSLYAA----NNIvKAVENYSKNGVRLAGLVANLRDpAGTEEIQAFAAAV---------GTKIlaviPRDPAVRRAELA 219
|
250 260 270
....*....|....*....|....*....|..
gi 504085602 263 GQTVLDYDPGSRGAMAYLDAARELAQRGDYLP 294
Cdd:cd02117 220 RVTVFEHDPVSPAASEFARLAAKIADAVPPVP 251
|
|
| PRK13230 |
PRK13230 |
nitrogenase reductase-like protein; Reviewed |
44-288 |
1.13e-05 |
|
nitrogenase reductase-like protein; Reviewed
Pssm-ID: 183903 Cd Length: 279 Bit Score: 46.30 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 44 KGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGADHRAGTLSSY-EMLIGECAAEEALQQSTASenLFCIPAt 122
Cdd:PRK13230 9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLrEKGIDNLGLEDIIYEGFNG--IYCVES- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 123 idlAGAEIELVSLVRREYRLADALN--DAFiKEHGFDYVFIDCppsLGLLTINA------MTAVDEVLIPIQCEYYALEG 194
Cdd:PRK13230 86 ---GGPEPGYGCAGRGVITAIDLLKklGVF-EELGPDVVIYDI---LGDVVCGGfamplqKGLADDVYIVTTCDPMAIYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 195 VgqllNNI--GMIRQHLNQNLHISAILltmYDGRTKLSE-QVTEEVRGHFGDVVLrTKIPRSVKVSEAPGYGQTVLDYDP 271
Cdd:PRK13230 159 A----NNIckGIKRFAKRGKSALGGII---YNGRSVIDApDIVEEFAKKIGTNVI-GKIPMSNIITEAEIYGKTVIEYAP 230
|
250
....*....|....*..
gi 504085602 272 GSRGAMAYldaaRELAQ 288
Cdd:PRK13230 231 DSEISNIF----RELAE 243
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
44-183 |
1.17e-05 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 46.20 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 44 KGGVGKTTSSVNLAAGLALGGLKVLVVDLDpQG--NASTALGADHRagtlssyemlI---------GECAAEEALQQSTA 112
Cdd:COG2894 11 KGGVGKTTTTANLGTALALLGKKVVLIDAD-IGlrNLDLVMGLENR----------IvydlvdvieGECRLKQALIKDKR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504085602 113 SENLFCIPA--TIDLAGAEIELVSlvrreyRLADALndafiKEHgFDYVFIDCPPSL--GLLtiNAMTAVDEVLI 183
Cdd:COG2894 80 FENLYLLPAsqTRDKDALTPEQMK------KLVEEL-----KEE-FDYILIDSPAGIeqGFK--NAIAGADEAIV 140
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
36-284 |
1.36e-05 |
|
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: 45.73 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVN-LAAGLALGGLKVLVVDLD-PQGNASTALGADHRAGTLSSYEML--IGECAAEEALQQST 111
Cdd:cd03111 1 RVVAVVGAKGGVGASTLAVNlAQELAQRAKDKVLLIDLDlPFGDLGLYLNLRPDYDLADVIQNLdrLDRTLLDSAVTRHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 112 ASENLFCIPATIDLA---GAE--IELVSLVRREYrladalndafikehgfDYVFIDCPPSLGLLTINAMTAVDEVLIPIQ 186
Cdd:cd03111 81 SGLSLLPAPQELEDLealGAEqvDKLLQVLRAFY----------------DHIIVDLGHFLDEVTLAVLEAADEILLVTQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 187 CEYYALEGVGQLLNnigMIRQHLNQNLHISaILLTMYDGRTKLSEQVTEEVrghFGDVVLRTkIP-RSVKVSEAPGYGQT 265
Cdd:cd03111 145 QDLPSLRNARRLLD---SLRELEGSSDRLR-LVLNRYDKKSEISPKDIEEA---LGLEVFAT-LPnDYKAVSESANTGRP 216
|
250
....*....|....*....
gi 504085602 266 VLDYDPGSRGAMAYLDAAR 284
Cdd:cd03111 217 LVEVAPRSALVRALQDLAA 235
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
44-170 |
1.38e-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: 46.19 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 44 KGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGadhragtlssyemligecaaEEALQQSTA-SENLFCIpaT 122
Cdd:pfam02374 9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFN--------------------QKFGHEPTKvKENLSAM--E 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504085602 123 IDLAGAEIELVSLVRREYR-----------LADALN-----------DAFIK---EHGFDYVFIDCPP---SLGLL 170
Cdd:pfam02374 67 IDPNMELEEYWQEVQKYMNallglrmlegiLAEELAslpgideaasfDEFKKymdEGEYDVVVFDTAPtghTLRLL 142
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
36-185 |
1.57e-04 |
|
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: 42.83 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQgNASTALGADHRAGTLSSYEMligECAAEEALQQSTASEN 115
Cdd:pfam09140 1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFHRYFENRSATADRTGL---SLPTPEHLNLPDNDVA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 116 LFCIPATIDLAgaeielvslvrreyRLADALNDAfikEHGFDYVFIDCPPSLGLLTINAMTAVDEVLIPI 185
Cdd:pfam09140 77 EVPDGENIDDA--------------RLEEAFADL---EARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
250-289 |
8.10e-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: 40.57 E-value: 8.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 504085602 250 IPRSVKVSEAPGYGQTVLDYDPGSRGAMAYldaaRELAQR 289
Cdd:cd02040 207 VPRSNEVQEAELRGKTVIEYDPDSEQADEY----RELAKK 242
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
36-188 |
9.02e-04 |
|
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: 39.73 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 36 RRLTVANQKGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGnaSTALG---ADHRAGTLSSYemLIGECAAEEALQQsTA 112
Cdd:TIGR01007 18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRN--SVMSGtfkSQNKITGLTNF--LSGTTDLSDAICD-TN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504085602 113 SENLFCIPAtidlAGAEIELVSLVRREY--RLADALNDAfikehgFDYVFIDCPPsLGLLTINA--MTAVDEVLIPIQCE 188
Cdd:TIGR01007 93 IENLDVITA----GPVPPNPTELLQSSNfkTLIETLRKR------FDYIIIDTPP-IGTVTDAAiiARACDASILVTDAG 161
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
44-91 |
4.07e-03 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 38.22 E-value: 4.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504085602 44 KGGVGKTTSSVNLAAGLALGGLKVLVVDLDPQGNASTALGADHRAGTL 91
Cdd:COG3640 8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLI 55
|
|
| |
