|
Name |
Accession |
Description |
Interval |
E-value |
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
16-290 |
1.95e-86 |
|
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF).
Pssm-ID: 132074 [Multi-domain] Cd Length: 274 Bit Score: 259.80 E-value: 1.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 16 DRSIGAIISETRNLSADQVERILAYQLEKGVRFGEAAISLGFASADDVLFALAQQFHYPYAAEEQRKLSPELVTFNQPFS 95
Cdd:TIGR03029 2 DANIGKVLLDAGKLSEDEAERILRLQKQENIRFGEAALRLGLINEDDIRQALSRQFEYPYLPPNDGSFSPDLIAAYQPFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 96 LQSEAFRATRSQITMRvWSDsEPRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGL 175
Cdd:TIGR03029 82 PQVEALRALRSQLMLR-WFS-EGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNFKLSEQRGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 176 SGILSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAA 255
Cdd:TIGR03029 160 SDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQIVATRARGT 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1525821860 256 IVVARKDASRVASLQDMVAVMSGSPVRFAGVVMNE 290
Cdd:TIGR03029 240 LIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ 274
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
99-289 |
2.93e-55 |
|
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: 176.99 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 99 EAFRATRSQITMRVwsDSEPRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGLSGI 178
Cdd:cd05387 1 EAFRTLRTNLLFAG--SDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 179 LSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAAIVV 258
Cdd:cd05387 79 LSGQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLV 158
|
170 180 190
....*....|....*....|....*....|.
gi 1525821860 259 ARKDASRVASLQDMVAVMSGSPVRFAGVVMN 289
Cdd:cd05387 159 VRAGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
115-289 |
2.63e-50 |
|
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: 167.67 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 115 DSEPRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGLSGILSGRAESSVIQQVVGV 194
Cdd:COG0489 88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 195 PSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAAIVVARKDASRVASLQDMVA 274
Cdd:COG0489 168 EGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALE 247
|
170
....*....|....*
gi 1525821860 275 VMSGSPVRFAGVVMN 289
Cdd:COG0489 248 MLEKAGVPVLGVVLN 262
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
80-260 |
4.08e-28 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 113.71 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 80 QRKLSPELVTFNQPFSLQSEAFRATRSQITMRVWSDSEPRRALAVVSPEIGdgKTYFAANLAVVLAQLGGRTLLVDADMR 159
Cdd:PRK11519 489 KRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIG--KTFVCANLAAVISQTNKRVLLIDCDMR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 160 SPRQHDVFNLNNNAGLSGILSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAA 239
Cdd:PRK11519 567 KGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPI 646
|
170 180
....*....|....*....|.
gi 1525821860 240 ELGADASVIAARCGAAIVVAR 260
Cdd:PRK11519 647 LAVTDAAIVGRHVGTTLMVAR 667
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
122-289 |
1.84e-08 |
|
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: 53.89 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDAD-MRS--------PRQHDVFNlNNNAGLSG-------ILSGRAES 185
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpQSNnssvegleGDIAPALQ-ALAEGLKGrvnldpiLLKEKSDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 186 SVIQQVVGVPSLFVMPVGSTPPNPLELVERpafalLIRELCSKFDHVVVDTPA--------AELGADASVIAARCGAAIV 257
Cdd:pfam01656 80 GGLDLIPGNIDLEKFEKELLGPRKEERLRE-----ALEALKEDYDYVIIDGAPglgellrnALIAADYVIIPLEPEVILV 154
|
170 180 190
....*....|....*....|....*....|..
gi 1525821860 258 VARKDASRVASlqDMVAVMSGSPVRFAGVVMN 289
Cdd:pfam01656 155 EDAKRLGGVIA--ALVGGYALLGLKIIGVVLN 184
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
122-250 |
1.09e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 42.15 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADmrsPRqhdvfnlnnnaGLSGILSGRAESSVIQQVVGVPslfvmp 201
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD---PQ-----------GSALDWAAAREDERPFPVVGLA------ 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1525821860 202 vgstppnplelveRPAFALLIRELCSKFDHVVVDTP--AAELGADAsVIAA 250
Cdd:NF041546 62 -------------RPTLHRELPSLARDYDFVVIDGPprAEDLARSA-IKAA 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
16-290 |
1.95e-86 |
|
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF).
Pssm-ID: 132074 [Multi-domain] Cd Length: 274 Bit Score: 259.80 E-value: 1.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 16 DRSIGAIISETRNLSADQVERILAYQLEKGVRFGEAAISLGFASADDVLFALAQQFHYPYAAEEQRKLSPELVTFNQPFS 95
Cdd:TIGR03029 2 DANIGKVLLDAGKLSEDEAERILRLQKQENIRFGEAALRLGLINEDDIRQALSRQFEYPYLPPNDGSFSPDLIAAYQPFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 96 LQSEAFRATRSQITMRvWSDsEPRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGL 175
Cdd:TIGR03029 82 PQVEALRALRSQLMLR-WFS-EGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNFKLSEQRGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 176 SGILSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAA 255
Cdd:TIGR03029 160 SDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQIVATRARGT 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1525821860 256 IVVARKDASRVASLQDMVAVMSGSPVRFAGVVMNE 290
Cdd:TIGR03029 240 LIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ 274
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
99-289 |
2.93e-55 |
|
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: 176.99 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 99 EAFRATRSQITMRVwsDSEPRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGLSGI 178
Cdd:cd05387 1 EAFRTLRTNLLFAG--SDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 179 LSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAAIVV 258
Cdd:cd05387 79 LSGQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLV 158
|
170 180 190
....*....|....*....|....*....|.
gi 1525821860 259 ARKDASRVASLQDMVAVMSGSPVRFAGVVMN 289
Cdd:cd05387 159 VRAGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
115-289 |
2.63e-50 |
|
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: 167.67 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 115 DSEPRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGLSGILSGRAESSVIQQVVGV 194
Cdd:COG0489 88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 195 PSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAAIVVARKDASRVASLQDMVA 274
Cdd:COG0489 168 EGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALE 247
|
170
....*....|....*
gi 1525821860 275 VMSGSPVRFAGVVMN 289
Cdd:COG0489 248 MLEKAGVPVLGVVLN 262
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
99-289 |
6.75e-42 |
|
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: 143.35 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 99 EAFRATRSQITMrvwSDSEPRRaLAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNN-NAGLSG 177
Cdd:TIGR01007 1 EYYNAIRTNIQF---SGAEIKV-LLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 178 ILSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVIAARCGAAIV 257
Cdd:TIGR01007 77 FLSGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASIL 156
|
170 180 190
....*....|....*....|....*....|..
gi 1525821860 258 VARKDASRVASLQDMVAVMSGSPVRFAGVVMN 289
Cdd:TIGR01007 157 VTDAGKIKKREVKKAKEQLEQAGSNFLGVVLN 188
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
80-260 |
4.08e-28 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 113.71 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 80 QRKLSPELVTFNQPFSLQSEAFRATRSQITMRVWSDSEPRRALAVVSPEIGdgKTYFAANLAVVLAQLGGRTLLVDADMR 159
Cdd:PRK11519 489 KRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIG--KTFVCANLAAVISQTNKRVLLIDCDMR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 160 SPRQHDVFNLNNNAGLSGILSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAA 239
Cdd:PRK11519 567 KGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPI 646
|
170 180
....*....|....*....|.
gi 1525821860 240 ELGADASVIAARCGAAIVVAR 260
Cdd:PRK11519 647 LAVTDAAIVGRHVGTTLMVAR 667
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
91-289 |
1.94e-26 |
|
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: 108.65 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 91 NQPFSLQSEAFRATRSQITMRVwSDSEpRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLN 170
Cdd:TIGR01005 527 DAPRSTFAEAFRNAKLACDFAL-ADAE-NNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKA 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 171 NNAGLSGILSGRAESSVIQQVVGVPSLFVMPVGST---PPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASV 247
Cdd:TIGR01005 605 PKPGLLDLLAGEASIEAGIHRDQRPGLAFIAAGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAA 684
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525821860 248 IAARCGAAIVVARKDASRVASLQDMVAVMSGSPVRFAGVVMN 289
Cdd:TIGR01005 685 FAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFN 726
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
91-290 |
7.20e-24 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 101.14 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 91 NQPFSLQSEAFRATRSQI--TMRvwsDSEpRRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFN 168
Cdd:PRK09841 505 DNPADSAVEAVRALRTSLhfAMM---ETE-NNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFT 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 169 LNNNAGLSGILSGRAESSVIQQVVGVPSLFVMPVGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASVI 248
Cdd:PRK09841 581 VSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVV 660
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525821860 249 AARCGAAIVVARKDASRVASLQDMVAVMSGSPVRFAGVVMNE 290
Cdd:PRK09841 661 GRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNG 702
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
136-289 |
1.99e-17 |
|
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: 79.16 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 136 FAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGLSGILSGRAE-SSVIQQvvGVPSLFVMPVGSTPPNPLELVE 214
Cdd:COG0455 2 VAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADlEDAIVQ--GPGGLDVLPGGSGPAELAELDP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525821860 215 RPAFALLIRELCSKFDHVVVDTPAAeLGADASVIAARCGAAIVVARkdaSRVASLQDMVAVM----SGSPVRFAGVVMN 289
Cdd:COG0455 80 EERLIRVLEELERFYDVVLVDTGAG-ISDSVLLFLAAADEVVVVTT---PEPTSITDAYALLkllrRRLGVRRAGVVVN 154
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
120-276 |
1.36e-14 |
|
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: 72.84 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 120 RALAVVSPEIGDGKTYFAANLAVVLAQLGG-RTLLVDADMRSPRQHDVFNLNNNAGLSGILS--GRAESSVIQQVVGVPS 196
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALARESGrRVLLVDLDLQFGDVALYLDLEPRRGLADALRnpDRLDETLLDRALTRHS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 197 --LFVMPvGSTPPNPLELVERPAFALLIRELCSKFDHVVVDTPAAELGADASViAARCGAAIVVARKDasrVASLQDMVA 274
Cdd:COG4963 183 sgLSVLA-APADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAA-LEAADEVVLVTEPD---LPSLRNAKR 257
|
..
gi 1525821860 275 VM 276
Cdd:COG4963 258 LL 259
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
120-259 |
1.98e-10 |
|
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: 59.51 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 120 RALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNNAGLSGILSGRAE-SSVIqqVVGVPSLF 198
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSlEDII--VEGPEGLD 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 199 VMPVGSTPPnplELVERPA--FALLIRE---LCSKFDHVVVDTPAaelGADASVI----AARCGaaIVVA 259
Cdd:cd02038 79 IIPGGSGME---ELANLDPeqKAKLIEElssLESNYDYLLIDTGA---GISRNVLdfllAADEV--IVVT 140
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
120-269 |
9.01e-10 |
|
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: 57.60 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 120 RALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDAD--MRsprqhdvfNLNNNAGLSG--------ILSGRAEssvIQ 189
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADigLR--------NLDLILGLENrivytlvdVLEGECR---LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 190 QVV----GVPSLFVMPVGSTPPNplELVERPAFALLIRELCSKFDHVVVDTPAA-ELGADASVIAARcgAAIVV------ 258
Cdd:cd02036 70 QALikdkRWENLYLLPASQTRDK--DALTPEKLEELVKELKDSFDFILIDSPAGiESGFINAIAPAD--EAIIVtnpeis 145
|
170
....*....|.
gi 1525821860 259 ARKDASRVASL 269
Cdd:cd02036 146 SVRDADRVIGL 156
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
120-291 |
3.02e-09 |
|
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: 56.28 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 120 RALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNN-NAGLSGILSGRAEssvIQQVV--GVPS 196
Cdd:TIGR01969 1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDkPVTLHDVLAGEAD---IKDAIyeGPFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 197 LFVMPVGSTppnpLELVERPAFALL---IRELCSKFDHVVVDTPAAeLGADA-SVIAARCGAAIVVARKDASRVASLQ-D 271
Cdd:TIGR01969 78 VKVIPAGVS----LEGLRKADPDKLedvLKEIIDDTDFLLIDAPAG-LERDAvTALAAADELLLVVNPEISSITDALKtK 152
|
170 180
....*....|....*....|
gi 1525821860 272 MVAVMSGSPVrfAGVVMNEY 291
Cdd:TIGR01969 153 IVAEKLGTAI--LGVVLNRV 170
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
122-289 |
1.84e-08 |
|
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: 53.89 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDAD-MRS--------PRQHDVFNlNNNAGLSG-------ILSGRAES 185
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpQSNnssvegleGDIAPALQ-ALAEGLKGrvnldpiLLKEKSDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 186 SVIQQVVGVPSLFVMPVGSTPPNPLELVERpafalLIRELCSKFDHVVVDTPA--------AELGADASVIAARCGAAIV 257
Cdd:pfam01656 80 GGLDLIPGNIDLEKFEKELLGPRKEERLRE-----ALEALKEDYDYVIIDGAPglgellrnALIAADYVIIPLEPEVILV 154
|
170 180 190
....*....|....*....|....*....|..
gi 1525821860 258 VARKDASRVASlqDMVAVMSGSPVRFAGVVMN 289
Cdd:pfam01656 155 EDAKRLGGVIA--ALVGGYALLGLKIIGVVLN 184
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
132-291 |
2.30e-06 |
|
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: 47.93 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 132 GKTYFAANLAVVLAQLGGRTLLVDADMrsprQHDV---FNLNNNA---GLSGILSGRAESSVIQQVVGVPSLFVMPvgST 205
Cdd:COG1192 14 GKTTTAVNLAAALARRGKRVLLIDLDP----QGNLtsgLGLDPDDldpTLYDLLLDDAPLEDAIVPTEIPGLDLIP--AN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 206 PP---NPLELVERPA----FALLIRELCSKFDHVVVDTPAAeLG--ADASVIAARcgAAIVVARKDASRVASLQDMVAVM 276
Cdd:COG1192 88 IDlagAEIELVSRPGrelrLKRALAPLADDYDYILIDCPPS-LGllTLNALAAAD--SVLIPVQPEYLSLEGLAQLLETI 164
|
170 180
....*....|....*....|.
gi 1525821860 277 S------GSPVRFAGVVMNEY 291
Cdd:COG1192 165 EevredlNPKLEILGILLTMV 185
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
106-269 |
4.75e-06 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 47.07 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 106 SQITMRVWSDSEP-RRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMrSPRQHD-VFNLNNNAGLSG--ILSG 181
Cdd:CHL00175 1 EQITTEDKEKSATmSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI-GLRNLDlLLGLENRVLYTAmdVLEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 182 --RAESSVIQQVVGvPSLFVMPVGStppNPLEL-VERPAFALLIRELCSK-FDHVVVDTPAaelGADASVIAARCGA--A 255
Cdd:CHL00175 80 ecRLDQALIRDKRW-KNLSLLAISK---NRQRYnVTRKNMNMLVDSLKNRgYDYILIDCPA---GIDVGFINAIAPAqeA 152
|
170 180
....*....|....*....|
gi 1525821860 256 IVV------ARKDASRVASL 269
Cdd:CHL00175 153 IVVttpeitAIRDADRVAGL 172
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
120-157 |
1.03e-05 |
|
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: 43.57 E-value: 1.03e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1525821860 120 RALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDAD 157
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
122-279 |
1.85e-05 |
|
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: 45.03 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDvFNL--NNNAGLSG-ILSGRAESSVIQQvvGVPSLF 198
Cdd:TIGR03371 4 IAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLH-FGMdwSVRDGWARaLLNGADWAAAAYR--SPDGVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 199 VMPVGStppnpLELVERPAF----ALLIRELCSKFD----HVV-VDTPAAELGADASVIAArCGAAIVVARKDASRVASL 269
Cdd:TIGR03371 81 FLPYGD-----LSADEREAYqahdAGWLARLLQQLDlaarDWVlIDLPRGPSPITRQALAA-ADLVLVVVNADAACYATL 154
|
170
....*....|.
gi 1525821860 270 -QDMVAVMSGS 279
Cdd:TIGR03371 155 hQLALALFAGS 165
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
132-157 |
2.22e-05 |
|
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: 43.30 E-value: 2.22e-05
10 20
....*....|....*....|....*.
gi 1525821860 132 GKTYFAANLAVVLAQLGGRTLLVDAD 157
Cdd:cd02042 13 GKTTLAVNLAAALALRGKRVLLIDLD 38
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
122-250 |
1.09e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 42.15 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADmrsPRqhdvfnlnnnaGLSGILSGRAESSVIQQVVGVPslfvmp 201
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD---PQ-----------GSALDWAAAREDERPFPVVGLA------ 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1525821860 202 vgstppnplelveRPAFALLIRELCSKFDHVVVDTP--AAELGADAsVIAA 250
Cdd:NF041546 62 -------------RPTLHRELPSLARDYDFVVIDGPprAEDLARSA-IKAA 98
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
122-273 |
1.19e-04 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 42.14 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRsprqhdvfnlnnnaglsgilsGRAESSVIQQVVGVPSLFVMP 201
Cdd:PHA02518 3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQ---------------------GSSTDWAEAREEGEPLIPVVR 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525821860 202 VGSTPPNPLElverpafallirELCSKFDHVVVDTPAAELGADASVIAArCGAAIVVARKDASRVASLQDMV 273
Cdd:PHA02518 62 MGKSIRADLP------------KVASGYDYVVVDGAPQDSELARAALRI-ADMVLIPVQPSPFDIWAAPDLV 120
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
122-172 |
1.62e-04 |
|
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: 41.72 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1525821860 122 LAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNN 172
Cdd:cd02037 3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGK 53
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
130-237 |
4.49e-04 |
|
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: 40.26 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 130 GDGKTYFAANLAVVLAQLGGRTLLVDADMR----SPRQHDVFNLNNNaglsgILSGRAESSVIQQVV---GVPSLFVMPV 202
Cdd:pfam13614 12 GVGKTTTSVNLAAALAKKGKKVLLIDLDPQgnatSGLGIDKNNVEKT-----IYELLIGECNIEEAIiktVIENLDLIPS 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1525821860 203 G---STPPNPLELVERPAFAL--LIRELCSKFDHVVVDTP 237
Cdd:pfam13614 87 NidlAGAEIELIGIENRENILkeALEPVKDNYDYIIIDCP 126
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
120-238 |
4.57e-04 |
|
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: 40.72 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525821860 120 RALAVVSPEIGDGKTYFAANLAVVLAQL-GGRTLLVDADMRSPRQHDVFNLNNNAGLSGILS--GRAESSVIQQVVG--V 194
Cdd:cd03111 1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQnlDRLDRTLLDSAVTrhS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1525821860 195 PSLFVMPVgstpPNPLELVER---PAFALLIRELCSKFDHVVVDTPA 238
Cdd:cd03111 81 SGLSLLPA----PQELEDLEAlgaEQVDKLLQVLRAFYDHIIVDLGH 123
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
119-172 |
2.27e-03 |
|
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: 38.59 E-value: 2.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1525821860 119 RRALAVVSPEIGDGKTYFAANLAVVLAQLGGRTLLVDADMRSPRQHDVFNLNNN 172
Cdd:pfam10609 3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGE 56
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
121-164 |
8.39e-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: 8.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1525821860 121 ALAVVSPEIGDGKTYFAANLAVVLaqlgGRTLLVDADMRSPRQH 164
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLH 40
|
|
| |
