|
Name |
Accession |
Description |
Interval |
E-value |
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-203 |
6.27e-68 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 207.36 E-value: 6.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITY----KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQT 79
Cdd:COG4619 3 LEGLSFrvggKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDGTIKDNLLMGLRFSEKPFpNDDALQGALTTVSLDKK-LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:COG4619 83 PALWGGTVRDNLPFPFQLRERKF-DRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 159 DGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG4619 162 DPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-219 |
8.30e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 188.82 E-value: 8.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:COG4987 350 VLDGLS---------LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLDK-----------KLEDNASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:COG4987 421 FDTTLRENLRLA-----RPDATDEELWAALERVGLGDwlaalpdgldtWLGEGGRRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 152 DEPTSALDGDTERRVMKqfTLLAREKKKTVIFITHsQQLPEEIADDIIEIskTNG-----ATRKEVLSIEGRY 219
Cdd:COG4987 496 DEPTEGLDAATEQALLA--DLLEALAGRTVLLITH-RLAGLERMDRILVL--EDGriveqGTHEELLAQNGRY 563
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-199 |
6.57e-55 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 183.81 E-value: 6.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP 81
Cdd:COG4988 351 PALDGLS---------LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLDK-----------KLEDNASSLSGGEKQRLAFARIILMDPPVYL 150
Cdd:COG4988 422 LFAGTIRENLRLG-----RPDASDEELEAALEAAGLDEfvaalpdgldtPLGEGGRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487961256 151 LDEPTSALDGDTERRVMKqfTLLAREKKKTVIFITHSQQLpEEIADDII 199
Cdd:COG4988 497 LDEPTAHLDAETEAEILQ--ALRRLAKGRTVILITHRLAL-LAQADRIL 542
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-219 |
9.42e-53 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 180.03 E-value: 9.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITY------KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLG 77
Cdd:COG2274 476 LENVSFrypgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 QTPPIFDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLDK-----------KLEDNASSLSGGEKQRLAFARIILMDP 146
Cdd:COG2274 556 QDVFLFSGTIRENITLG-----DPDATDEEIIEAARLAGLHDfiealpmgydtVVGEGGSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 147 PVYLLDEPTSALDGDTERRVMKqfTLLAREKKKTVIFITHSQQLPeEIADDIIEISktNGA-----TRKEVLSIEGRY 219
Cdd:COG2274 631 RILILDEATSALDAETEAIILE--NLRRLLKGRTVIIIAHRLSTI-RLADRIIVLD--KGRivedgTHEELLARKGLY 703
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-205 |
6.35e-50 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 161.96 E-value: 6.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLN---DLQS--PTSGTIEYNGKSI--LDYPPIQLRREVVM 75
Cdd:cd03260 15 ALKDIS---------LDIPKGEITALIGPSGCGKSTLLRLLNrlnDLIPgaPDEGEVLLDGKDIydLDVDVLELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 76 LGQTPPIFDGTIKDNLLMGLRFS-EKPFPNDDAL-QGALTTVSLDKKLED--NASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:cd03260 86 VFQKPNPFPGSIYDNVAYGLRLHgIKLKEELDERvEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 152 DEPTSALDGDTERRVMKqftLLAREKKK-TVIFITHSQQLPEEIADD--------IIEISKTN 205
Cdd:cd03260 166 DEPTSALDPISTAKIEE---LIAELKKEyTIVIVTHNMQQAARVADRtafllngrLVEFGPTE 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-201 |
9.16e-50 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 159.86 E-value: 9.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:cd03228 17 VLKDVS---------LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLmglrfsekpfpnddalqgalttvsldkklednasslSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT 162
Cdd:cd03228 88 FSGTIRENIL------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 163 ERRVMKqfTLLAREKKKTVIFITHSQQLpEEIADDIIEI 201
Cdd:cd03228 132 EALILE--ALRALAKGKTVIVIAHRLST-IRDADRIIVL 167
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-202 |
3.38e-48 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 157.27 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL----RREVVMLG 77
Cdd:cd03255 18 QALKGVS---------LSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 QTP---PIFdgTIKDNLLMGLRFSEKPFPNDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDE 153
Cdd:cd03255 89 QSFnllPDL--TALENVELPLLLAGVPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487961256 154 PTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLpEEIADDIIEIS 202
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELR 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-203 |
1.85e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 155.95 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP- 81
Cdd:COG1122 16 ALDDVS---------LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 -IFDGTIKDNLLMGLRfsekpfpN--------DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:COG1122 87 qLFAPTVEEDVAFGPE-------NlglpreeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487961256 153 EPTSALDGDTERRVMKQFTLLAREkKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-186 |
1.66e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 161.49 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:COG1132 355 VLKDIS---------LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLD---KKLED--------NASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:COG1132 426 FSGTIRENIRYG-----RPDATDEEVEEAAKAAQAHefiEALPDgydtvvgeRGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190
....*....|....*....|....*....|....*
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLAREkkKTVIFITH 186
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMKG--RTTIVIAH 533
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-203 |
2.83e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 149.54 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP- 81
Cdd:cd03225 16 ALDDIS---------LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 -IFDGTIKDNLLMGLRFseKPFPNDDALQ---GALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:cd03225 87 qFFGPTVEEEVAFGLEN--LGLPEEEIEErveEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 158 LDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03225 165 LDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-202 |
7.55e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.04 E-value: 7.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDIT--YKD------ILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL--- 69
Cdd:COG1136 4 LLELRNLTksYGTgegevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 70 RREvvMLG---QTP---PIFdgTIKDNLLMGLRFSEKPFPNDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARII 142
Cdd:COG1136 84 RRR--HIGfvfQFFnllPEL--TALENVALPLLLAGVSRKERRErARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 143 LMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLpEEIADDIIEIS 202
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLR 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-186 |
6.04e-44 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.50 E-value: 6.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:COG1120 16 VLDDVS---------LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 -FDGTIKDNLLMG----LRFSEKPFPNDDAL-QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:COG1120 87 pFGLTVRELVALGryphLGLFGRPSAEDREAvEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190
....*....|....*....|....*....|
gi 487961256 157 ALDGDTERRVMKQFTLLAREKKKTVIFITH 186
Cdd:COG1120 167 HLDLAHQLEVLELLRRLARERGRTVVMVLH 196
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-199 |
4.58e-42 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 148.97 E-value: 4.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGlrf 97
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 seKPFPNDDALQGALTTV-----------SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:TIGR02857 420 --RPDASDAEIREALERAgldefvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 167 MKQFTLLARekKKTVIFITHSQQLPEEiADDII 199
Cdd:TIGR02857 498 LEALRALAQ--GRTVLLVTHRLALAAL-ADRIV 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-199 |
8.87e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.74 E-value: 8.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPI---QLRREVVMLGQTP-----PIFdgTIKD 89
Cdd:COG1123 286 LTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPysslnPRM--TVGD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMGLRFSEKPFPND--DALQGALTTVSLDKKLED-NASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:COG1123 364 IIAEPLRLHGLLSRAErrERVAELLERVGLPPDLADrYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI 443
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 167 MKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:COG1123 444 LNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-199 |
2.01e-41 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 140.03 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 13 LHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLL 92
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGlrfseKPFPNDDALQGALTTV-----------SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:cd03245 100 LG-----APLADDERILRAAELAgvtdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 487961256 162 TERRVMKQFTLLAREkkKTVIFITHSQQLpEEIADDII 199
Cdd:cd03245 175 SEERLKERLRQLLGD--KTLIIITHRPSL-LDLVDRII 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-199 |
2.44e-41 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 139.95 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQTP-----PIFdgTIKD 89
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQDPmsslnPRM--TIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMGLRFSEKPFPNDDALQGA---LTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERR 165
Cdd:cd03257 104 QIAEPLRIHGKLSKKEARKEAVlllLVGVGLPEEVLNRyPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 166 VMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03257 184 ILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-186 |
3.11e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 144.58 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGlrf 97
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 seKPFPNDDALQGALTTVSLDKKLEDNAS----------SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVM 167
Cdd:PRK11160 438 --APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL 515
|
170
....*....|....*....
gi 487961256 168 KQftLLAREKKKTVIFITH 186
Cdd:PRK11160 516 EL--LAEHAQNKTVLMITH 532
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-203 |
8.03e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.91 E-value: 8.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQtppifdgtikd 89
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 nllmglrfsekpfpnddalqgalttvsldkklednassLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:cd00267 81 --------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 170 FTLLArEKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd00267 123 LRELA-EEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-189 |
8.14e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.09 E-value: 8.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLN---DLQsP---TSGTIEYNGKSILD--YPPIQLRREVV 74
Cdd:COG1117 26 ALKDIN---------LDIPENKVTALIGPSGCGKSTLLRCLNrmnDLI-PgarVEGEILLDGEDIYDpdVDVVELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 75 MLGQTPPIFDGTIKDNLLMGLRFSEKPFPN--DDALQGALTTVSL-----DKkLEDNASSLSGGEKQRLAFARIILMDPP 147
Cdd:COG1117 96 MVFQKPNPFPKSIYDNVAYGLRLHGIKSKSelDEIVEESLRKAALwdevkDR-LKKSALGLSGGQQQRLCIARALAVEPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487961256 148 VYLLDEPTSALDGDTERRVMKqftLLAREKKK-TVIFITHS-QQ 189
Cdd:COG1117 175 VLLMDEPTSALDPISTAKIEE---LILELKKDyTIVIVTHNmQQ 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-199 |
2.29e-39 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 134.58 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPP--IQLRREVVMLGQTP 80
Cdd:cd03262 15 VLKGID---------LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVGMVFQQF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 PIFDG-TIKDNLLMGLRFSEKpFPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:cd03262 86 NLFPHlTVLENITLAPIKVKG-MSKAEAEERAlelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 157 ALDGDTER---RVMKQftlLAREkKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03262 165 ALDPELVGevlDVMKD---LAEE-GMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-156 |
3.45e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.00 E-value: 3.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487961256 97 FSEKPFPNDDA-LQGALTTVSL----DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:pfam00005 86 LKGLSKREKDArAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-199 |
7.10e-39 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 134.23 E-value: 7.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPI---QLRREVVMLGQT 79
Cdd:cd03256 16 ALKDVS---------LSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDG-TIKDNLLMGlRFSEKPF---------PND--DALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPP 147
Cdd:cd03256 87 FNLIERlSVLENVLSG-RLGRRSTwrslfglfpKEEkqRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 487961256 148 VYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIV 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-199 |
1.21e-38 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 132.64 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIqlRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVAENIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAR 175
Cdd:cd03259 99 LRGVPKAEiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQR 178
|
170 180
....*....|....*....|....
gi 487961256 176 EKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03259 179 ELGITTIYVTHDQEEALALADRIA 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-199 |
1.32e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.20 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYP--PIQLRREVVMLGQTP 80
Cdd:COG1126 16 VLKGIS---------LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdINKLRRKVGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 PIF-DGTIKDNLLMGLRFSEKpFPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:COG1126 87 NLFpHLTVLENVTLAPIKVKK-MSKAEAEERAmelLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 157 ALD----GDTErRVMKQftlLAREkKKTVIFITHSQQLPEEIADDII 199
Cdd:COG1126 166 ALDpelvGEVL-DVMRD---LAKE-GMTMVVVTHEMGFAREVADRVV 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-199 |
1.50e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 131.16 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 5 KDITYKDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI--LDYPPIQLRREVVMLGQTPPI 82
Cdd:cd03229 8 KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGMVFQDFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDG-TIKDNLLMGLrfsekpfpnddalqgalttvsldkklednasslSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:cd03229 88 FPHlTVLENIALGL---------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 487961256 162 TERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVV 172
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-203 |
1.52e-38 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 133.44 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLGQTPP 81
Cdd:COG4555 15 PALKDVS---------FTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDG-TIKDNL-----LMGLRFSEKPFPNDDALQgaltTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:COG4555 85 LYDRlTVRENIryfaeLYGLFDEELKKRIEELIE----LLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 487961256 156 SALDGDTeRRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG4555 161 NGLDVMA-RRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-199 |
2.42e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.29 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsildyPPIQLRREVVMLGQTPPI 82
Cdd:COG1116 26 ALDDVS---------LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTGPGPDRGVVFQEPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FD-GTIKDNLLMGLRFSEKPFPNDDAL-QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDG 160
Cdd:COG1116 92 LPwLTVLDNVALGLELRGVPKAERRERaRELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487961256 161 DTeRRVMKQFTL-LAREKKKTVIFITHSqqlPEE---IADDII 199
Cdd:COG1116 172 LT-RERLQDELLrLWQETGKTVLFVTHD---VDEavfLADRVV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-203 |
2.49e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.49 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYVPQEPALYPDlTVRENLRFFAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPNDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeRRVMKQFTLLAR 175
Cdd:COG1131 100 LYGLPRKEARErIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA-RRELWELLRELA 178
|
170 180 190
....*....|....*....|....*....|
gi 487961256 176 EKKKTVIFITHsqQLPE--EIADDIIEISK 203
Cdd:COG1131 179 AEGKTVLLSTH--YLEEaeRLCDRVAIIDK 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-186 |
8.26e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.48 E-value: 8.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQtpp 81
Cdd:cd03214 13 TVLDDLS---------LSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 ifdgtikdnllmglrfsekpfpnddalqgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180
....*....|....*....|....*
gi 487961256 162 TERRVMKQFTLLAREKKKTVIFITH 186
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLH 156
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-219 |
9.44e-38 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 131.20 E-value: 9.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP 81
Cdd:cd03253 15 PVLKDVSFT---------IPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLD---KKLEDNASS--------LSGGEKQRLAFARIILMDPPVYL 150
Cdd:cd03253 86 LFNDTIGYNIRYG-----RPDATDEEVIEAAKAAQIHdkiMRFPDGYDTivgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 151 LDEPTSALDGDTERRVMKQFTLLAreKKKTVIFITHsqQLPEEI-ADDIIEISKTNGA---TRKEVLSIEGRY 219
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVS--KGRTTIVIAH--RLSTIVnADKIIVLKDGRIVergTHEELLAKGGLY 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-186 |
1.19e-37 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 130.74 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGlRF 97
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYG-KP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 SEKPFPNDDALQGALTT---VSLDKKLE----DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkQF 170
Cdd:cd03249 103 DATDEEVEEAAKKANIHdfiMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV--QE 180
|
170
....*....|....*.
gi 487961256 171 TLLAREKKKTVIFITH 186
Cdd:cd03249 181 ALDRAMKGRTTIVIAH 196
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-202 |
1.87e-37 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 129.83 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITYK----DILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQT 79
Cdd:PRK10247 10 LQNVGYLagdaKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDGTIKDNLLMGLRFSEKPfPNDDALQGALTTVSLDKK-LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:PRK10247 90 PTLFGDTVYDNLIFPWQIRNQQ-PDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 159 DGDTERRVMKQFTLLAREKKKTVIFITHSQqlpEEI--ADDIIEIS 202
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDK---DEInhADKVITLQ 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-212 |
2.03e-37 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 129.90 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsildyPPIQLRREVVMLGQTPPIFD-GTIKDNLLMGLR 96
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDRGYVFQQDALLPwLTVLDNVALGLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeRRVMKQFTL-LA 174
Cdd:cd03293 100 LQGVPKAEaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT-REQLQEELLdIW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487961256 175 REKKKTVIFITHSqqLPEEI--ADDIIEISKTNGATRKEV 212
Cdd:cd03293 179 RETGKTVLLVTHD--IDEAVflADRVVVLSARPGRIVAEV 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-187 |
1.18e-36 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 134.41 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGlrf 97
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA--- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 seKPFPNDDALQGALTTVSL-----------DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:TIGR02868 433 --RPDATDEELWAALERVGLadwlralpdglDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
170 180
....*....|....*....|.
gi 487961256 167 MKqfTLLAREKKKTVIFITHS 187
Cdd:TIGR02868 511 LE--DLLAALSGRTVVLITHH 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-199 |
1.49e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.88 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPT---SGTIEYNGKSILDYPPIQLRREVVMLGQTPP--IFDGTIKDNLL 92
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQDPMtqLNPVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLRFSEKPFPNDDAL-QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFT 171
Cdd:COG1123 107 EALENLGLSRAEARARvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLR 186
|
170 180
....*....|....*....|....*...
gi 487961256 172 LLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:COG1123 187 ELQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-204 |
2.08e-36 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.88 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsildyPPIQLRREVVMLGQTPPI 82
Cdd:cd03235 14 VLEDVS---------FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 ---FDGTIKDNLLMGLRFSEKPFPN------DDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDE 153
Cdd:cd03235 80 drdFPISVRDVVLMGLYGHKGLFRRlskadkAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 154 PTSALDGDTERRVMkqfTLLA--REKKKTVIFITHSQQLPEEIADDIIEISKT 204
Cdd:cd03235 159 PFAGVDPKTQEDIY---ELLRelRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-201 |
4.17e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 127.23 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTP-- 80
Cdd:COG1124 20 VLKDVS---------LEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPya 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 ---PIFdgTIKDNLLMGLRFSEKPFPNDDALQgALTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:COG1124 91 slhPRH--TVDRILAEPLRIHGLPDREERIAE-LLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALILEPELLLLDEPTS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 157 ALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:COG1124 168 ALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-186 |
4.91e-36 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 133.71 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 6 DITYK-----DILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTP 80
Cdd:TIGR01193 478 DVSYSygygsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 PIFDGTIKDNLLMGlrfsEKPFPNDDALQGALTTVSLDKKLE-----------DNASSLSGGEKQRLAFARIILMDPPVY 149
Cdd:TIGR01193 558 YIFSGSILENLLLG----AKENVSQDEIWAACEIAEIKDDIEnmplgyqtelsEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190
....*....|....*....|....*....|....*..
gi 487961256 150 LLDEPTSALDGDTERRVMKQFTLLareKKKTVIFITH 186
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNL---QDKTIIFVAH 667
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-216 |
9.05e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.97 E-value: 9.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILD------YPPiQLR------ 70
Cdd:COG1121 21 VLEDVS---------LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigYVP-QRAevdwdf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 71 ----REVVMLGQTPPIfdgtikdNLLMGLRFSEKpfpndDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDP 146
Cdd:COG1121 91 pitvRDVVLMGRYGRR-------GLFRRPSRADR-----EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487961256 147 PVYLLDEPTSALDGDTERRVMKQFTLLAREkKKTVIFITHSQQLPEEIADDIIEISKTNGA--TRKEVLSIE 216
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAhgPPEEVLTPE 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
26-202 |
1.06e-35 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 124.90 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDyPPIQLRREVVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPN 104
Cdd:COG4133 31 LALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENLRFWAALYGLRADR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 105 DDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMkqfTLLA--REKKKTVI 182
Cdd:COG4133 110 EAIDE-ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA---ELIAahLARGGAVL 185
|
170 180
....*....|....*....|
gi 487961256 183 FITHsQQLPEEiADDIIEIS 202
Cdd:COG4133 186 LTTH-QPLELA-AARVLDLG 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-198 |
1.32e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 125.88 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDG-TIKDN--LLMG 94
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVEENiaLVPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 LRFSEKPFPNDDALQgALTTVSLDKK--LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTL 172
Cdd:cd03295 102 LLKWPKEKIRERADE-LLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKR 180
|
170 180
....*....|....*....|....*.
gi 487961256 173 LAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:cd03295 181 LQQELGKTIVFVTHDIDEAFRLADRI 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-199 |
2.57e-35 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 123.73 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 5 KDITYKDILHIPYLQIQKEKTTCIIGESGSGKSTLLR-MLNDLQsPTSGTIEYNGKsiLDYPPiqlrrevvmlgQTPPIF 83
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPGS--IAYVS-----------QEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 84 DGTIKDNLLMGLRFSEKPFpnDDALQGAlttvSLDKKLE-----------DNASSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:cd03250 79 NGTIRENILFGKPFDEERY--EKVIKAC----ALEPDLEilpdgdlteigEKGINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 153 EPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEiADDII 199
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIV 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-186 |
3.70e-35 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 124.26 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:cd03254 18 VLKDIN---------FSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLD---KKLED--------NASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:cd03254 89 FSGTIMENIRLG-----RPNATDEEVIEAAKEAGAHdfiMKLPNgydtvlgeNGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 487961256 152 DEPTSALDGDTERRVmkQFTLLAREKKKTVIFITH 186
Cdd:cd03254 164 DEATSNIDTETEKLI--QEALEKLMKGRTSIIIAH 196
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-199 |
4.42e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.10 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDITYK---DILHIPyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLG 77
Cdd:COG3840 1 MLRLDDLTYRygdFPLRFD-LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 QTPPIFDG-TIKDNLLMGLRFSEKPFPND-DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGLRPGLKLTAEQrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 487961256 156 SALDgdterRVMKQFTL-----LAREKKKTVIFITHSqqlPEE---IADDII 199
Cdd:COG3840 158 SALD-----PALRQEMLdlvdeLCRERGLTVLMVTHD---PEDaarIADRVL 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-204 |
8.87e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.73 E-value: 8.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLN---DL--QSPTSGTIEYNGKSIldYPP----IQLRREVVMLGQTP 80
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLnpEVTITGSIVYNGHNI--YSPrtdtVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 PIFDGTIKDNLLMGLRFS---EKPFPN---DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEP 154
Cdd:PRK14239 96 NPFPMSIYENVVYGLRLKgikDKQVLDeavEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 155 TSALDGDTERRVmkQFTLLAREKKKTVIFITHSQQLPEEIAD--------DIIEISKT 204
Cdd:PRK14239 176 TSALDPISAGKI--EETLLGLKDDYTMLLVTRSMQQASRISDrtgffldgDLIEYNDT 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-199 |
5.18e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.05 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIqlRREVVMLGQTPP 81
Cdd:COG3842 19 TALDDVS---------LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDG-TIKDNLLMGLRFseKPFPNDDA---LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:COG3842 88 LFPHlTVAENVAFGLRM--RGVPKAEIrarVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 158 LDGDTeRRVMkQFTLLA--REKKKTVIFITHSQqlpEE---IADDII 199
Cdd:COG3842 166 LDAKL-REEM-REELRRlqRELGITFIYVTHDQ---EEalaLADRIA 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-203 |
5.80e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 119.42 E-value: 5.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLGQTPPI 82
Cdd:cd03230 15 ALDDIS---------LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLPEEPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDG-TIKDNLlmglrfsekpfpnddalqgalttvsldkklednasSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:cd03230 85 YENlTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 487961256 162 TeRRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03230 130 S-RREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-186 |
7.69e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 120.80 E-value: 7.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP 81
Cdd:cd03251 16 PVLRDIS---------LDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSL-----------DKKLEDNASSLSGGEKQRLAFARIILMDPPVYL 150
Cdd:cd03251 87 LFNDTVAENIAYG-----RPGATREEVEEAARAANAhefimelpegyDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 487961256 151 LDEPTSALDGDTERRVMKQFTLLAreKKKTVIFITH 186
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLM--KNRTTFVIAH 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-203 |
9.83e-34 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 120.76 E-value: 9.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITykdiLHIPYLQIqkektTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQTP 80
Cdd:cd03258 21 LKDVS----LSVPKGEI-----FGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 PIFDG-TIKDNL-----LMGLRFSEKPFPNDDALQgaltTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEP 154
Cdd:cd03258 92 NLLSSrTVFENValpleIAGVPKAEIEERVLELLE----LVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487961256 155 TSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03258 168 TSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-199 |
1.43e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.28 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITYK-----DILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIldyPPIQLRREVVMLGQ 78
Cdd:cd03226 2 IENISFSykkgtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 79 TP--PIFDGTIKDNLLMGLRfsEKPFPNDDAlQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLK--ELDAGNEQA-ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487961256 157 ALDGDTERRVMKQFTLLAREkKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-201 |
2.65e-33 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 118.75 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIqlRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPND-DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgDTERRVMKQFTL-LA 174
Cdd:cd03298 97 PGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAEMLDLVLdLH 175
|
170 180
....*....|....*....|....*..
gi 487961256 175 REKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-199 |
3.30e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 119.46 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqlrREVVMLG-----QTPPIFDG-TIKDNL 91
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP----HEIARLGigrtfQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 LMGLRFSEKPFPNDDALQG-----------ALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdG 160
Cdd:cd03219 97 MVAAQARTGSGLLLARARReereareraeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL-N 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 161 DTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03219 176 PEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-199 |
1.32e-32 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 117.60 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQT 79
Cdd:cd03261 15 VLKGVD---------LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDG-TIKDN----LLMGLRFSEKPFpnDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEP 154
Cdd:cd03261 86 GALFDSlTVFENvafpLREHTRLSEEEI--REIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487961256 155 TSALD----GDTERRVMKqftlLAREKKKTVIFITHsqQLPE--EIADDII 199
Cdd:cd03261 164 TAGLDpiasGVIDDLIRS----LKKELGLTSIMVTH--DLDTafAIADRIA 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-186 |
1.71e-32 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 115.87 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITY------KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLG 77
Cdd:cd03247 3 INNVSFsypeqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 QTPPIFDGTIKDNLlmGLRFSekpfpnddalqgalttvsldkklednasslsGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:cd03247 82 QRPYLFDTTLRNNL--GRRFS-------------------------------GGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180
....*....|....*....|....*....
gi 487961256 158 LDGDTERRVMKQFTLLAREkkKTVIFITH 186
Cdd:cd03247 129 LDPITERQLLSLIFEVLKD--KTLIWITH 155
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-212 |
2.15e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 122.99 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDIT-----YKDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYngksildyPPiqlRREVVM 75
Cdd:COG4178 362 ALALEDLTlrtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PA---GARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 76 LGQTPPIFDGTIKDNLLmglrfsekpFPN------DDALQGALTTVSLDK---KLEDNAS---SLSGGEKQRLAFARIIL 143
Cdd:COG4178 431 LPQRPYLPLGTLREALL---------YPAtaeafsDAELREALEAVGLGHlaeRLDEEADwdqVLSLGEQQRLAFARLLL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 144 MDPPVYLLDEPTSALDGDTERRVMKQftLLAREKKKTVIFITHSQQLpEEIADDIIEISKTNGATRKEV 212
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQL--LREELPGTTVISVGHRSTL-AAFHDRVLELTGDGSWQLLPA 567
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-203 |
8.56e-32 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 115.26 E-value: 8.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 24 KTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGLrfSEKPFP 103
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGL--QSCSFE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 104 NDDALQGALTTVSLDKKLED--------NASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgDTERRVMKQFTLLAR 175
Cdd:cd03248 119 CVKEAAQKAHAHSFISELASgydtevgeKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL--DAESEQQVQQALYDW 196
|
170 180
....*....|....*....|....*...
gi 487961256 176 EKKKTVIFITHSQQLPEEiADDIIEISK 203
Cdd:cd03248 197 PERRTVLVIAHRLSTVER-ADQILVLDG 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-203 |
1.85e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.38 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI--LDYPPI-QLRREVVMLGQT 79
Cdd:COG2884 17 ALSDVS---------LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrLKRREIpYLRRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PP-IFDGTIKDNLLMGLRFSEKPfPND--DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:COG2884 88 FRlLPDRTVYENVALPLRVTGKS-RKEirRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487961256 157 ALDGDTERRVMKqftLLAR--EKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG2884 167 NLDPETSWEIME---LLEEinRRGTTVLIATHDLELVDRMPKRVLELED 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-203 |
3.70e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 119.83 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:TIGR00958 496 VLKGLTFT---------LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGLRFSEKPFPNDDALQ-GALTTVS-----LDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:TIGR00958 567 FSGSVRENIAYGLTDTPDEEIMAAAKAaNAHDFIMefpngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 157 ALDGDTERRVMKqftlLAREKKKTVIFITHSQQLPEEiADDIIEISK 203
Cdd:TIGR00958 647 ALDAECEQLLQE----SRSRASRTVLLIAHRLSTVER-ADQILVLKK 688
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-196 |
9.88e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.72 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 17 YLQIQKEKTTCIIGESGSGKSTLLR---MLNDL--QSPTSGTIEYNGKSILD--YPPIQLRREVVMLGQTPPIFDGTIKD 89
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLipGFRVEGKVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFPKSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMGLRFSEKPFPNDDALQGALTTVSL----DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERR 165
Cdd:PRK14243 110 NIAYGARINGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLR 189
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 166 VMKQFTLLAREkkKTVIFITHSQQLPEEIAD 196
Cdd:PRK14243 190 IEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-199 |
2.27e-30 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 117.12 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGLRF 97
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 SEKPFPNDDALQGALTT-------VSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkQF 170
Cdd:TIGR02203 433 QADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV--QA 510
|
170 180
....*....|....*....|....*....
gi 487961256 171 TLLAREKKKTVIFITHSQQLPEEiADDII 199
Cdd:TIGR02203 511 ALERLMQGRTTLVIAHRLSTIEK-ADRIV 538
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-199 |
2.90e-30 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 111.61 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPP---IQLRREVVMLGQT 79
Cdd:COG1127 20 VLDGVS---------LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDG-TIKDNLLMGLR-FSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:COG1127 91 GALFDSlTVFENVAFPLReHTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 157 ALDGDTERRVMKQFTLLAREKKKTVIFITHsqQLPE--EIADDII 199
Cdd:COG1127 171 GLDPITSAVIDELIRELRDELGLTSVVVTH--DLDSafAIADRVA 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-186 |
3.33e-30 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 111.05 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:cd03244 19 VLKNISFS---------IKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLlmglrfseKPFP--NDDALQGALTTVS-----------LDKKLEDNASSLSGGEKQRLAFARIILMDPPVY 149
Cdd:cd03244 90 FSGTIRSNL--------DPFGeySDEELWQALERVGlkefveslpggLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 487961256 150 LLDEPTSALDGDTERRVMKqfTLLAREKKKTVIFITH 186
Cdd:cd03244 162 VLDEATASVDPETDALIQK--TIREAFKDCTVLTIAH 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-198 |
6.25e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 110.29 E-value: 6.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILdYPPIQLRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDElTVREHLRFYAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKP-FPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKqfTLLAR 175
Cdd:cd03263 102 LKGLPkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD--LILEV 179
|
170 180
....*....|....*....|...
gi 487961256 176 EKKKTVIFITHSQQLPEEIADDI 198
Cdd:cd03263 180 RKGRSIILTTHSMDEAEALCDRI 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-186 |
1.24e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 115.33 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQsPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGlrf 97
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 seKPFPNDDALQGALT-----------TVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:PRK11174 447 --NPDASDEQLQQALEnawvseflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180
....*....|....*....|
gi 487961256 167 MKqfTLLAREKKKTVIFITH 186
Cdd:PRK11174 525 MQ--ALNAASRRQTTLMVTH 542
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-199 |
1.24e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 112.07 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSP---TSGTIEYNGKSILDYPPIQLR----REVVMLGQTP-----PIFdg 85
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPmtslnPVM-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 86 TIKDNLLMGLRFSEKpFPNDDALQ---GALTTVSLDKKlEDNASS----LSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:COG0444 104 TVGDQIAEPLRIHGG-LSKAEAREraiELLERVGLPDP-ERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 159 DGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:COG0444 182 DVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-198 |
3.34e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 108.11 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQTPPIF-DGTIKDNLLMGLR 96
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMTVYDNIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPNDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAR 175
Cdd:cd03301 99 LRKVPKDEIDErVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQ 178
|
170 180
....*....|....*....|...
gi 487961256 176 EKKKTVIFITHSQQLPEEIADDI 198
Cdd:cd03301 179 RLGTTTIYVTHDQVEAMTMADRI 201
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-186 |
4.14e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMlgqtp 80
Cdd:COG1135 21 LDDVS---------LTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaRRKIGM----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 pIFDG-------TIKDNLLMGLRFSEKPfPND-----DALqgaLTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPV 148
Cdd:COG1135 87 -IFQHfnllssrTVAENVALPLEIAGVP-KAEirkrvAEL---LELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 149 YLLDEPTSALDGDTERRVMkqfTLLAREKKK---TVIFITH 186
Cdd:COG1135 162 LLCDEATSALDPETTRSIL---DLLKDINRElglTIVLITH 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-214 |
4.38e-29 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 113.69 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:COG4618 347 ILRGVS---------FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLlmgLRFSEkpfPNDDALQGALTTV-------SL----DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:COG4618 418 FDGTIAENI---ARFGD---ADPEKVVAAAKLAgvhemilRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLpEEIADDIIEISktNGA-----TRKEVLS 214
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSL-LAAVDKLLVLR--DGRvqafgPRDEVLA 555
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-199 |
6.93e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 6.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 6 DITYKDILHI-----PY---------LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEY------NGKSILDYP 65
Cdd:PRK13634 2 DITFQKVEHRyqyktPFerralydvnVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 66 PiqLRREVVMLGQTPP--IFDGTI-KDnllmgLRFSEKPF--PNDDALQGA---LTTVSLDKKLEDNAS-SLSGGEKQRL 136
Cdd:PRK13634 82 P--LRKKVGIVFQFPEhqLFEETVeKD-----ICFGPMNFgvSEEDAKQKAremIELVGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 137 AFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIV 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-199 |
7.34e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 108.67 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPI-QLRREVVMLGQTP 80
Cdd:TIGR04520 16 PALKNVS---------LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLwEIRKKVGMVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 pifD-----GTIKDNLLMGLrfsE-KPFPND---DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:TIGR04520 87 ---DnqfvgATVEDDVAFGL---EnLGVPREemrKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHsqqLPEEI--ADDII 199
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITH---DMEEAvlADRVI 207
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-199 |
7.40e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 107.38 E-value: 7.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQ---KEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILD------YPPIQlrREVVMLGQTPPIFDG-TI 87
Cdd:cd03297 15 LKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQ--RKIGLVFQQYALFPHlNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 88 KDNLLMGLRFSEkPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVM 167
Cdd:cd03297 93 RENLAFGLKRKR-NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|..
gi 487961256 168 KQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-159 |
8.02e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.28 E-value: 8.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDITY----KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL-RREVVM 75
Cdd:COG4559 1 MLEAENLSVrlggRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 76 LGQTPPIFDGTIKDNLLMGL--RFSEKPFPNDDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIIL------MDPP 147
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRapHGSSAAQDRQIVRE-ALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvDGGP 159
|
170
....*....|...
gi 487961256 148 VYL-LDEPTSALD 159
Cdd:COG4559 160 RWLfLDEPTSALD 172
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-203 |
1.09e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.11 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ---LRREVVMLGQ-TPPIFDGTIKDNLLM 93
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQdFRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 GLRFSEKPfPNDDA--LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMkqfT 171
Cdd:cd03292 102 ALEVTGVP-PREIRkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM---N 177
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 172 LLAREKKK--TVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03292 178 LLKKINKAgtTVVVATHAKELVDTTRHRVIALER 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-186 |
1.31e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDITY----KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVML 76
Cdd:PRK13548 2 MLEARNLSVrlggRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 77 GQTPPI-FDGTIKDNLLMGL-RFSEKPFPNDDALQGALTTVSLDkKLEDNA-SSLSGGEKQRLAFARIIL------MDPP 147
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRaPHGLSRAEDDALVAAALAQVDLA-HLAGRDyPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 148 VYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITH 186
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH 199
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-198 |
1.35e-28 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 107.32 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqLRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTVFQNYALFPHlTVFENIAFGLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FseKPFPNDDALQG---ALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeRRVMkQFTL- 172
Cdd:cd03300 99 L--KKLPKAEIKERvaeALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL-RKDM-QLELk 174
|
170 180
....*....|....*....|....*..
gi 487961256 173 -LAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:cd03300 175 rLQKELGITFVFVTHDQEEALTMSDRI 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-203 |
1.45e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 107.43 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNVAFGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 fsEKP---FPNDDALQGA----LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:cd03296 101 --VKPrseRPPEAEIRAKvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRW 178
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 170 FTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03296 179 LRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-204 |
1.73e-28 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 104.93 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIeyngksilDYPPiqlRREVVMLGQTPPIFDGTIKDNLLmglrfsekpFPNDDA 107
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPE---GEDLLFLPQRPYLPLGTLREQLI---------YPWDDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 lqgalttvsldkklednassLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKqftlLAREKKKTVIFITHS 187
Cdd:cd03223 92 --------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ----LLKELGITVISVGHR 147
|
170
....*....|....*..
gi 487961256 188 QQLpEEIADDIIEISKT 204
Cdd:cd03223 148 PSL-WKFHDRVLDLDGE 163
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-186 |
3.79e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.82 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 25 TTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGlrfseKPFPN 104
Cdd:PRK13657 363 TVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG-----RPDAT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 105 DDALQGALTTVS-----------LDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkQFTLL 173
Cdd:PRK13657 438 DEEMRAAAERAQahdfierkpdgYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV--KAALD 515
|
170
....*....|...
gi 487961256 174 AREKKKTVIFITH 186
Cdd:PRK13657 516 ELMKGRTTFIIAH 528
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-203 |
6.45e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.99 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 12 ILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPI--------QLRREVVMLGQTPPIF 83
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 84 -DGTIKDNLLMGLRFSEKPfPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGE-PKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487961256 160 GDTERRVMKQFTLLAREKKKTVIfITHSQQLPEEIADDIIEISK 203
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQ 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-188 |
7.56e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.85 E-value: 7.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqLRREVVMLGQTPPI 82
Cdd:COG3839 18 ALKDID---------LDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP--KDRNIAMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDG-TIKDNLLMGLRF-----SEKpfpnDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:COG3839 87 YPHmTVYENIAFPLKLrkvpkAEI----DRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 487961256 157 ALD----GDTeRRVMKQftlLAREKKKTVIFITHSQ 188
Cdd:COG3839 163 NLDaklrVEM-RAEIKR---LHRRLGTTTIYVTHDQ 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-203 |
8.97e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.17 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 11 DILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDyPPI---QLRREVVMLGQTPPIFDG-T 86
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVderLIRQEAGMVFQQFYLFPHlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLLMG---LRFSEKPFPNDDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:PRK09493 94 ALENVMFGplrVRGASKEEAEKQARE-LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487961256 164 RRVMKQFTLLArEKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:PRK09493 173 HEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-195 |
1.24e-27 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 104.73 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIqlRREVVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPNDD 106
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNIAYGLKKRKVDKKEIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 ALQGALTTV-SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFIT 185
Cdd:cd03299 108 RKVLEIAEMlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVT 187
|
170
....*....|
gi 487961256 186 HSQqlpEEIA 195
Cdd:cd03299 188 HDF---EEAW 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-199 |
1.87e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 104.74 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqlrREVVMLG-----QTPPIFDG-TIKDNL 91
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP----HRIARLGiartfQNPRLFPElTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 LMGLRFSEKPFPNDDALQG----------------ALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:COG0411 101 LVAAHARLGRGLLAALLRLprarreereareraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 156 SALdGDTERRVMKQFTL-LAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:COG0411 181 AGL-NPEETEELAELIRrLRDERGITILLIEHDMDLVMGLADRIV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-186 |
1.92e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.48 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP-IFDG-TIKDNLLMGL 95
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDnQFVGaTVQDDVAFGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 96 RfsEKPFPNDDAL---QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTL 172
Cdd:PRK13635 108 E--NIGVPREEMVervDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQ 185
|
170
....*....|....
gi 487961256 173 LAREKKKTVIFITH 186
Cdd:PRK13635 186 LKEQKGITVLSITH 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-205 |
3.48e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.94 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdiLHIPYLQIqkektTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsilDYPPIQLR-REVVMLGQTPP 81
Cdd:PRK10851 17 VLNDIS----LDIPSGQM-----VALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDG-TIKDNLLMGLR-FSEKPFPNDDALQGALTT----VSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:PRK10851 85 LFRHmTVFDNIAFGLTvLPRRERPNAAAIKAKVTQllemVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 156 SALDGDTE---RRVMKQftlLAREKKKTVIFITHSQQLPEEIADDIIEISKTN 205
Cdd:PRK10851 165 GALDAQVRkelRRWLRQ---LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-186 |
3.86e-27 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 107.98 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:COG5265 373 ILKGVS---------FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGlrfseKPFPNDDALQGALTTVSLD---KKLEDNASS--------LSGGEKQRLAFARIILMDPPVYLL 151
Cdd:COG5265 444 FNDTIAYNIAYG-----RPDASEEEVEAAARAAQIHdfiESLPDGYDTrvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLAREkkKTVIFITH 186
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARG--RTTLVIAH 551
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-186 |
5.39e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 103.88 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 27 CIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL----RREVVMLGQTPPIF-DGTIKDNLLMGLRfsekp 101
Cdd:cd03294 54 VIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENVAFGLE----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 fpnddaLQG------------ALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgDTERRVMK- 168
Cdd:cd03294 129 ------VQGvpraereeraaeALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRREMQd 201
|
170
....*....|....*...
gi 487961256 169 QFTLLAREKKKTVIFITH 186
Cdd:cd03294 202 ELLRLQAELQKTIVFITH 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-196 |
8.51e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 8.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDL-----QSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTP-PIFDGTIKDNL 91
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 LMGLRF-----SEKPFPN--DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTER 164
Cdd:PRK14247 104 ALGLKLnrlvkSKKELQErvRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA 183
|
170 180 190
....*....|....*....|....*....|..
gi 487961256 165 RVMKQFtlLAREKKKTVIFITHSQQLPEEIAD 196
Cdd:PRK14247 184 KIESLF--LELKKDMTIVLVTHFPQQAARISD 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-158 |
8.63e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 102.13 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ-LRREVVMLGQTPP 81
Cdd:cd03224 15 ILFGVS---------LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRR 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 82 IFDG-TIKDNLLMGLRFSEKPfPNDDALQGALTTVS-LDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:cd03224 86 IFPElTVEENLLLGAYARRRA-KRKARLERVYELFPrLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-199 |
1.03e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 100.75 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:cd03246 17 VLRNVS---------FSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLlmglrfsekpfpnddalqgalttvsldkklednassLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT 162
Cdd:cd03246 88 FSGSIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 163 ERRVMKQFTLLaREKKKTVIFITHSqqlPE--EIADDII 199
Cdd:cd03246 132 ERALNQAIAAL-KAAGATRIVIAHR---PEtlASADRIL 166
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-201 |
1.43e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.64 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITykdiLHIPylqiqKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIF 83
Cdd:PRK11176 359 LRNIN----FKIP-----AGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 84 DGTIKDNLLMGlrfSEKPFPNDDALQGALTTVSLD--KKLED--------NASSLSGGEKQRLAFARIILMDPPVYLLDE 153
Cdd:PRK11176 430 NDTIANNIAYA---RTEQYSREQIEEAARMAYAMDfiNKMDNgldtvigeNGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 487961256 154 PTSALDGDTERRVmkQFTLLAREKKKTVIFITHSQQLPEEiADDIIEI 201
Cdd:PRK11176 507 ATSALDTESERAI--QAALDELQKNRTSLVIAHRLSTIEK-ADEILVV 551
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-196 |
5.53e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.33 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSG-----TIEYNGKSILDYPPI-QLRREVVMLGQTPPIFDGTIKDNLLMGLRfSE 99
Cdd:PRK14271 50 TSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIMDNVLAGVR-AH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 100 KPFPNDD---ALQGALTTVSL----DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTL 172
Cdd:PRK14271 129 KLVPRKEfrgVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180
....*....|....*....|....
gi 487961256 173 LAreKKKTVIFITHSQQLPEEIAD 196
Cdd:PRK14271 209 LA--DRLTVIIVTHNLAQAARISD 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-190 |
8.78e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 99.82 E-value: 8.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI--LDYPPI-QLRREVV----- 74
Cdd:COG4181 27 ILKGIS---------LEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDEDARaRLRARHVgfvfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 75 --MLGQTPpifdgTIKDNLLMGLRFSekpfPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVY 149
Cdd:COG4181 98 sfQLLPTL-----TALENVMLPLELA----GRRDARARAralLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 150 LLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQL 190
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-203 |
1.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 21 QKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIE----YNGKSILDYPPI------------QLRREVVMLGQTPP--I 82
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELItnpyskkiknfkELRRRVSMVFQFPEyqL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGlrfsekPF----PNDDALQGA---LTTVSLDKK-LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEP 154
Cdd:PRK13631 130 FKDTIEKDIMFG------PValgvKKSEAKKLAkfyLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487961256 155 TSALDGDTERRVMkQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:PRK13631 204 TAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-204 |
2.01e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDL-----QSPTSGTIEYNGKSIL--DYPPIQLRREVVMLGQTP-PIFDGTIKD 89
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYspDVDPIEVRREVGMVFQYPnPFPHLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMGLRFSEKPFPNDD-------ALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT 162
Cdd:PRK14267 105 NVAIGVKLNGLVKSKKEldervewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVG 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487961256 163 ERRVMKqfTLLAREKKKTVIFITHSQQLPEEIAD--------DIIEISKT 204
Cdd:PRK14267 185 TAKIEE--LLFELKKEYTIVLVTHSPAQAARVSDyvaflylgKLIEVGPT 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-199 |
9.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILD--YPPIQLRREVVMLGQTPP--IFDGTIKDNLLM 93
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPEyqLFEETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 GLR---FSEKPFPNddALQGALTTVSLDKKLEDNAS--SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMK 168
Cdd:PRK13637 108 GPInlgLSEEEIEN--RVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 169 QFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK13637 186 KIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-219 |
1.07e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 97.17 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 11 DILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDN 90
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 91 LLMGlrfseKPFPNDD------ALQGALTTVS-----LDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:cd03252 96 IALA-----DPGMSMErvieaaKLAGAHDFISelpegYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 160 GDTERRVMKQFTLLAreKKKTVIFITHSQQLPEEiADDIIEISK---TNGATRKEVLSIEGRY 219
Cdd:cd03252 171 YESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKgriVEQGSHDELLAENGLY 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-201 |
1.70e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdiLHIPYLQIqkektTCIIGESGSGKSTLLRMLNDLQSPTSGTIeYNGKSILDyppiQLRREVVMLGQTPPI 82
Cdd:PRK11247 27 VLNQLD----LHIPAGQF-----VAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLA----EAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FD-GTIKDNLLMGLRFSEKPfpndDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:PRK11247 93 LPwKKVIDNVGLGLKGQWRD----AALQ-ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 162 TeRRVMKQFTL-LAREKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:PRK11247 168 T-RIEMQDLIEsLWQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-199 |
1.75e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.50 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 19 QIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPI---QLRREVVMLGQTP-----PifDGTIKDN 90
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNPygslnP--RKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 91 LlmglrfsEKPFPNDDALQGA---------LTTVSLDKKLEDNASSL-SGGEKQRLAFARIILMDPPVYLLDEPTSALDG 160
Cdd:PRK11308 115 L-------EEPLLINTSLSAAerrekalamMAKVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 161 DTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-187 |
2.44e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDITYK-DILHIPY-LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQ 78
Cdd:PRK10771 1 MLKLTDITWLyHHLPMRFdLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 79 TPPIFDG-TIKDNLLMG----LRFSEKpfpNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDE 153
Cdd:PRK10771 79 ENNLFSHlTVAQNIGLGlnpgLKLNAA---QREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 487961256 154 PTSALDgDTERRVMkqFTLLA---REKKKTVIFITHS 187
Cdd:PRK10771 156 PFSALD-PALRQEM--LTLVSqvcQERQLTLLMVSHS 189
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-196 |
3.96e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITykdiLHIPYLQIqkektTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMlgqtp 80
Cdd:PRK11153 21 LNNVS----LHIPAGEI-----FGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQIGM----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 pIFDG-------TIKDNLLMGLRFSEKPFPNDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:PRK11153 87 -IFQHfnllssrTVFDNVALPLELAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 153 EPTSALDGDTERRVMKqftLLA---REKKKTVIFITHSQQLPEEIAD 196
Cdd:PRK11153 166 EATSALDPATTRSILE---LLKdinRELGLTIVLITHEMDVVKRICD 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-186 |
4.69e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITY----KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLG 77
Cdd:PRK10575 12 FALRNVSFrvpgRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 QTPPIFDG-TIKDNLLMGL--------RFSEKpfpNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPV 148
Cdd:PRK10575 92 QQLPAAEGmTVRELVAIGRypwhgalgRFGAA---DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 487961256 149 YLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITH 186
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-198 |
5.60e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 27 CIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRE-VVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPN 104
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENIFLGREPRRGGLID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 105 DDAL----QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDG-DTER--RVMKQFtllaREK 177
Cdd:COG1129 114 WRAMrrraRELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTErEVERlfRIIRRL----KAQ 189
|
170 180
....*....|....*....|...
gi 487961256 178 KKTVIFITHsqQLPE--EIADDI 198
Cdd:COG1129 190 GVAIIYISH--RLDEvfEIADRV 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-195 |
7.17e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 97.09 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILD-----YPPIQLRRevvmLG---QTPPIFDG-TIKDNLLMGLR 96
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargiFLPPHRRR----IGyvfQEARLFPHlSVRGNLLYGRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPNDDaLQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLARE 176
Cdd:COG4148 104 RAPRAERRIS-FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDE 182
|
170
....*....|....*....
gi 487961256 177 KKKTVIFITHSqqlPEEIA 195
Cdd:COG4148 183 LDIPILYVSHS---LDEVA 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
28-189 |
1.20e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.94 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPNDD 106
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYALFPHmTVFENVAFGLRMQKTPAAEIT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 A-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeRRVMkQFTL--LAREKKKTVIF 183
Cdd:PRK09452 123 PrVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL-RKQM-QNELkaLQRKLGITFVF 200
|
....*.
gi 487961256 184 ITHSQQ 189
Cdd:PRK09452 201 VTHDQE 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-186 |
1.27e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDG-TIK 88
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 89 DNLLMG----LRFSEKPFPNDDAL-QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:PRK11231 95 ELVAYGrspwLSLWGRLSAEDNARvNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180
....*....|....*....|....*.
gi 487961256 164 RRVMKqftlLARE---KKKTVIFITH 186
Cdd:PRK11231 175 VELMR----LMRElntQGKTVVTVLH 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-186 |
1.74e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRrevvmLGQTPPIfdgTIKDNLLMGL-- 95
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE-----VPDSLPL---TVRDLVAMGRwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 96 -RFSEKPFPNDD--ALQGALTTVSLDKkLEDNA-SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKqft 171
Cdd:NF040873 85 rRGLWRRLTRDDraAVDDALERVGLAD-LAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA--- 160
|
170
....*....|....*..
gi 487961256 172 LLARE--KKKTVIFITH 186
Cdd:NF040873 161 LLAEEhaRGATVVVVTH 177
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-203 |
3.10e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSiLDYPP-------IQLRREVVM 75
Cdd:COG4161 17 ALFDIN---------LECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ-FDFSQkpsekaiRLLRQKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 76 LGQT----PPIfdgTIKDNLLmglrfsEKP-----FPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIIL 143
Cdd:COG4161 87 VFQQynlwPHL---TVMENLI------EAPckvlgLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 144 MDPPVYLLDEPTSALDGDterrVMKQFTLLAREKKKTVI---FITHSQQLPEEIADDIIEISK 203
Cdd:COG4161 158 MEPQVLLFDEPTAALDPE----ITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEK 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-203 |
3.75e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP-IFDG-TIKDNLLMGL 95
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDnQFIGaTVEDDIAFGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 96 ---RFSEKPFPndDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTL 172
Cdd:PRK13632 110 enkKVPPKKMK--DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVD 187
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 173 LAREKKKTVIFITHSQqlpEEI--ADDIIEISK 203
Cdd:PRK13632 188 LRKTRKKTLISITHDM---DEAilADKVIVFSE 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-186 |
4.05e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.16 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 1 MFILKDITY----KDILHIPYLQIQKEKTTCIIGESGSGKSTLLR-MLNDLQSP--TSGTIEYNGKSILDYPPiqLRREV 73
Cdd:COG4136 1 MLSLENLTItlggRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPA--EQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 74 VMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:COG4136 79 GILFQDDLLFPHlSVGENLAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 487961256 153 EPTSALDGDTeRRVMKQFTL-LAREKKKTVIFITH 186
Cdd:COG4136 159 EPFSKLDAAL-RAQFREFVFeQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-199 |
4.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKDILHIPY---------LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSG-------TIEYNGKSILDYPp 66
Cdd:PRK13645 8 ILDNVSYTYAKKTPFefkalnntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 67 iQLRREVVMLGQTPP--IFDGTIKDNLLMG-LRFSEKPFPNDDALQGALTTVSLDKKLEDNAS-SLSGGEKQRLAFARII 142
Cdd:PRK13645 87 -RLRKEIGLVFQFPEyqLFQETIEKDIAFGpVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 487961256 143 LMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-199 |
7.78e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.06 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsilDYP---PIQLRReVVMLGQTPPIF-DGTIKDNLLM 93
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFtnlPPRERR-VGFVFQHYALFpHMTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 GLRfsEKPFPNDDALQGA---LTTVSLDKkLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:COG1118 99 GLR--VRPPSKAEIRARVeelLELVQLEG-LADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRW 175
|
170 180 190
....*....|....*....|....*....|
gi 487961256 170 FTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:COG1118 176 LRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-199 |
9.48e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.33 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQTPPI 82
Cdd:PRK11000 18 ISKDIN---------LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDG-TIKDNLLMGLRFSE-KPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDG 160
Cdd:PRK11000 87 YPHlSVAENMSFGLKLAGaKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 161 DTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK11000 167 ALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-203 |
9.68e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 91.49 E-value: 9.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLGQTPPIFDG-TIKDNL-----LMGLRFSEKp 101
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYLPQEFGVYPNfTVREFLdyiawLKGIPSKEV- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 fpnDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREkkKTV 181
Cdd:cd03264 108 ---KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIV 182
|
170 180
....*....|....*....|..
gi 487961256 182 IFITHSQQLPEEIADDIIEISK 203
Cdd:cd03264 183 ILSTHIVEDVESLCNQVAVLNK 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-196 |
1.09e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.41 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLN---DLQSPT--SGTIEYNGKSILD--YPPIQLRREVVMLGQTPPIFDGTIKDN 90
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCLNrmnELESEVrvEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFPMSVYDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 91 LLMGLRFS--EKPFPNDDALQGALTTVSL----DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTER 164
Cdd:PRK14258 108 VAYGVKIVgwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
170 180 190
....*....|....*....|....*....|..
gi 487961256 165 RVMKQFTLLAREKKKTVIFITHSQQLPEEIAD 196
Cdd:PRK14258 188 KVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-203 |
1.37e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 90.30 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 9 YKDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSP--TSGTIEYNGKSIldyPPIQLRREVVMLGQtppifdgt 86
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL---DKRSFRKIIGYVPQ-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 ikdnllmglrfsekpfpnDDALQGALT---TVSLDKKLednaSSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:cd03213 90 ------------------DDILHPTLTvreTLMFAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487961256 164 RRVMKQFTLLAREkKKTVIFITHsqQLPEEI---ADDIIEISK 203
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIH--QPSSEIfelFDKLLLLSQ 187
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-199 |
1.61e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 93.64 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDY-PPIQL---RREVVMLGQTPPIFDG-TIKDNLLMGLRFSEK 100
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrKGIFLppeKRRIGYVFQEARLFPHlSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 101 PFPN--DDALQGALttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKK 178
Cdd:TIGR02142 106 SERRisFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFG 182
|
170 180
....*....|....*....|.
gi 487961256 179 KTVIFITHSQQLPEEIADDII 199
Cdd:TIGR02142 183 IPILYVSHSLQEVLRLADRVV 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-191 |
1.74e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.63 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLGQTPpifdGtIKDNL--LMGLRFSEKPF--P 103
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQP----G-IKTELtaLENLRFYQRLHgpG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 104 NDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgdteRRVMKQFT-LLAR--EKKKT 180
Cdd:PRK13538 106 DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID----KQGVARLEaLLAQhaEQGGM 181
|
170
....*....|.
gi 487961256 181 VIFITHsQQLP 191
Cdd:PRK13538 182 VILTTH-QDLP 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-205 |
2.67e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 9 YKDILHIpYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIL----DYPPIQLRREVVMLGQTPP--I 82
Cdd:PRK13646 20 HQAIHDV-NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKRIGMVFQFPEsqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGLRFSEKPFPN--DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDG 160
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEvkNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 161 DTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISKTN 205
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-187 |
2.80e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.08 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsildypPIQ---LRREVVmlgqtppiF--DG-----TI 87
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV------PVTgpgADRGVV--------FqkDAllpwlNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 88 KDNLLMGLRFseKPFPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeR 164
Cdd:COG4525 94 LDNVAFGLRL--RGVPKAERRARAeelLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT-R 170
|
170 180
....*....|....*....|....
gi 487961256 165 RVMKQFTL-LAREKKKTVIFITHS 187
Cdd:COG4525 171 EQMQELLLdVWQRTGKGVFLITHS 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-199 |
2.85e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 88.64 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsildyppiqlrrevvmlgqtppifdgtikdnllmglrf 97
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 sEKPFPND-DALQGALTTVSldkklednasSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLaRE 176
Cdd:cd03216 63 -EVSFASPrDARRAGIAMVY----------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RA 130
|
170 180
....*....|....*....|....*
gi 487961256 177 KKKTVIFITHSqqLPE--EIADDII 199
Cdd:cd03216 131 QGVAVIFISHR--LDEvfEIADRVT 153
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-191 |
2.89e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.73 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiQLRREVVMLGQTPPI-FDGTIKDNLLMGLRFSEkpfPNDD 106
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLkPELSALENLHFWAAIHG---GAQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 ALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLArEKKKTVIFITH 186
Cdd:TIGR01189 107 TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHL-ARGGIVLLTTH 185
|
....*
gi 487961256 187 sQQLP 191
Cdd:TIGR01189 186 -QDLG 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-190 |
4.37e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 9 YKDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPP---IQLR-REVVMLGQTPPIF- 83
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRnQKLGFIYQFHHLLp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 84 DGTIKDNLLMGLRF-SEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT 162
Cdd:PRK11629 101 DFTALENVAMPLLIgKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*...
gi 487961256 163 ERRVMKQFTLLAREKKKTVIFITHSQQL 190
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-203 |
4.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP 81
Cdd:PRK13648 23 FTLKDVSFN---------IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 -IFDGTI-KDNLLMGLRFSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:PRK13648 94 nQFVGSIvKYDVAFGLENHAVPYDEmHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 159 DGDTERRVMKQFTLLAREKKKTVIFITHSqqLPEEI-ADDIIEISK 203
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHD--LSEAMeADHVIVMNK 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-203 |
5.08e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 89.73 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDyPPIQLRREVVMLGQTPPIFDG-TIKDNL----- 91
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENLeyfag 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 LMGLrfsekpfpNDDALQGALTTVS--LDKK--LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgDTERRVM 167
Cdd:cd03266 105 LYGL--------KGDELTARLEELAdrLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD-VMATRAL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 487961256 168 KQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03266 176 REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-155 |
7.26e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 89.66 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqlrREVVMLG----- 77
Cdd:COG0410 18 VLHGVS---------LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP----HRIARLGigyvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 QTPPIFDG-TIKDNLLMGLRFSEKPFPNDDALQGALTTV-SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:COG0410 85 EGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-189 |
7.29e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.82 E-value: 7.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 fsEKPFPND---DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLL 173
Cdd:PRK11607 118 --QDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDI 195
|
170
....*....|....*.
gi 487961256 174 AREKKKTVIFITHSQQ 189
Cdd:PRK11607 196 LERVGVTCVMVTHDQE 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-203 |
8.08e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 12 ILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNG-----------KSILdyppiQLRREVVMLGQT- 79
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIR-----ELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 ---PPIfdgTIKDNLL------MGLrfsEKPFPNDDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYL 150
Cdd:PRK11124 92 nlwPHL---TVQQNLIeapcrvLGL---SKDQALARAEK-LLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 151 LDEPTSALDGDTERRVMKQFTLLArEKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-193 |
1.27e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 88.32 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIqLRREVVMLGQTPPIfDGTIkdNLLMGLRFSeKPFPNDDA 107
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGI-KTTL--SVLENLRFW-HADHSDEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 LQGALTTVSLdKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLArEKKKTVIFITH 186
Cdd:cd03231 106 VEEALARVGL-NGFEDRpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC-ARGGMVVLTTH 183
|
....*..
gi 487961256 187 sQQLPEE 193
Cdd:cd03231 184 -QDLGLS 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-196 |
1.70e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLN------DLQSPTSGTIEYNGKSILDYPPIQLRREVVML 76
Cdd:PRK14246 25 ILKDITIK---------IPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 77 GQTP-PIFDGTIKDNLLMGLRFS--EKPFPNDDALQGALTTVSLDKKLEDN----ASSLSGGEKQRLAFARIILMDPPVY 149
Cdd:PRK14246 96 FQQPnPFPHLSIYDNIAYPLKSHgiKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 150 LLDEPTSALDGDTERRVMKQFTLLAREkkKTVIFITHSQQLPEEIAD 196
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVAD 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-215 |
1.95e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.29 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqlRREVVMlgQTPPIFDG-TIKDNLLMG-- 94
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVF--QNYSLLPWlTVRENIALAvd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 -----LRFSEKPFPNDDALQgaltTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:TIGR01184 81 rvlpdLSKSERRAIVEEHIA----LVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 170 FTLLAREKKKTVIFITHSQQLPEEIADDIIEISKTNGATRKEVLSI 215
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-199 |
2.18e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.18 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQTP-----PIFdgTIKD 89
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDPyaslnPRM--TVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMGLRFSEKPFPND--DALQGALTTVSLDKK-LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:COG4608 117 IIAEPLRIHGLASKAErrERVAELLELVGLRPEhADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQV 196
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 167 MKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:COG4608 197 LNLLEDLQDELGLTYLFISHDLSVVRHISDRVA 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-186 |
2.64e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.60 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:COG4604 16 VLDDVS---------LTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 ---FdgTIKDnLLMGLRFsekPFPnddalQGALTTVslDKKLEDNA--------------SSLSGGEKQRlAF-ARIILM 144
Cdd:COG4604 87 nsrL--TVRE-LVAFGRF---PYS-----KGRLTAE--DREIIDEAiayldledladrylDELSGGQRQR-AFiAMVLAQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 487961256 145 DPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITH 186
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-203 |
3.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.71 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTP--PIFDGTIKDNLLMG---LRFSEKPF 102
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpinLGLDEETV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 PNddALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVI 182
Cdd:PRK13652 115 AH--RVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVI 192
|
170 180
....*....|....*....|.
gi 487961256 183 FITHSQQLPEEIADDIIEISK 203
Cdd:PRK13652 193 FSTHQLDLVPEMADYIYVMDK 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-199 |
3.66e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI------------LDYPPIQ-LRREVVMLGQTPPIFD 84
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvADKNQLRlLRTRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 85 G-TIKDNLL------MGLRFSEKpfpNDDALQgALTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:PRK10619 106 HmTVLENVMeapiqvLGLSKQEA---RERAVK-YLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487961256 157 ALDGDTERRVMKQFTLLArEKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-186 |
5.22e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 86.70 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:cd03369 23 VLKNVSFK---------VKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGLRFSekpfpnDDALQGALttvsldkKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT 162
Cdd:cd03369 94 FSGTIRSNLDPFDEYS------DEEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180
....*....|....*....|....
gi 487961256 163 ERRVMKqfTLLAREKKKTVIFITH 186
Cdd:cd03369 161 DALIQK--TIREEFTNSTILTIAH 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-201 |
1.03e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGksildyppiQLRreVVMLGQTPPI 82
Cdd:COG0488 13 LLDDVS---------LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDG-TIKDNLLMGL-----------RFSEKP-FPNDD-----ALQGA---------------------LTTVSLDKKLed 123
Cdd:COG0488 73 DDDlTVLDTVLDGDaelraleaeleELEAKLaEPDEDlerlaELQEEfealggweaearaeeilsglgFPEEDLDRPV-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 124 naSSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT----ERrvmkqftLLAREkKKTVIFITHSQQLPEEIADDII 199
Cdd:COG0488 151 --SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEE-------FLKNY-PGTVLVVSHDRYFLDRVATRIL 220
|
..
gi 487961256 200 EI 201
Cdd:COG0488 221 EL 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-199 |
1.32e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 89.36 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQsPTSGTIEYNGKSILDYPPIQ---LRREVVMLGQTP-----PIFdgTIKD 89
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPfgslsPRM--TVGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMGLRFSEkPFPNDDALQG----ALTTVSLDKKL------EdnassLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:COG4172 384 IIAEGLRVHG-PGLSAAERRArvaeALEEVGLDPAArhryphE-----FSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487961256 160 gdteRRVMKQ-FTLLAREKKK---TVIFITHSQQLPEEIADDII 199
Cdd:COG4172 458 ----VSVQAQiLDLLRDLQREhglAYLFISHDLAVVRALAHRVM 497
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-219 |
1.67e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.01 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdiLHIPYLQIqkektTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI 82
Cdd:PRK10790 356 VLQNIN----LSVPSRGF-----VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGLRFSEkpfpndDALQGALTTVSL-----------DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:PRK10790 427 LADTFLANVTLGRDISE------EQVWQALETVQLaelarslpdglYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487961256 152 DEPTSALDGDTERRVmkQFTLLAREKKKTVIFITHSQQLPEEiADDIIEISK---TNGATRKEVLSIEGRY 219
Cdd:PRK10790 501 DEATANIDSGTEQAI--QQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRgqaVEQGTHQQLLAAQGRY 568
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-203 |
3.30e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 84.58 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIqLRREVVMLgqTPPIFDG--TIKDNLLMGL 95
Cdd:cd03268 21 LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-LRRIGALI--EAPGFYPnlTARENLRLLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 96 RFSEKPfpnDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRvMKQFTLLAR 175
Cdd:cd03268 98 RLLGIR---KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE-LRELILSLR 173
|
170 180 190
....*....|....*....|....*....|
gi 487961256 176 EKKKTVIFITHsqQLPE--EIADDIIEISK 203
Cdd:cd03268 174 DQGITVLISSH--LLSEiqKVADRIGIINK 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-203 |
3.46e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 84.64 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILD---------------YPPIQLRREVVMLGQtppi 82
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIaarnrigylpeerglYPKMKVIDQLVYLAQ---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 fdgtikdnlLMGLRFSEKPFPNDDALQGALTTVSLDKKLEDnassLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgDT 162
Cdd:cd03269 97 ---------LKGLKKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLD-PV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 163 ERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
28-199 |
3.86e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPI-FDGTIKDNLLMGL-----RFSEKP 101
Cdd:PRK09536 34 LVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRtphrsRFDTWT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 FPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLArEKKKTV 181
Cdd:PRK09536 114 ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTA 192
|
170
....*....|....*...
gi 487961256 182 IFITHSQQLPEEIADDII 199
Cdd:PRK09536 193 VAAIHDLDLAARYCDELV 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-211 |
4.76e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQS--PTSGTIEYN----------------------- 57
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 58 ----GKSILDY--PPIQLRREV-----VMLGQTPPIF-DGTIKDNLLMGLrfSEKPFPNDDALQGA---LTTVSLDKKLE 122
Cdd:TIGR03269 86 ggtlEPEEVDFwnLSDKLRRRIrkriaIMLQRTFALYgDDTVLDNVLEAL--EEIGYEGKEAVGRAvdlIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 123 DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEIS 202
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
....*....
gi 487961256 203 ktNGATRKE 211
Cdd:TIGR03269 244 --NGEIKEE 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-208 |
5.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTP--PIFDGTIKDNLL--- 92
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAfgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 --MGLRFSEKpfpnDDALQGALTTVSLdKKLEDNAS-SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:PRK13647 106 vnMGLDKDEV----ERRVEEALKAVRM-WDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEI 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 170 FTLLAREkKKTVIFITHSQQLPEEIADDIIEIskTNGAT 208
Cdd:PRK13647 181 LDRLHNQ-GKTVIVATHDVDLAAEWADQVIVL--KEGRV 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-199 |
6.00e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSGtieyngKSILDYPPIQLRREVVMLGQTPPifDGTIKDNLlmglrfsekpfpnd 105
Cdd:COG2401 59 VLIVGASGSGKSTLLRLLAGALKGTPV------AGCVDVPDNQFGREASLIDAIGR--KGDFKDAV-------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 106 dalqGALTTVsldkKLEDNA------SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKK 179
Cdd:COG2401 117 ----ELLNAV----GLSDAVlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGI 188
|
170 180
....*....|....*....|
gi 487961256 180 TVIFITHSQQLPEEIADDII 199
Cdd:COG2401 189 TLVVATHHYDVIDDLQPDLL 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-203 |
6.59e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.31 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDyPPIQlRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQ-QRDICMVFQSYALFPHmSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeRRVMkqftllaR 175
Cdd:PRK11432 105 MLGVPKEErKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL-RRSM-------R 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 487961256 176 EKKK--------TVIFITHSQQLPEEIADDIIEISK 203
Cdd:PRK11432 177 EKIRelqqqfniTSLYVTHDQSEAFAVSDTVIVMNK 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-197 |
7.70e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRML--NDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLG-QT 79
Cdd:COG0396 15 ILKGVN---------LTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDERARAGIFLAfQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDG-TIKDNL---LMGLRFSEKPFPN-DDALQGALTTVSLDKKLED---NASsLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:COG0396 86 PVEIPGvSVSNFLrtaLNARRGEELSAREfLKLLKEKMKELGLDEDFLDryvNEG-FSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEIADD 197
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQRILDYIKPD 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-186 |
1.08e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQ---TPPifDGTIKDNLLMGlRFSEKPF 102
Cdd:PRK10253 36 TAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnatTPG--DITVQELVARG-RYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 ------PNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLARE 176
Cdd:PRK10253 113 ftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRE 192
|
170
....*....|
gi 487961256 177 KKKTVIFITH 186
Cdd:PRK10253 193 KGYTLAAVLH 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-198 |
1.10e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 27 CIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsildypPIQLR--RE-----VVMLGQTPPIFDG-TIKDNLLMGLRFS 98
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGK------PVRIRspRDaialgIGMVHQHFMLVPNlTVAENIVLGLEPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 99 EKPFPNDDALQGALTTVS--------LDKKLEDnassLSGGEKQRLAFARIILMDPPVYLLDEPTSAL-DGDTER--RVM 167
Cdd:COG3845 109 KGGRLDRKAARARIRELSerygldvdPDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADElfEIL 184
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 168 KQFtllaREKKKTVIFITHsqQLPE--EIADDI 198
Cdd:COG3845 185 RRL----AAEGKSIIFITH--KLREvmAIADRV 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-199 |
1.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 19 QIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIL----DYPPIQLRREVVMLGQTPP--IFDGTIKDNLL 92
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPEaqLFENTVLKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLR---FSEKPfPNDDALQGaLTTVSLDKKLEDNAS-SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMK 168
Cdd:PRK13641 109 FGPKnfgFSEDE-AKEKALKW-LKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ 186
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 169 QFTLLAREkKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK13641 187 LFKDYQKA-GHTVILVTHNMDDVAEYADDVL 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-166 |
1.33e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 21 QKEKTTcIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPpiQLRREVVMLGQTppifDGtIKDNLLMG--LRFS 98
Cdd:PRK13539 27 AGEALV-LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDP--DVAEACHYLGHR----NA-MKPALTVAenLEFW 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 99 EKPFPNDD-ALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:PRK13539 98 AAFLGGEElDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-203 |
1.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.27 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ-LRREVVMLGQTPPI-FDG-TIKDNLLMG 94
Cdd:PRK13644 23 LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVGIVFQNPETqFVGrTVEEDLAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 LR-FSEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLL 173
Cdd:PRK13644 103 PEnLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL 182
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 174 aREKKKTVIFITHSqqLPE-EIADDIIEISK 203
Cdd:PRK13644 183 -HEKGKTIVYITHN--LEElHDADRIIVMDR 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-201 |
1.59e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPP---IQLRREvvMLG-- 77
Cdd:PRK10535 23 VLKGIS---------LDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQLRRE--HFGfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 78 ----------------QTPPIFDGTIKDNLLmglrfsekpfpndDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARI 141
Cdd:PRK10535 92 fqryhllshltaaqnvEVPAVYAGLERKQRL-------------LRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 142 ILMDPPVYLLDEPTSALDGDTERRVM---KQFtllaREKKKTVIFITHSQQLPEEiADDIIEI 201
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMailHQL----RDRGHTVIIVTHDPQVAAQ-AERVIEI 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-186 |
1.91e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIL------DYPPIqlRREVVMLGQTPP--IFDGTIkd 89
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQI--RKKVGLVFQFPEsqLFEETV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 nlLMGLRFSEKPF--PNDDALQGA---LTTVSLDKKL-EDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:PRK13649 104 --LKDVAFGPQNFgvSQEEAEALArekLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180
....*....|....*....|...
gi 487961256 164 RRVMKQFTLLaREKKKTVIFITH 186
Cdd:PRK13649 182 KELMTLFKKL-HQSGMTIVLVTH 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
28-202 |
2.32e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.87 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRML--NDLqsPTSGTIEYN-GKSILDY---PP---IQLRR-------------------EVVMLgqt 79
Cdd:COG4778 42 LTGPSGAGKSTLLKCIygNYL--PDSGSILVRhDGGWVDLaqaSPreiLALRRrtigyvsqflrviprvsalDVVAE--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 pPIFDgtikdnllMGlrfsekpFPNDDALQGA---LTTVSLDKKLEDNA-SSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:COG4778 117 -PLLE--------RG-------VDREEARARArelLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487961256 156 SALDGDTERRVMKqftlLAREKKK---TVIFITHSQQLPEEIADDIIEIS 202
Cdd:COG4778 181 ASLDAANRAVVVE----LIEEAKArgtAIIGIFHDEEVREAVADRVVDVT 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-196 |
2.66e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYnGKSILDYPPIQ-----LRREVVMLGQTPP--IFDGTIKDN 90
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeikpVRKKVGVVFQFPEsqLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 91 LLMGLR-FSEKPFPNDDALQGALTTVSLDKKL-EDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMK 168
Cdd:PRK13643 106 VAFGPQnFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ 185
|
170 180
....*....|....*....|....*...
gi 487961256 169 QFTLLaREKKKTVIFITHsqqLPEEIAD 196
Cdd:PRK13643 186 LFESI-HQSGQTVVLVTH---LMDDVAD 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-196 |
7.08e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIeyngkSILDYP-PIQLRREVVMLGQTPPiFDG-----TIKDNLLM-GLRFSEK 100
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKI-----TVLGVPvPARARLARARIGVVPQ-FDNldlefTVRENLLVfGRYFGMS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 101 PFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQF-TLLARekKK 179
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLrSLLAR--GK 223
|
170
....*....|....*..
gi 487961256 180 TVIFITHSQQLPEEIAD 196
Cdd:PRK13536 224 TILLTTHFMEEAERLCD 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-159 |
9.40e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 9.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLqSPTSGTIEYNGKSILDYPPIQLRREVVMLGQ-TPPIFdgtikdnlLMG-- 94
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQqQSPPF--------AMPvf 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 95 --LRFSEKPFPNDDALQGALTTVS----LDKKLEDNASSLSGGEKQRLAFARIIL-MDPPV------YLLDEPTSALD 159
Cdd:COG4138 88 qyLALHQPAGASSEAVEQLLAQLAealgLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLD 165
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-201 |
1.17e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEY-----------------NGKSILDY--------PPIQLRRevvMLGqtppi 82
Cdd:COG0488 346 LIGPNGAGKSTLLKLLAGELEPDSGTVKLgetvkigyfdqhqeeldPDKTVLDElrdgapggTEQEVRG---YLG----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 fdgtikdnllmglRFSekpFPNDDAlqgalttvslDKKlednASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDT 162
Cdd:COG0488 418 -------------RFL---FSGDDA----------FKP----VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 163 eRRVMKQftLLArEKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:COG0488 468 -LEALEE--ALD-DFPGTVLLVSHDRYFLDRVATRILEF 502
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
2.17e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.26 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITY----KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYppiqlrrevvmLGQt 79
Cdd:cd03221 3 LENLSKtyggKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY-----------FEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 ppifdgtikdnllmglrfsekpfpnddalqgalttvsldkklednassLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487961256 160 GDTeRRVMKQFtLlaREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03221 103 LES-IEALEEA-L--KEYPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-198 |
3.09e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.42 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKS----TLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRR----EVVMLGQTP-----PIFd 84
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPmtslnPLH- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 85 gTIKDNLLMGLRFSeKPFPNDDALQGA---LTTVSLD---KKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:COG4172 110 -TIGKQIAEVLRLH-RGLSGAAARARAlelLERVGIPdpeRRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487961256 159 DGDTERRVMKqftLLAREKKKT---VIFITHSQQLPEEIADDI 198
Cdd:COG4172 188 DVTVQAQILD---LLKDLQRELgmaLLLITHDLGVVRRFADRV 227
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-186 |
3.13e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.45 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIldyPPIQL---RREVVMLGQTPPIFDGT 86
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---TKLQLdswRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLLMGlrfseKPFP--------------NDDAL---QGALTTVSldkkleDNASSLSGGEKQRLAFARIILMDPPVY 149
Cdd:PRK10789 405 VANNIALG-----RPDAtqqeiehvarlasvHDDILrlpQGYDTEVG------ERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190
....*....|....*....|....*....|....*..
gi 487961256 150 LLDEPTSALDGDTERRVMKQftLLAREKKKTVIFITH 186
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHN--LRQWGEGRTVIISAH 508
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-211 |
4.05e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 79.34 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDyPPIQLRREVVMLGQTPPIFDG-TIKDNLLMGLR 96
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEkpFPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLL 173
Cdd:cd03265 100 LYG--VPGAERRERIdelLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 487961256 174 AREKKKTVIFITHSQQLPEEIADDIIEISktNGATRKE 211
Cdd:cd03265 178 KEEFGMTILLTTHYMEEAEQLCDRVAIID--HGRIIAE 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-203 |
4.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 80.61 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGT--------IEYNGKSILDyppiqLRREVV 74
Cdd:PRK13640 22 ALNDISFS---------IPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWD-----IREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 75 MLGQTP--PIFDGTIKDNLLMGLRFSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:PRK13640 88 IVFQNPdnQFVGATVGDDVAFGLENRAVPRPEmIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQlPEEIADDIIEISK 203
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDD 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-199 |
5.04e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 79.76 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPPIQLRrevvmlgqtpPIFDGTIKDnLLMGL--RFSEKPFPND 105
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIK----------ADYEGTVRD-LLSSItkDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 106 DALQgaltTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgDTERRVM--KQFTLLAREKKKTVIF 183
Cdd:cd03237 98 EIAK----PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL--DVEQRLMasKVIRRFAENNEKTAFV 171
|
170
....*....|....*.
gi 487961256 184 ITHSQQLPEEIADDII 199
Cdd:cd03237 172 VEHDIIMIDYLADRLI 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-201 |
5.86e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 78.34 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLR--MLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLG-QTPPIFDGt 86
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtiMGHPKYEVTEGEILFKGEDITDLPPEERARLGIFLAfQYPPEIPG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 ikdnllmglrfsekpfpnddalqgalttVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:cd03217 92 ----------------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190
....*....|....*....|....*....|....*
gi 487961256 167 MKQFTLLaREKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:cd03217 144 AEVINKL-REEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-186 |
6.24e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPP---IQLRREVVMLGQTP--PIFDGTIKDNL- 91
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRkglMKLRESVGMVFQDPdnQLFSASVYQDVs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 --LMGLRFSEKPFpnDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:PRK13636 106 fgAVNLKLPEDEV--RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL 183
|
170
....*....|....*..
gi 487961256 170 FTLLAREKKKTVIFITH 186
Cdd:PRK13636 184 LVEMQKELGLTIIIATH 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-203 |
7.36e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 78.73 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGK--SILDY-----PPIQLRREVVM 75
Cdd:cd03220 37 ALKDVS---------FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGLgggfnPELTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 76 LGqtppifdgtikdnLLMGLRFSEKPFPNDDALQGAlttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:cd03220 108 NG-------------RLLGLSRKEIDEKIDEIIEFS----ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 156 SAldGDTE-----RRVMKQFtllaREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03220 171 AV--GDAAfqekcQRRLREL----LKQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-214 |
7.44e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.74 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPP---IQLRREVVMLGQTP--PIFDGTIKDNLL 92
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKkslLEVRKTVGIVFQNPddQLFAPTVEEDVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MG---LRFSEKPFPNddALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:PRK13639 102 FGplnLGLSKEEVEK--RVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 487961256 170 FTLLAREkKKTVIFITHSQQLPEEIADDIIEISKTN---GATRKEVLS 214
Cdd:PRK13639 180 LYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKiikEGTPKEVFS 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-203 |
7.82e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGK--SILDyppiqlrrevVMLGqtp 80
Cdd:COG1134 41 ALKDVS---------FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLE----------LGAG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 piFDG--TIKDN-----LLMGLRFSEkpfpnddalqgalttvsLDKKLEDNAS-------------SLSGGEKQRLAFAR 140
Cdd:COG1134 99 --FHPelTGRENiylngRLLGLSRKE-----------------IDEKFDEIVEfaelgdfidqpvkTYSSGMRARLAFAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 141 IILMDPPVYLLDEPTSAldGDTE-----RRVMKQFtllaREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG1134 160 ATAVDPDILLVDEVLAV--GDAAfqkkcLARIREL----RESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-186 |
7.86e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.78 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP-IFDG-TIKDNLLMGLRfsEKPFPND 105
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDnQFVGaTVEDDVAFGLE--NKGIPHE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 106 DA---LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVI 182
Cdd:PRK13650 116 EMkerVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVI 195
|
....
gi 487961256 183 FITH 186
Cdd:PRK13650 196 SITH 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-217 |
8.69e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.92 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRML--NDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLG-QTPPIFDGT 86
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEERAHLGIFLAfQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLLMGLRFSEKPFPND---DALQ------GALTTVSLDKK-LEDNASS-LSGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:CHL00131 100 SNADFLRLAYNSKRKFQGLpelDPLEfleiinEKLKLVGMDPSfLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 156 SALDGDTERRVMKQFTLLAReKKKTVIFITHSQQLPEEIADDII------EISKTNGATRKEVLSIEG 217
Cdd:CHL00131 180 SGLDIDALKIIAEGINKLMT-SENSIILITHYQRLLDYIKPDYVhvmqngKIIKTGDAELAKELEKKG 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-187 |
1.03e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 27 CIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlRREVV-------MLGQTPpifDGTIKDNLLM------ 93
Cdd:COG1101 36 TVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKYIgrvfqdpMMGTAP---SMTIEENLALayrrgk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 --GLRFSEKPfPNDDALQGALTTVS--LDKKLEDNASSLSGGEKQRLAFariiLM----DPPVYLLDEPTSALDGDTERR 165
Cdd:COG1101 112 rrGLRRGLTK-KRRELFRELLATLGlgLENRLDTKVGLLSGGQRQALSL----LMatltKPKLLLLDEHTAALDPKTAAL 186
|
170 180
....*....|....*....|..
gi 487961256 166 VMKQFTLLAREKKKTVIFITHS 187
Cdd:COG1101 187 VLELTEKIVEENNLTTLMVTHN 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-198 |
1.03e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.10 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 12 ILHIPYLQIQKEKTTCIIGESGSGKSTLLRML-NDLQSPT-------SGTIEYNGKSILDYPPIQL-RREVVMLGQTPPI 82
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLaRLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMG-----LRFSEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIIL--------MDPPVY 149
Cdd:PRK13547 96 FAFSAREIVLLGryphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaAQPPRY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487961256 150 LL-DEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK13547 176 LLlDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-198 |
1.04e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLR----REVVMLGQTPPIFDG-TIKDNLL 92
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLRFSEKPFP--NDDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQF 170
Cdd:PRK10070 129 FGMELAGINAEerREKALD-ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180
....*....|....*....|....*...
gi 487961256 171 TLLAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-190 |
1.10e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI--LDYPP-IQLRREVV-------MLGQTPPIFDGTI 87
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEArAKLRAKHVgfvfqsfMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 88 KDNLLMGlrfsEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVM 167
Cdd:PRK10584 111 LPALLRG----ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180
....*....|....*....|...
gi 487961256 168 KQFTLLAREKKKTVIFITHSQQL 190
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQL 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-190 |
2.01e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ---LRREVVMLGQTPPIF-DGTIKDNLLMGLRFSEKPfp 103
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDRTVYDNVAIPLIIAGAS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 104 NDDA---LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAReKKKT 180
Cdd:PRK10908 111 GDDIrrrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVT 189
|
170
....*....|
gi 487961256 181 VIFITHSQQL 190
Cdd:PRK10908 190 VLMATHDIGL 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-185 |
2.41e-17 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 80.34 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsiLDYPPiqlrrevvmlgQTPPI 82
Cdd:TIGR01271 441 VLKNISFK---------LEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSP-----------QTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGLRFSEKPFP---NDDALQGALTTVSLDKK--LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYDEYRYTsviKACQLEEDIALFPEKDKtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180
....*....|....*....|....*...
gi 487961256 158 LDGDTERRVMKQfTLLAREKKKTVIFIT 185
Cdd:TIGR01271 579 LDVVTEKEIFES-CLCKLMSNKTRILVT 605
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-201 |
2.42e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIldypPIQLRREVVMLGQTPPiFDG-----TIKDNLL 92
Cdd:PRK13537 28 FHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQRVGVVPQ-FDNldpdfTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 M-GLRFSEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQF- 170
Cdd:PRK13537 103 VfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLr 182
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 171 TLLARekKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:PRK13537 183 SLLAR--GKTILLTTHFMEEAERLCDRLCVI 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-186 |
2.95e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYkdilhipylQIQKEKTTCIIGESGSGKSTLLRML--------------------------------------- 43
Cdd:PTZ00265 1183 IYKDLTF---------SCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmk 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 44 --NDLQSP-------------TSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLlmglRFSEKPFPNDDAL 108
Cdd:PTZ00265 1254 nvNEFSLTkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI----KFGKEDATREDVK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 109 QGALTTV------SLDKKLEDN----ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKK 178
Cdd:PTZ00265 1330 RACKFAAidefieSLPNKYDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD 1409
|
....*...
gi 487961256 179 KTVIFITH 186
Cdd:PTZ00265 1410 KTIITIAH 1417
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-199 |
4.59e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.15 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ---LRREVVMLGQTPPifdGT 86
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDSP---SA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLLMGLRFSEkPFPN----DDALQGA-----LTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:TIGR02769 101 VNPRMTVRQIIGE-PLRHltslDESEQKAriaelLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487961256 157 ALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVA 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-186 |
5.07e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.30 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 5 KDI-TYKDIlhipYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIL-DYPPIQLRREVVMLGQTPPI 82
Cdd:PTZ00265 396 KDVeIYKDL----NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLkDINLKWWRSKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGL-----------RFSEKPFPNDDALQGALT-----------------------------------TVS 116
Cdd:PTZ00265 472 FSNSIKNNIKYSLyslkdlealsnYYNEDGNDSQENKNKRNScrakcagdlndmsnttdsneliemrknyqtikdseVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 117 LDKK---------LED--------NASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKK 179
Cdd:PTZ00265 552 VSKKvlihdfvsaLPDkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
....*..
gi 487961256 180 TVIFITH 186
Cdd:PTZ00265 632 ITIIIAH 638
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-198 |
5.38e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 76.66 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSG-TI-----EYNGKSILD--------YPPIQ 68
Cdd:COG1119 18 ILDDIS---------WTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVrlfgeRRGGEDVWElrkriglvSPALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 69 LR-------REVVMLGqtppiFDGTIkdnllmGLrfSEKPFPNDDAL-QGALTTVSLDKKLEDNASSLSGGEKQRLAFAR 140
Cdd:COG1119 89 LRfprdetvLDVVLSG-----FFDSI------GL--YREPTDEQRERaRELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 141 IILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSqqlPEEIADDI 198
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPGI 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-198 |
5.42e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKS-TLLRMLNDLQSP----TSGTIEYNGKSILDYPPIQLRR----EVVMLGQTP-----PIF 83
Cdd:PRK15134 30 LQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPmvslnPLH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 84 dgTIKDNLLMGL---RFSEKPFPNDDALQGaLTTVSL---DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:PRK15134 110 --TLEKQLYEVLslhRGMRREAARGEILNC-LDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 158 LDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK15134 187 LDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRV 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-188 |
7.07e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQlrREVVMLGQT----PPIfdgTIKDNLLMGLRFSEKPFP 103
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNyalyPHM---SVRENMAYGLKIRGMPKA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 104 NDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgDTERRVmkQFTL----LAREKK 178
Cdd:PRK11650 110 EIEErVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL--DAKLRV--QMRLeiqrLHRRLK 185
|
170
....*....|
gi 487961256 179 KTVIFITHSQ 188
Cdd:PRK11650 186 TTSLYVTHDQ 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
28-186 |
7.23e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGK----------------SILDYPPI--------QLRREVVMLGQTPP-- 81
Cdd:PRK13651 38 IIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKdeknkkktkekekvleKLVIQKTRfkkikkikEIRRRVGVVFQFAEyq 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDGTIKDNLLMGLRfsEKPFPNDDALQGA---LTTVSLDKK-LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:PRK13651 118 LFEQTIEKDIIFGPV--SMGVSKEEAKKRAakyIELVGLDESyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAG 195
|
170 180
....*....|....*....|....*....
gi 487961256 158 LDGDTERRVMKQFTLLaREKKKTVIFITH 186
Cdd:PRK13651 196 LDPQGVKEILEIFDNL-NKQGKTIILVTH 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-199 |
1.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.28 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPI-QLRREVVMLGQTPpifdgtikDNLLMGLR 96
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNP--------DNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSE-----------KPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERR 165
Cdd:PRK13633 103 VEEdvafgpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 166 VMKQFTLLAREKKKTVIFITHSQQLPEEiADDII 199
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEAVE-ADRII 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-187 |
1.60e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILD-----YPPIQLRRevvmLG---QTPPIFDG-TIK 88
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgiCLPPEKRR----IGyvfQDARLFPHyKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 89 DNLLMGLRFSEKP-FpndDALQGALttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVM 167
Cdd:PRK11144 95 GNLRYGMAKSMVAqF---DKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180
....*....|....*....|
gi 487961256 168 KQFTLLAREKKKTVIFITHS 187
Cdd:PRK11144 169 PYLERLAREINIPILYVSHS 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-199 |
1.70e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsiLDYPPIQLRREVVM-----LGQTPPIFDGTIKDNLLMglrfseKPF 102
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKPQYIKPDYDGtvedlLRSITDDLGSSYYKSEII------KPL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 pnddalqgalttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgDTERRVM--KQFTLLAREKKKT 180
Cdd:PRK13409 442 -------------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL--DVEQRLAvaKAIRRIAEEREAT 506
|
170
....*....|....*....
gi 487961256 181 VIFITHSQQLPEEIADDII 199
Cdd:PRK13409 507 ALVVDHDIYMIDYISDRLM 525
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
18-219 |
1.75e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 75.13 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILdyppiqlRREVVMLG---QTPPIFDG-TIKDNL-- 91
Cdd:TIGR03740 21 LTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDLHKIGsliESPPLYENlTARENLkv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 ---LMGLRFSEkpfpnddaLQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD--GDTE-RR 165
Cdd:TIGR03740 94 httLLGLPDSR--------IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDpiGIQElRE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487961256 166 VMKQFTllarEKKKTVIFITHSQQLPEEIADDIIEISktNGatrkeVLSIEGRY 219
Cdd:TIGR03740 166 LIRSFP----EQGITVILSSHILSEVQQLADHIGIIS--EG-----VLGYQGKI 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-199 |
2.15e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.13 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsiLDYPPIQLRrevvmlgqtpPIFDGTIKDNLLMGL--RFSEKPFPND 105
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--ISYKPQYIS----------PDYDGTVEEFLRSANtdDFGSSYYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 106 --DALQgalttvsLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgDTERRVM--KQFTLLAREKKKTV 181
Cdd:COG1245 439 iiKPLG-------LEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL--DVEQRLAvaKAIRRFAENRGKTA 509
|
170
....*....|....*...
gi 487961256 182 IFITHSQQLPEEIADDII 199
Cdd:COG1245 510 MVVDHDIYLIDYISDRLM 527
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-203 |
2.47e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTP--PIFDGTIKDNLLMGL 95
Cdd:PRK13642 28 FSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 96 RfsEKPFPNDDAL----QGALTTVSLDKKLEDNASsLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFT 171
Cdd:PRK13642 108 E--NQGIPREEMIkrvdEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH 184
|
170 180 190
....*....|....*....|....*....|..
gi 487961256 172 LLAREKKKTVIFITHSqqLPEEIADDIIEISK 203
Cdd:PRK13642 185 EIKEKYQLTVLSITHD--LDEAASSDRILVMK 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-203 |
2.65e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.53 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI----------------LdYPPIQLRREVVMLGQtpp 81
Cdd:COG4152 22 FTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrrigylpeergL-YPKMKVGEQLVYLAR--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 ifdgtikdnlLMGLrfsekpfPNDDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:COG4152 98 ----------LKGL-------SKAEAKRRAdewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 159 DGDTeRRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG4152 161 DPVN-VELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-192 |
3.74e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI--LDYPPIQ-LRREVVMLGQTPP-IFD- 84
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakLNRAQRKaFRRDIQMVFQDSIsAVNp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 85 -GTIKDNL------LMGLrfsekpfpnDDALQGA-----LTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLL 151
Cdd:PRK10419 105 rKTVREIIreplrhLLSL---------DKAERLArasemLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 152 DEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPE 192
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVE 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-199 |
5.26e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLL-RMLNDLQSpTSGTIEYNGKSILDYPPIQL----RREVVMLGQTPPIFDGTIKDNLL 92
Cdd:cd03290 22 IRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVEENIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLRFSE---KPFPNDDALQGALTTVSLDKKLE--DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVM 167
Cdd:cd03290 101 FGSPFNKqryKAVTDACSLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 180
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 168 KQFTL-LAREKKKTVIFITHS-QQLPEeiADDII 199
Cdd:cd03290 181 QEGILkFLQDDKRTLVLVTHKlQYLPH--ADWII 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-158 |
8.60e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 13 LHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRE-VVMLGQTPPIFDG-TIKDN 90
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 91 LLMGLRFSEKpfpndDALQGALTTV-----SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:PRK11614 101 LAMGGFFAER-----DQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-186 |
9.61e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.42 E-value: 9.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 27 CIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL----RRevvMLGQTppifD-GTIKDNLLMGLRFSEKP 101
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRR---RLLRT----EwGFVHQHPRDGLRMQVSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 FPN-----------------DDALQGaLTTVSLD-KKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:PRK11701 109 GGNigerlmavgarhygdirATAGDW-LERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQ 187
|
170 180
....*....|....*....|...
gi 487961256 164 RRVMKQFTLLAREKKKTVIFITH 186
Cdd:PRK11701 188 ARLLDLLRGLVRELGLAVVIVTH 210
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
10-201 |
1.64e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 72.68 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRML--NDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLG-QTPPIFDGT 86
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPDERARAGLFLAfQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLL---MGLRFSEKPFPNDDALQgalttvsLDKKLEDNASSL---------------SGGEKQRLAFARIILMDPPV 148
Cdd:TIGR01978 93 SNLEFLrsaLNARRSARGEEPLDLLD-------FEKLLKEKLALLdmdeeflnrsvnegfSGGEKKRNEILQMALLEPKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 149 YLLDEPTSALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:TIGR01978 166 AILDEIDSGLDIDALKIVAEGINRL-REPDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-186 |
1.89e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.30 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 5 KDITYKDILHIPYLQIQKEKTTCIIGESGSGKSTLL-----RMLNDlqSPTSGTIEYNGKSIldyPPIQLRREVVMLGQT 79
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNGQPR---KPDQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDG-TIKDNLLMGLRFSeKPFPNDDALQGALTTVSLDKKLED------NASSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:cd03234 90 DILLPGlTVRETLTYTAILR-LPRKSSDAIRKKRVEDVLLRDLALtriggnLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 153 EPTSALDGDTERRVMKQFTLLAReKKKTVIFITH 186
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIH 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-159 |
2.12e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLqSPTSGTIEYNGKSILDYPPIQLRREVVMLGQ--TPPIfdgtikdnlLMG----LRFSEKP 101
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQqqTPPF---------AMPvfqyLTLHQPD 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 102 FPNDDALQGALTTVS----LDKKLEDNASSLSGGEKQRLAFARIILMDPP-------VYLLDEPTSALD 159
Cdd:PRK03695 97 KTRTEAVASALNEVAealgLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLD 165
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-186 |
2.42e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 13 LHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDL----QSPTS------GTIEYNGKSILDyppIQLRRevvmlGQTPPI 82
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGShiellgRTVQREGRLARD---IRKSR-----ANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDG-------TIKDNLLMGLRFSE----------KPFPNDDALQgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMD 145
Cdd:PRK09984 92 FQQfnlvnrlSVLENVLIGALGSTpfwrtcfswfTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 146 PPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITH 186
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLH 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-159 |
2.45e-15 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.81 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 30 GESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ-LRREVVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPN-DD 106
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTVEENILAVLEIRGLSKKErEE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 107 ALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:cd03218 113 KLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-186 |
2.69e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIeYNGKSILdYPPiqlrrevvmlgQTPPIFDGTIKD 89
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIA-YVP-----------QQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMglrfsekpFPNDDA--LQGALTTVSLDKKLE-----------DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:PTZ00243 740 NILF--------FDEEDAarLADAVRVSQLEADLAqlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190
....*....|....*....|....*....|
gi 487961256 157 ALDGDTERRVMKQfTLLAREKKKTVIFITH 186
Cdd:PTZ00243 812 ALDAHVGERVVEE-CFLGALAGKTRVLATH 840
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-213 |
3.13e-15 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 70.43 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLrmlndlqsptSGTIEYNGKSIL-DYPPIQLRREVVMLGQTPPIFDgtikdnllMGLr 96
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLV----------NEGLYASGKARLiSFLPKFSRNKLIFIDQLQFLID--------VGL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 fsekpfpnddalqGALTtvsldkkLEDNASSLSGGEKQRLAFARIILMDPP--VYLLDEPTSALDGDTERRVMKQFTLLa 174
Cdd:cd03238 77 -------------GYLT-------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL- 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 487961256 175 REKKKTVIFITHSQQLPEEiADDIIEISKTNGATRKEVL 213
Cdd:cd03238 136 IDLGNTVILIEHNLDVLSS-ADWIIDFGPGSGKSGGKVV 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-203 |
5.97e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.12 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 11 DILHIPYLQIQkekTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI---LDyppiQLRREVVMLGQTPPIFDG-T 86
Cdd:TIGR01257 947 DRLNITFYENQ---ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnLD----AVRQSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLLMGLRFSEKPFpnDDA---LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSW--EEAqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487961256 164 RRVMKqfTLLAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:TIGR01257 1098 RSIWD--LLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-202 |
7.17e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.62 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRML-NDLQsPTSGTIEYNGKSILDYPPIQLRREvvmlgqtppiFDGTIkdNLLMGLRFSEKPFPNDD 106
Cdd:PRK15064 350 IIGENGVGKTTLLRTLvGELE-PDSGTVKWSENANIGYYAQDHAYD----------FENDL--TLFDWMSQWRQEGDDEQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 ALQGALTTV--SLD--KKledNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgdterrvMKQFTLL--AREK-KK 179
Cdd:PRK15064 417 AVRGTLGRLlfSQDdiKK---SVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLnmALEKyEG 486
|
170 180
....*....|....*....|...
gi 487961256 180 TVIFITHSQQLPEEIADDIIEIS 202
Cdd:PRK15064 487 TLIFVSHDREFVSSLATRIIEIT 509
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-159 |
7.57e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 70.77 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYP-PIQLRREVVMLGQTPPIFDG-TIKDNLLMGL 95
Cdd:TIGR04406 22 LSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmHERARLGIGYLPQEASIFRKlTVEENIMAVL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 96 RFSEKPfpnDDALQGALTTVSLDK----KLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:TIGR04406 102 EIRKDL---DRAEREERLEALLEEfqisHLRDNkAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-203 |
9.64e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.44 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQ-TPPIFDGTIKDNLLMGLR 96
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQkTQLWWDLPVIDSFYLLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 -FSEKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAR 175
Cdd:cd03267 122 iYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNR 201
|
170 180
....*....|....*....|....*...
gi 487961256 176 EKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:cd03267 202 ERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-186 |
1.13e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPPIQlrREVVMlgQTppifDG-----TIKDNLL 92
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAE--RGVVF--QN----EGllpwrNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLRFSEKPFPNDDAL-QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTeRRVMKQFT 171
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT-REQMQTLL 171
|
170
....*....|....*.
gi 487961256 172 L-LAREKKKTVIFITH 186
Cdd:PRK11248 172 LkLWQETGKQVLLITH 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-199 |
1.41e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.00 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRevvmlgqtppifdgtikdnllMGLRFsekpFPNDDA 107
Cdd:cd03215 31 IAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR---------------------AGIAY----VPEDRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 LQGALTTVSLdkklEDN---ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD-GDTE--RRVMKQftllAREKKKTV 181
Cdd:cd03215 86 REGLVLDLSV----AENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvGAKAeiYRLIRE----LADAGKAV 157
|
170 180
....*....|....*....|
gi 487961256 182 IFIthSQQLPE--EIADDII 199
Cdd:cd03215 158 LLI--SSELDEllGLCDRIL 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-198 |
1.97e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRevvmLG-----QTPPIFDG-TIKDNLLMGLRFSEKP 101
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ----LGiylvpQEPLLFPNlSVKENILFGLPKRQAS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 FPNDDALQGALtTVSLDkkLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD-GDTERRVMKQFTLLAreKKKT 180
Cdd:PRK15439 118 MQKMKQLLAAL-GCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLA--QGVG 192
|
170 180
....*....|....*....|
gi 487961256 181 VIFITHsqQLPE--EIADDI 198
Cdd:PRK15439 193 IVFISH--KLPEirQLADRI 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3-199 |
2.04e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 70.27 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 3 ILKDITYKdilhipylqIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKsiLDYPPiqlrrevvmlgQTPPI 82
Cdd:cd03291 52 VLKNINLK---------IEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSS-----------QFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDNLLMGLRFSEKPFPN-DDALQGALTTVSLDKK----LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSA 157
Cdd:cd03291 110 MPGTIKENIIFGVSYDEYRYKSvVKACQLEEDITKFPEKdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 158 LDGDTERRVMKQFT--LLArekKKTVIFITHS-QQLpeEIADDII 199
Cdd:cd03291 190 LDVFTEKEIFESCVckLMA---NKTRILVTSKmEHL--KKADKIL 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-199 |
3.38e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 25 TTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQTP-----PIFdgTIKDNLLMGLR 96
Cdd:PRK15079 49 TLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPlaslnPRM--TIGEIIAEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPFPND---DALQGALTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTL 172
Cdd:PRK15079 127 TYHPKLSRQevkDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
170 180
....*....|....*....|....*..
gi 487961256 173 LAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK15079 207 LQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-189 |
3.47e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKST----LLRMLNdlqspTSGTIEYNGKSILDYPPIQL---RREVVMLGQTPpifDGTIKDNLLM------G 94
Cdd:PRK15134 317 LVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSLNPRLNVlqiieeG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 LRFSEKPFP---NDDALQGALTTVSLDKKLEDN-ASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgdteRRVMKQ- 169
Cdd:PRK15134 389 LRVHQPTLSaaqREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQi 464
|
170 180
....*....|....*....|...
gi 487961256 170 FTLLAREKKK---TVIFITHSQQ 189
Cdd:PRK15134 465 LALLKSLQQKhqlAYLFISHDLH 487
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-206 |
4.70e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSptsgtiEYNGKSILdyppiQLRREVVMLGQTPPIFDG-TIKDNLLMGL--------RFS 98
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDK------DFNGEARP-----QPGIKVGYLPQEPQLDPTkTVRENVEEGVaeikdaldRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 99 E------KPFPNDDAL---QGALTTV-------SLDKKLE------------DNASSLSGGEKQRLAFARIILMDPPVYL 150
Cdd:TIGR03719 105 EisakyaEPDADFDKLaaeQAELQEIidaadawDLDSQLEiamdalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 151 LDEPTSALDGDT----ERRVmkqftllaREKKKTVIFITHSQQLPEEIADDIIEISKTNG 206
Cdd:TIGR03719 185 LDEPTNHLDAESvawlERHL--------QEYPGTVVAVTHDRYFLDNVAGWILELDRGRG 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-185 |
5.98e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLR-MLNDLqSPTSGTIeyngksildyppIQLRREVVMLGQTPPIFDGTIKDNLLMGLRFsekpfpNDD 106
Cdd:PLN03130 648 IVGSTGEGKTSLISaMLGEL-PPRSDAS------------VVIRGTVAYVPQVSWIFNATVRDNILFGSPF------DPE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 ALQGALTTVSLDKKLE-----------DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKqfTLLAR 175
Cdd:PLN03130 709 RYERAIDVTALQHDLDllpggdlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKD 786
|
170
....*....|.
gi 487961256 176 E-KKKTVIFIT 185
Cdd:PLN03130 787 ElRGKTRVLVT 797
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-186 |
6.29e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSP---TSGTIEYNGKSIlDYPPIQLRREVVmlgQTPPIFDG--TIKDNLL------MGLR 96
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKEMRAISAYV---QQDDLFIPtlTVREHLMfqahlrMPRR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 FSEKPfpNDDALQGALTTVSLDK------KLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQF 170
Cdd:TIGR00955 132 VTKKE--KRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL 209
|
170
....*....|....*.
gi 487961256 171 TLLArEKKKTVIFITH 186
Cdd:TIGR00955 210 KGLA-QKGKTIICTIH 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-196 |
7.36e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQTPPIF-DGTIKDNLLM 93
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFtDMNVFDNVAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 GLR-FSEKPFPN-DDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFT 171
Cdd:PRK11831 108 PLReHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIS 187
|
170 180
....*....|....*....|....*..
gi 487961256 172 LLAREKKKTVIFITHSqqLPE--EIAD 196
Cdd:PRK11831 188 ELNSALGVTCVVVSHD--VPEvlSIAD 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-186 |
1.52e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLlmglrfseKPF--PND 105
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV--------DPFleASS 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 106 DALQGALTTVSL-----------DKKLEDNASSLSGGEKQRLAFARIIL-MDPPVYLLDEPTSALDGDTERRVmkQFTLL 173
Cdd:PTZ00243 1413 AEVWAALELVGLrervasesegiDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQI--QATVM 1490
|
170
....*....|...
gi 487961256 174 AREKKKTVIFITH 186
Cdd:PTZ00243 1491 SAFSAYTVITIAH 1503
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-203 |
1.61e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLR-MLNDLQSPTSGTIEyngksildyppiqLRREVVMLGQTPPIFDGTIKDNLLMGLR 96
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVV-------------IRGSVAYVPQVSWIFNATVRENILFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 97 F-SEKPFPNDD--ALQGALTTVSLDKKLE--DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkqFT 171
Cdd:PLN03232 705 FeSERYWRAIDvtALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV---FD 781
|
170 180 190
....*....|....*....|....*....|....*
gi 487961256 172 LLARE--KKKTVIFITHSQQ-LPeeIADDIIEISK 203
Cdd:PLN03232 782 SCMKDelKGKTRVLVTNQLHfLP--LMDRIILVSE 814
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-196 |
3.87e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI--LDyPPIQLRREVVMLGQTPPIFDG-TIKDNLLMG 94
Cdd:PRK09700 26 LTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLD-HKLAAQLGIGIIYQELSVIDElTVLENLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 LRFSEKPFPND--------DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgdTERRV 166
Cdd:PRK09700 105 RHLTKKVCGVNiidwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEV 181
|
170 180 190
....*....|....*....|....*....|..
gi 487961256 167 MKQFTLLAREKK--KTVIFITHSQQLPEEIAD 196
Cdd:PRK09700 182 DYLFLIMNQLRKegTAIVYISHKLAEIRRICD 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-190 |
4.93e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.47 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPiqlrrevvmlgQTPPIFDGTIKDNLLMGLR---FSEKPFPN 104
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVP-----------QRPYMTLGTLRDQIIYPDSsedMKRRGLSD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 105 DDaLQGALTTVSLDKKLEDNAS---------SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKqftlLAR 175
Cdd:TIGR00954 552 KD-LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR----LCR 626
|
170
....*....|....*
gi 487961256 176 EKKKTVIFITHSQQL 190
Cdd:TIGR00954 627 EFGITLFSVSHRKSL 641
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-198 |
4.95e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSiLDYPP---IQLRREVVMLGQTP--PIFDGTIKDNLL 92
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-LDYSKrglLALRQQVATVFQDPeqQIFYTDIDSDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLR---FSEKPFPN--DDALqgalTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD--GDTE-- 163
Cdd:PRK13638 101 FSLRnlgVPEAEITRrvDEAL----TLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpaGRTQmi 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 487961256 164 ---RRVMKQftllarekKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK13638 177 aiiRRIVAQ--------GNHVIISSHDIDLIYEISDAV 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-186 |
5.24e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIkdnllmglRFSEKPFP--ND 105
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTV--------RFNIDPFSehND 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 106 DALQGAL-----------TTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKqfTLLA 174
Cdd:PLN03232 1339 ADLWEALerahikdvidrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR--TIRE 1416
|
170
....*....|..
gi 487961256 175 REKKKTVIFITH 186
Cdd:PLN03232 1417 EFKSCTMLVIAH 1428
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
10-159 |
7.36e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRrevvmLGQTPPIfdgTIKD 89
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-----LDTTLPL---TVNR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 90 NLLMglrfseKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:PRK09544 89 FLRL------RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-196 |
7.98e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYN-GKSILDY--PPIQLR----REVVMLGQTPPIF-DGTIKDNLL--MGLRF 97
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMtkPGPDGRgrakRYIGILHQEYDLYpHRTVLDNLTeaIGLEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 sekpfPNDDALQGA---LTTVSLDKK-----LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ 169
Cdd:TIGR03269 395 -----PDELARMKAvitLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
170 180
....*....|....*....|....*...
gi 487961256 170 FtLLAREK-KKTVIFITHSQQLPEEIAD 196
Cdd:TIGR03269 470 I-LKAREEmEQTFIIVSHDMDFVLDVCD 496
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-161 |
9.77e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 30 GESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDyppIQLRREVVMLGQTPPI-FDGTIKDNL-----LMGLRFSEKPfp 103
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLkADLSTLENLhflcgLHGRRAKQMP-- 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 104 nddalQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:PRK13543 119 -----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-198 |
1.07e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL-RREVVMLGQTPPIF-DGTIKDNLLM-- 93
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFrEMTVIENLLVaq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 ----------GL------RFSEKpfpndDALQGA---LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEP 154
Cdd:PRK11300 106 hqqlktglfsGLlktpafRRAES-----EALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 155 TSALDgDTERRVMKQF-TLLAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK11300 181 AAGLN-PKETKELDELiAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
30-159 |
1.62e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.28 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 30 GESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ-LRREVVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPNDDA 107
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKrARLGIGYLPQEASIFRKlTVEDNILAVLELRKLSKKEREE 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 487961256 108 -LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:COG1137 116 rLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-199 |
1.89e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGK----------SILDYPPIQLRR----EVVMLGQTP--- 80
Cdd:PRK10261 37 FSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHvrgaDMAMIFQEPmts 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 81 --PIFdgTIKDNLLMGLRFSEKpFPNDDALQGALTTVSLDKKLEDNA------SSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:PRK10261 117 lnPVF--TVGEQIAESIRLHQG-ASREEAMVEAKRMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487961256 153 EPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-186 |
2.03e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 25 TTCIIGESGSGKSTLLRMLNDLQSP---TSGTIEYNGKSILDYPPIQLRR----EVVMLGQTP-----PIFdgTIKDNL- 91
Cdd:PRK09473 44 TLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKlraeQISMIFQDPmtslnPYM--RVGEQLm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 --LM---GLRFSEKpFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRV 166
Cdd:PRK09473 122 evLMlhkGMSKAEA-FEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 200
|
170 180
....*....|....*....|
gi 487961256 167 MKQFTLLAREKKKTVIFITH 186
Cdd:PRK09473 201 MTLLNELKREFNTAIIMITH 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-198 |
2.05e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSP----TSGTIEYNGKSILdypPIQLR-REVVMLGQTP-----PIFdgTI 87
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA---PCALRgRKIATIMQNPrsafnPLH--TM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 88 KDNLLMGLRFSEKPfPNDDALQGALTTVSLD---KKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTER 164
Cdd:PRK10418 99 HTHARETCLALGKP-ADDATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177
|
170 180 190
....*....|....*....|....*....|....
gi 487961256 165 RVMKQFTLLAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK10418 178 RILDLLESIVQKRALGMLLVTHDMGVVARLADDV 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-196 |
2.54e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 30 GESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPPIQLRREVVMLGQTPPIFDG-TIKDNLLMGLRFSEKPFPNDDal 108
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSGINPYlTLRENCLYDIHFSPGAVGITE-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 109 qgALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgdtERRVMKQFTLL-AREKKKTVIFITHS 187
Cdd:PRK13540 111 --LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIITKIqEHRAKGGAVLLTSH 185
|
....*....
gi 487961256 188 QQLPEEIAD 196
Cdd:PRK13540 186 QDLPLNKAD 194
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-186 |
3.47e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.82 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRevvmlgQTPPIF-DGTIKDNLLmGLRfsekPFPNDD 106
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ------LFSAVFsDFHLFDRLL-GLD----GEADPA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 ALQGALTTVSLDKK--LEDNASS---LSGGEKQRLAFARIILMDPPVYLLDEptSALDGDTE-RRVmkqF--TLLA--RE 176
Cdd:COG4615 432 RARELLERLELDHKvsVEDGRFSttdLSQGQRKRLALLVALLEDRPILVFDE--WAADQDPEfRRV---FytELLPelKA 506
|
170
....*....|
gi 487961256 177 KKKTVIFITH 186
Cdd:COG4615 507 RGKTVIAISH 516
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-204 |
3.64e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 7 ITYKD---ILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIeyngkSILDYPPIQLRRE--VVMLGQTPP 81
Cdd:PRK15056 14 VTWRNghtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKnlVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 I---FDGTIKDNLLMG----LRFSEKPFPNDDA-LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDE 153
Cdd:PRK15056 89 VdwsFPVLVEDVVMMGryghMGWLRRAKKRDRQiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487961256 154 PTSALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEIADDIIEISKT 204
Cdd:PRK15056 169 PFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGT 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-199 |
5.05e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 20 IQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSiLDYPPIQLRREVV-MLGQTPP-----------IFDGTI 87
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP-LHFGDYSYRSQRIrMIFQDPStslnprqrisqILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 88 KDNLLMGLRFSEKpfpnddALQGALTTVSLdkkLEDNAS----SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE 163
Cdd:PRK15112 115 RLNTDLEPEQREK------QIIETLRQVGL---LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 487961256 164 RRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-186 |
7.08e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 21 QKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIE-----------YNGKSILDYppiqLRR------EVVMLGQ----T 79
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQDY----FKKlangeiKVAHKPQyvdlI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 80 PPIFDGTIKDnLLMglRFSEKpfpndDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:COG1245 173 PKVFKGTVRE-LLE--KVDER-----GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 160 gDTER----RVMKQFTllarEKKKTVIFITH 186
Cdd:COG1245 245 -IYQRlnvaRLIRELA----EEGKYVLVVEH 270
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-186 |
1.01e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKDITykdilhipyLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPP 81
Cdd:TIGR00957 1300 LVLRHIN---------VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 IFDGTIKDNLLMGLRFSEKPFPNDDALQGALTTVS-----LDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:TIGR00957 1371 LFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSalpdkLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190
....*....|....*....|....*....|
gi 487961256 157 ALDGDTERRVmkQFTLLAREKKKTVIFITH 186
Cdd:TIGR00957 1451 AVDLETDNLI--QSTIRTQFEDCTVLTIAH 1478
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-169 |
1.35e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.18 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTL----LRMLNdlqspTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNL------------ 91
Cdd:cd03289 35 LLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLdpygkwsdeeiw 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 ----LMGLRFSEKPFPNddalqgalttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE---R 164
Cdd:cd03289 110 kvaeEVGLKSVIEQFPG-----------QLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYqviR 178
|
....*
gi 487961256 165 RVMKQ 169
Cdd:cd03289 179 KTLKQ 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-195 |
1.68e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 24 KTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQL---RREVVMLGQTPPifdGTIKDNLLMGLRFSEk 100
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDPY---ASLDPRQTVGDSIME- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 101 PFPNDDALQGALTTVSLDKKLE------DNA----SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQF 170
Cdd:PRK10261 427 PLRVHGLLPGKAAAARVAWLLErvgllpEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180
....*....|....*....|....*
gi 487961256 171 TLLAREKKKTVIFITHSQQLPEEIA 195
Cdd:PRK10261 507 LDLQRDFGIAYLFISHDMAVVERIS 531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-169 |
1.69e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSpTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNL---------------- 91
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdpyeqwsdeeiwkvae 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 LMGLRFSEKPFPNddalqgalttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE---RRVMK 168
Cdd:TIGR01271 1329 EVGLKSVIEQFPD-----------KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLqiiRKTLK 1397
|
.
gi 487961256 169 Q 169
Cdd:TIGR01271 1398 Q 1398
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-186 |
1.74e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSptsgtiEYNGKSILDyPPIQlrreVVMLGQTPPIFDG-TIKDNLLMGL--------RFS 98
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDK------EFEGEARPA-PGIK----VGYLPQEPQLDPEkTVRENVEEGVaevkaaldRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 99 E------KPFPNDDAL---QGALTTV-------SLDKKLEDNA------------SSLSGGEKQRLAFARIILMDPPVYL 150
Cdd:PRK11819 107 EiyaayaEPDADFDALaaeQGELQEIidaadawDLDSQLEIAMdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLL 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 487961256 151 LDEPTSALDGDTerrV--MKQFTllaREKKKTVIFITH 186
Cdd:PRK11819 187 LDEPTNHLDAES---VawLEQFL---HDYPGTVVAVTH 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-186 |
1.80e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 12 ILHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIkdnl 91
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTV---- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 lmglRFSEKPFP--NDDALQGAL-----------TTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:PLN03130 1330 ----RFNLDPFNehNDADLWESLerahlkdvirrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190
....*....|....*....|....*....|
gi 487961256 159 DGDTERRVMKQFtllaREKKK--TVIFITH 186
Cdd:PLN03130 1406 DVRTDALIQKTI----REEFKscTMLIIAH 1431
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-186 |
5.67e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNdlqsptsgtieynGKSILDYPPIQLRREVVM--LGQTPP------IFD----- 84
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILN-------------GEVLLDDGRIIYEQDLIVarLQQDPPrnvegtVYDfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 85 -GTIKDNL--------LMGLRFSEKPFPNDDALQGALTTV---SLDKKLEDNA-----------SSLSGGEKQRLAFARI 141
Cdd:PRK11147 91 iEEQAEYLkryhdishLVETDPSEKNLNELAKLQEQLDHHnlwQLENRINEVLaqlgldpdaalSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487961256 142 ILMDPPVYLLDEPTSALDGDTeRRVMKQFTLlarEKKKTVIFITH 186
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIET-IEWLEGFLK---TFQGSIIFISH 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-159 |
9.16e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 24 KTTCIIGESGSGKSTLLRMLNDLQSPTSGTI-----------EYNGKSILDY------PPIQLRREVVMLGQTPPIFDGT 86
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYftklleGDVKVIVKPQYVDLIPKAVKGK 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 87 IKDNLlmglrfseKPFPNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:cd03236 107 VGELL--------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-202 |
1.19e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 13 LHIPYLQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGksildyppiqlrrEVVMLGQTPPIFDGTIKDNLL 92
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 93 MGLRFSEKPFpnddalQGALTTVSLDKKLE-----------DNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD 161
Cdd:TIGR00957 721 FGKALNEKYY------QQVLEACALLPDLEilpsgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 162 TERRVMKQFT----LLareKKKTVIFITHSQQ-LPEeiADDIIEIS 202
Cdd:TIGR00957 795 VGKHIFEHVIgpegVL---KNKTRILVTHGISyLPQ--VDVIIVMS 835
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
24-203 |
1.28e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.77 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 24 KTTCIIGESGSGKSTLLRML-NDLQSPTSGTIEYNGKSILDYPPIQLRREVVmlgqtppifdgtikdnllmglrfsekpf 102
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIV---------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 pnddalqgalttvsldkklEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTL-----LAREK 177
Cdd:smart00382 55 -------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSEK 115
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 178 KKTVIFITHSQQLPEE-----IADDIIEISK 203
Cdd:smart00382 116 NLTVILTTNDEKDLGPallrrRFDRRIVLLL 146
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-199 |
3.44e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 33 GSGKSTLLRMLNDLQSPTSGTIEYNGKSI-LDYPPIQLRREVVMLgqtpP--------IFDGTIKDNLLMGL--RFSEKP 101
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVrIRSPRDAIRAGIAYV----PedrkgeglVLDLSIRENITLASldRLSRGG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 FPNDDALQGALTTV--SLDKK---LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTsaldgdteR-----------R 165
Cdd:COG1129 364 LLDRRRERALAEEYikRLRIKtpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT--------RgidvgakaeiyR 435
|
170 180 190
....*....|....*....|....*....|....*.
gi 487961256 166 VMKQftlLAREkKKTVIFIthSQQLPE--EIADDII 199
Cdd:COG1129 436 LIRE---LAAE-GKAVIVI--SSELPEllGLSDRIL 465
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-159 |
3.85e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.19 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTppiFDGTIKDNllmgLRFSEKPFPND 105
Cdd:PRK13541 29 TYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLK---LEMTVFEN----LKFWSEIYNSA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 487961256 106 DALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:PRK13541 102 ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-198 |
4.47e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQ--------LRREVVMLGQTppifdgTIKDNLLMGLRFS- 98
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQL------TIAENIFLGREFVn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 99 -------EKPFPNDDALqgaLTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL-DGDTER--RVMK 168
Cdd:PRK10762 109 rfgridwKKMYAEADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESlfRVIR 185
|
170 180 190
....*....|....*....|....*....|
gi 487961256 169 QFtllaREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK10762 186 EL----KSQGRGIVYISHRLKEIFEICDDV 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-199 |
6.50e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 5 KDITYKDILHIPYlQIQKEKTTCIIGESGSGKS-TLLRMLNDLQSP---TSGTIEYNGKSILDYPPIQLRR----EVVML 76
Cdd:PRK11022 16 ESAPFRAVDRISY-SVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNlvgaEVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 77 GQTP-----PIFdgTIKDNLLMGLRFSE---KPFPNDDALQgALTTVSL---DKKLEDNASSLSGGEKQRLAFARIILMD 145
Cdd:PRK11022 95 FQDPmtslnPCY--TVGFQIMEAIKVHQggnKKTRRQRAID-LLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487961256 146 PPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-186 |
7.46e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRevvmlgqtppIFDGTIKDNLLMGLRF 97
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----------LFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 98 SEKPFPNDDAL-QGALTTVSLDKKL--EDNASS---LSGGEKQRLAFARIILMDPPVYLLDEptSALDGDTE-RRVMKQF 170
Cdd:PRK10522 414 GPEGKPANPALvEKWLERLKMAHKLelEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE--WAADQDPHfRREFYQV 491
|
170
....*....|....*..
gi 487961256 171 TL-LAREKKKTVIFITH 186
Cdd:PRK10522 492 LLpLLQEMGKTIFAISH 508
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-189 |
1.36e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILdyppIQLRREVVMLGQTPPiFDG-----TIKDNLLMGLRFSEKPF 102
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQNMGYCPQ-FDAiddllTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 PNDDALQG-ALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREkKKTV 181
Cdd:TIGR01257 2045 EEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAV 2123
|
....*...
gi 487961256 182 IFITHSQQ 189
Cdd:TIGR01257 2124 VLTSHSME 2131
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-212 |
1.69e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRRE-------------VVMlgqtppifDGTIKDNLLMG 94
Cdd:COG3845 289 IAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedrlgrgLVP--------DMSVAENLILG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 L----RFSEKPFPNDDALQgALT----------TVSLDkkleDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD- 159
Cdd:COG3845 361 RyrrpPFSRGGFLDRKAIR-AFAeelieefdvrTPGPD----TPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDv 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487961256 160 GDTE---RRVMKqftllAREKKKTVIFIthSQQLPE--EIADDII-----EIS---KTNGATRKEV 212
Cdd:COG3845 436 GAIEfihQRLLE-----LRDAGAAVLLI--SEDLDEilALSDRIAvmyegRIVgevPAAEATREEI 494
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-186 |
2.06e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 24 KTTCIIGESGSGKSTLLRML--------NDLQSPTS--GTIE-YNGKSILDYppiqLRR------EVV----MLGQTPPI 82
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSwdEVLKrFRGTELQNY----FKKlyngeiKVVhkpqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 FDGTIKDnLLMGlrfsekpfpNDDAlqGALTTV----SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSAL 158
Cdd:PRK13409 176 FKGKVRE-LLKK---------VDER--GKLDEVverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 159 DgDTER-RVMKqftlLARE--KKKTVIFITH 186
Cdd:PRK13409 244 D-IRQRlNVAR----LIRElaEGKYVLVVEH 269
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
73-199 |
4.25e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 73 VVMLGQtppifDGTIKDNLLMGLRFSEKPFPNDDALQGALTTVSLDKklednaSSLSGGEKQRLAFARIILMDPPVYLLD 152
Cdd:cd03222 28 IGIVGP-----NGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY------IDLSGGELQRVAIAAALLRNATFYLFD 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 487961256 153 EPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDII 199
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-201 |
7.28e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.16 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLrmlNDLQSPTSGTIEYNGKSildyPPIQLRRE--------VVMLGQTPP-------------IFD 84
Cdd:cd03271 24 TCVTGVSGSGKSSLI---NDTLYPALARRLHLKKE----QPGNHDRIeglehidkVIVIDQSPIgrtprsnpatytgVFD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 85 --------------------------GTIKDNLLMGLRFSEKPFPND----DALQgALTTVSLDK-KLEDNASSLSGGEK 133
Cdd:cd03271 97 eirelfcevckgkrynretlevrykgKSIADVLDMTVEEALEFFENIpkiaRKLQ-TLCDVGLGYiKLGQPATTLSGGEA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487961256 134 QRLAFARIILMDPP---VYLLDEPTSALDGDTERRVMKQFTLLArEKKKTVIFITHSQQLPeEIADDIIEI 201
Cdd:cd03271 176 QRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEHNLDVI-KCADWIIDL 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-194 |
1.20e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 30 GESGSGKSTLLRMLNDLQSPTSGTIEYNGKSI-------------------LDYPPIQLRREVVMLGQTPPIFdGTIKDN 90
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaagvaiiyqeLHLVPEMTVAENLYLGQLPHKG-GIVNRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 91 LLMglRFSEkpfpndDALQGALTTVSLDKKLednaSSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDG-DTER--RVM 167
Cdd:PRK11288 116 LLN--YEAR------EQLEHLGVDIDPDTPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQlfRVI 183
|
170 180
....*....|....*....|....*..
gi 487961256 168 KQFtllaREKKKTVIFITHSQqlpEEI 194
Cdd:PRK11288 184 REL----RAEGRVILYVSHRM---EEI 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-198 |
1.22e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPPIQ--LRREVVMLGQT-PPIFDGTIKDNLLMG 94
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKeaLENGISMVHQElNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 95 lRFSEK-PFPNDDAL----QGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgdTERRVMKQ 169
Cdd:PRK10982 98 -RYPTKgMFVDQDKMyrdtKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNHL 173
|
170 180 190
....*....|....*....|....*....|.
gi 487961256 170 FTLLAREKKK--TVIFITHSQQLPEEIADDI 198
Cdd:PRK10982 174 FTIIRKLKERgcGIVYISHKMEEIFQLCDEI 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-203 |
2.54e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.17 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEyngksILDYPPIQLRRE------VVMlGQ-TPPIFDGTIKDNLLM-----GL 95
Cdd:COG4586 53 FIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPFKRRKEfarrigVVF-GQrSQLWWDLPAIDSFRLlkaiyRI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 96 rfsekpfPNDDALQ--GALTTV-SLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmKQFTL 172
Cdd:COG4586 127 -------PDAEYKKrlDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI-REFLK 198
|
170 180 190
....*....|....*....|....*....|..
gi 487961256 173 -LAREKKKTVIFITHSQQLPEEIADDIIEISK 203
Cdd:COG4586 199 eYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-186 |
3.07e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRML-NDLQSPT-SGTIEYNGKSildyPPIQLRREVVMLGQTPPIFDG-TIKDNLLMG--LRFSeKPF 102
Cdd:PLN03211 99 VLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRK----PTKQILKRTGFVTQDDILYPHlTVRETLVFCslLRLP-KSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 PNDDALQGALTTVS------LDKKLEDNA--SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLA 174
Cdd:PLN03211 174 TKQEKILVAESVISelgltkCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170
....*....|..
gi 487961256 175 rEKKKTVIFITH 186
Cdd:PLN03211 254 -QKGKTIVTSMH 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-164 |
4.35e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYppIQLRREVVMLGQT--PPIFDGTikDNLLMGLRFSekpfpND 105
Cdd:TIGR03719 353 VIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAY--VDQSRDALDPNKTvwEEISGGL--DIIKLGKREI-----PS 423
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 106 DALQGALTTVSLDKklEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTER 164
Cdd:TIGR03719 424 RAYVGRFNFKGSDQ--QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
128-206 |
9.21e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 128 LSGGEKQRLAFARII----LMDPPVYLLDEPTSALDGDTERRVMkQFTLLAREKKKTVIFITHSQQLpEEIADDIIEISK 203
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHLVKGAQVIVITHLPEL-AELADKLIHIKK 155
|
...
gi 487961256 204 TNG 206
Cdd:cd03227 156 VIT 158
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-186 |
1.30e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.68 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTL----LRMLNDLQsptsGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTIKDNLLMGLRFSekpfp 103
Cdd:cd03288 52 ICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCT----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 104 nDDALQGALTTVSL-----------DKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTE----RRVMK 168
Cdd:cd03288 123 -DDRLWEALEIAQLknmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilqKVVMT 201
|
170
....*....|....*...
gi 487961256 169 QFTllarekKKTVIFITH 186
Cdd:cd03288 202 AFA------DRTVVTIAH 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-203 |
1.91e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.57 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPT---SGTIEYNGKSILDYPPiQLRREVVMLGQT----PPIfdgTIKDNLlmglRFSEK 100
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE-KYPGEIIYVSEEdvhfPTL---TVRETL----DFALR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 101 pfpnddaLQGalttvsldkklEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKT 180
Cdd:cd03233 110 -------CKG-----------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTT 171
|
170 180
....*....|....*....|....*
gi 487961256 181 ViFITHSQQLPE--EIADDIIEISK 203
Cdd:cd03233 172 T-FVSLYQASDEiyDLFDKVLVLYE 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
117-205 |
2.73e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.14 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 117 LDKKLEDNASSLSGGEKQ------RLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQ-FTLLAREKKKTVIFITHSQQ 189
Cdd:cd03240 105 SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEiIEERKSQKNFQLIVITHDEE 184
|
90
....*....|....*.
gi 487961256 190 LpEEIADDIIEISKTN 205
Cdd:cd03240 185 L-VDAADHIYRVEKDG 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-190 |
2.85e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSildyppiqlrREVVMLGQTPPIFDGTIKDNLLMGLRFSEKPfpnDDA 107
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKV----------RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVP---EQK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 LQGALTTVSLDKKLEDNAS-SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLarekKKTVIFITH 186
Cdd:PLN03073 607 LRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF----QGGVLMVSH 682
|
....
gi 487961256 187 SQQL 190
Cdd:PLN03073 683 DEHL 686
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-162 |
2.98e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 19 QIQKEKTTCIIGESGSGKSTLLR-MLNDLQsPTSGTIEYNGKsildyppiqlrREVVMLGQTPPIFD--GTIKDNL---- 91
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHCGTK-----------LEVAYFDQHRAELDpeKTVMDNLaegk 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 92 ---------------LMGLRFSEKPfpnddalqgALTTVSldkklednasSLSGGEKQRLAFARIILMDPPVYLLDEPTS 156
Cdd:PRK11147 409 qevmvngrprhvlgyLQDFLFHPKR---------AMTPVK----------ALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
....*.
gi 487961256 157 ALDGDT 162
Cdd:PRK11147 470 DLDVET 475
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-186 |
3.23e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 29 IGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSIlDYPPIQLRREVVMLGQTppiF----DGTIKDNLLMGLR-FSekpFP 103
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIATRRRVGYMSQA---FslygELTVRQNLELHARlFH---LP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 104 NDDA---LQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDG---DTERRVMKQftlLAREK 177
Cdd:NF033858 371 AAEIaarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPvarDMFWRLLIE---LSRED 447
|
170
....*....|
gi 487961256 178 KKTvIFI-TH 186
Cdd:NF033858 448 GVT-IFIsTH 456
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
4-201 |
6.05e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 4 LKDITykdilhipyLQIQKEKTTCIIGESGSGKSTL----------LRMLNDLQSPTSGTIEYNGKSILDY-----PPIQ 68
Cdd:cd03270 11 LKNVD---------VDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLGQMDKPDVDSieglsPAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 69 LRREvvMLGQTPPIFDGTIKD-NLLMGLRFSEKPFPNDDALqgaLTTVSLDK-KLEDNASSLSGGEKQRLAFARII---L 143
Cdd:cd03270 82 IDQK--TTSRNPRSTVGTVTEiYDYLRLLFARVGIRERLGF---LVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIgsgL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 144 MDpPVYLLDEPTSALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEiADDIIEI 201
Cdd:cd03270 157 TG-VLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDI 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-201 |
7.76e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 10 KDILHIPYLQIQKEKTTCIIGESGSGKSTLLRML--NDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDGTI 87
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 88 KDNLLMGL------RFSEKP----FPNDDALQGALTTVSLDKKLEDNASSL--SGGEKQRLAFARIILMDPPVYLLDEPT 155
Cdd:PRK09580 94 SNQFFLQTalnavrSYRGQEpldrFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487961256 156 SALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:PRK09580 174 SGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVHV 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-201 |
1.84e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGK----------SILDYPPI-----------QLRREV------------- 73
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetPALPQPALeyvidgdreyrQLEAQLhdanerndghaia 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 74 VMLGQTPPIFDGTIKD---NLLMGLRFSEKpfpnddalqgalttvsldkKLEDNASSLSGGEKQRLAFARIILMDPPVYL 150
Cdd:PRK10636 112 TIHGKLDAIDAWTIRSraaSLLHGLGFSNE-------------------QLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487961256 151 LDEPTSALDGDTE---RRVMKQFTllarekkKTVIFITHSQQLPEEIADDIIEI 201
Cdd:PRK10636 173 LDEPTNHLDLDAViwlEKWLKSYQ-------GTLILISHDRDFLDPIVDKIIHI 219
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-187 |
2.11e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRrevvmlGQTPPIFDGTIKdNLLMGLRFSEKPFPNDDA 107
Cdd:PRK13545 55 IIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLN------GQLTGIENIELK-GLMMGLTKEKIKEIIPEI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 LQGAlttvSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLaREKKKTVIFITHS 187
Cdd:PRK13545 128 IEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHS 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-198 |
2.34e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIE--------YNGKSILDY-----PPIQ-LRRevvmlgQTPPIFDGTIKDnLLM 93
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGlakgiklgYFAQHQLEFlradeSPLQhLAR------LAPQELEQKLRD-YLG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 94 GLRFsekpfpnddalQGalttvsldKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDterrvMKQ-FTL 172
Cdd:PRK10636 416 GFGF-----------QG--------DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQaLTE 471
|
170 180
....*....|....*....|....*.
gi 487961256 173 LAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK10636 472 ALIDFEGALVVVSHDRHLLRSTTDDL 497
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-176 |
2.56e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.08 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRMLNdlQSPTSGTIEynGKSILD-YP-PIQLRREVVMLGQTpPIFDGTIKdnLLMGLRFSEKpfp 103
Cdd:cd03232 36 TALMGESGAGKTTLLDVLA--GRKTAGVIT--GEILINgRPlDKNFQRSTGYVEQQ-DVHSPNLT--VREALRFSAL--- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487961256 104 nddaLQGalttvsldkklednassLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLARE 176
Cdd:cd03232 106 ----LRG-----------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-199 |
3.49e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 33 GSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYPPIQLRREVVMLGQTPPIFDG-----TIKDNLLMGLRFSEKPFpndda 107
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGiipvhSVADNINISARRHHLRA----- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 lqGALttvsLDKKLE-DNASS------------------LSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMK 168
Cdd:PRK11288 364 --GCL----INNRWEaENADRfirslniktpsreqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYN 437
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 169 QFTLLArEKKKTVIFIthSQQLPE--EIADDII 199
Cdd:PRK11288 438 VIYELA-AQGVAVLFV--SSDLPEvlGVADRIV 467
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-164 |
3.61e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYnGKSI-LDYPPiQLRR---------EVVMLGQtppifdgtikDNLLMGLRf 97
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVkLAYVD-QSRDaldpnktvwEEISGGL----------DIIKVGNR- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487961256 98 sEKP---------FPNDDalQGalttvsldKKlednASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTER 164
Cdd:PRK11819 422 -EIPsrayvgrfnFKGGD--QQ--------KK----VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-159 |
4.08e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.04 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 18 LQIQKEKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYP-PIQLRREVVMLGQTPPIFDG-TIKDNLLMGL 95
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYDNLMAVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487961256 96 RF-----SEKPFPNDDALQGALTTVSLDKKLednASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALD 159
Cdd:PRK10895 104 QIrddlsAEQREDRANELMEEFHIEHLRDSM---GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
126-192 |
5.16e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 5.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487961256 126 SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKkktVIFITHSQQLPE 192
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG---VAIIVVSSELAE 465
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
87-190 |
6.73e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.84 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 87 IKDNLLMGLRFSEKPFPNDDALQGA-LTTVSLDKKLEDNASSLSGGEKQRLAFA---RIILMDPPVYLLDEPTSALDGDT 162
Cdd:pfam13304 195 ADLNLSDLGEGIEKSLLVDDRLRERgLILLENGGGGELPAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKL 274
|
90 100
....*....|....*....|....*...
gi 487961256 163 ERRVMKQFTLLAREKKKtVIFITHSQQL 190
Cdd:pfam13304 275 LRRLLELLKELSRNGAQ-LILTTHSPLL 301
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
126-219 |
1.15e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 126 SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAReKKKTVIFIthSQQLPE--EIADDIIEIS- 202
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIII--SSEMPEllGITDRILVMSn 466
|
90 100
....*....|....*....|....
gi 487961256 203 -------KTNGATRKEVLSIEGRY 219
Cdd:PRK10982 467 glvagivDTKTTTQNEILRLASLH 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-189 |
1.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 2 FILKD--ITYKD--ILHIPYLQIQKEKTTCIIGESGSGKSTLLRML---------NDL----QSPTSGT--------IEY 56
Cdd:PRK10938 261 IVLNNgvVSYNDrpILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgRRRGSGEtiwdikkhIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 57 NGKSI-LDYPPIQLRREVVMLGqtppIFDGtikdnllMGLrFSEKPfpndDALQGA----LTTVSLDKKLEDNA-SSLSG 130
Cdd:PRK10938 341 VSSSLhLDYRVSTSVRNVILSG----FFDS-------IGI-YQAVS----DRQQKLaqqwLDILGIDKRTADAPfHSLSW 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487961256 131 GEkQRLAF-ARIILMDPPVYLLDEPTSALDGdTERRVMKQFT-LLAREKKKTVIFITHSQQ 189
Cdd:PRK10938 405 GQ-QRLALiVRALVKHPTLLILDEPLQGLDP-LNRQLVRRFVdVLISEGETQLLFVSHHAE 463
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-203 |
2.12e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 112 LTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREkKKTVIFITHSQQLP 191
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEA 207
|
90
....*....|..
gi 487961256 192 EEIADDIIEISK 203
Cdd:NF000106 208 EQLAHELTVIDR 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-201 |
4.23e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 121 LEDNASSLSGGEKQRLAFARII------LMdppvYLLDEPTSALDGDTERRVMKQFTLLaREKKKTVIFITHSQQLPEEi 194
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIgsgltgVL----YVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA- 555
|
....*..
gi 487961256 195 ADDIIEI 201
Cdd:TIGR00630 556 ADYVIDI 562
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-213 |
4.57e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 121 LEDNASSLSGGEKQRLAFARIILM---DPPVYLLDEPTSALDGDTERRVMKQFTLLArEKKKTVIFITHSQQLPEEiADD 197
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLV-SLGHSVIYIDHDPALLKQ-ADY 1770
|
90
....*....|....*.
gi 487961256 198 IIEISKTNGATRKEVL 213
Cdd:PRK00635 1771 LIEMGPGSGKTGGKIL 1786
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
127-213 |
4.67e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 127 SLSGGEKQ------RLAFARIILMDPPVYLLDEPTSALDGD--TERRVMKQFTLLAREKKKTVIFITHSQQLpEEIADDI 198
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDrrTNLKDIIEYSLKDSSDIPQVIMISHHREL-LSVADVA 879
|
90
....*....|....*
gi 487961256 199 IEISKTNGATRKEVL 213
Cdd:PRK01156 880 YEVKKSSGSSKVIPL 894
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-201 |
5.92e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 5.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487961256 127 SLSGGEKQRLAFARIILMDPPVYLLDEPTSALDgdtERRVMKQFTLLAREkKKTVIFITHSQQLPEEIADDIIEI 201
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKW-PKTFIVVSHAREFLNTVVTDILHL 414
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
102-186 |
6.17e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.45 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 FPNDDA-----LQGALTTV--SLDKKLEdNASSLSGGEKQRLA----FArIILMDP-PVYLLDEPTSALDGDTERRVMKq 169
Cdd:cd03278 82 FDNSDGrysiiSQGDVSEIieAPGKKVQ-RLSLLSGGEKALTAlallFA-IFRVRPsPFCVLDEVDAALDDANVERFAR- 158
|
90
....*....|....*...
gi 487961256 170 ftLLAREKKKT-VIFITH 186
Cdd:cd03278 159 --LLKEFSKETqFIVITH 174
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
26-159 |
1.01e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 41.90 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLLRML--------------NDLQ-----------SPTSGTIEYNGKSILDYPP-------IQLRREV 73
Cdd:cd03273 28 NAITGLNGSGKSNILDAIcfvlgitnlstvraSNLQdliykrgqagiTKASVTIVFDNSDKSQSPIgfenypeITVTRQI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 74 VMLGQTPPIFDGTIKDNLLMGLRFSEKPF----PNDDALQGALTTV-SLDKKLEDNASSLSGGEKQRLAFARIILM---- 144
Cdd:cd03273 108 VLGGTNKYLINGHRAQQQRVQDLFQSVQLnvnnPHFLIMQGRITKVlNMGGVWKESLTELSGGQRSLVALSLILALllfk 187
|
170
....*....|....*
gi 487961256 145 DPPVYLLDEPTSALD 159
Cdd:cd03273 188 PAPMYILDEVDAALD 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
86-206 |
1.04e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 86 TIKDNLLMGLRFSEKPFPNDDALQG---ALTTVSLDK-KLEDNASSLSGGEKQRLAFARIILM---DPPVYLLDEPTSAL 158
Cdd:PRK00635 764 NIADILEMTAYEAEKFFLDEPSIHEkihALCSLGLDYlPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 487961256 159 DG-DTERRVMKQFTLLarEKKKTVIFITHSQQLPeEIADDIIEISKTNG 206
Cdd:PRK00635 844 HThDIKALIYVLQSLT--HQGHTVVIIEHNMHVV-KVADYVLELGPEGG 889
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-186 |
1.21e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487961256 120 KLEDNASSLSGGEKQRLAFARIIL---MDPPVYLLDEPTSALDGDTERRVMkqfTLLAR--EKKKTVIFITH 186
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLL---EVLQRlvDKGNTVVVIEH 890
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
28-193 |
1.30e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 41.58 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIeyngksildyppIQLRREVVMLGQTPPIFDG-TIKDNLLMglRFSEKPFPNDD 106
Cdd:PRK15177 18 ILAAPGSGKTTLTRLLCGLDAPDEGDF------------IGLRGDALPLGANSFILPGlTGEENARM--MASLYGLDGDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 107 ALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkQFTLLAREKKKTVIFITH 186
Cdd:PRK15177 84 FSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRM--QAALACQLQQKGLIVLTH 161
|
....*..
gi 487961256 187 SQQLPEE 193
Cdd:PRK15177 162 NPRLIKE 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
122-215 |
1.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 122 EDNASSLSGGEKQ------RLAFARIILMDPPVYLLDEPTSALDgdtERRVMKQFTLLAREKKK--TVIFITHSQQLpEE 193
Cdd:PRK03918 783 ERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLD---EERRRKLVDIMERYLRKipQVIIVSHDEEL-KD 858
|
90 100
....*....|....*....|..
gi 487961256 194 IADDIIEISKTNGATRKEVLSI 215
Cdd:PRK03918 859 AADYVIRVSLEGGVSKVEVVSL 880
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
121-195 |
1.74e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 1.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487961256 121 LEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLArEKKKTVIFIthSQQLPEEIA 195
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMV--SSELPEIIT 474
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
23-209 |
1.89e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 40.75 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 23 EKTTCIIGESGSGKSTLLRMLNDLQSPTSGTIEYNGKSILDYppiqlrrevvmLGQTPPIFDGTIKdnllmgLRFSEKPF 102
Cdd:cd03239 22 NSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG-----------GGVKAGINSASVE------ITFDKSYF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 PnddALQGALTTVsldkklednassLSGGEKQRLAFARIILM---DP-PVYLLDEPTSALDGDTERRVMKqftLLAREKK 178
Cdd:cd03239 85 L---VLQGKVEQI------------LSGGEKSLSALALIFALqeiKPsPFYVLDEIDAALDPTNRRRVSD---MIKEMAK 146
|
170 180 190
....*....|....*....|....*....|...
gi 487961256 179 KTV--IFITHsQQLPEEIADDIIEISKTNGATR 209
Cdd:cd03239 147 HTSqfIVITL-KKEMFENADKLIGVLFVHGVST 178
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1-43 |
2.69e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 487961256 1 MFILKDITYKDILHI----PYLQIQKEKTTCIIGESGSGKSTLLRML 43
Cdd:PHA02562 1 MLKFKKIRYKNILSVgnqpIEIQLDKVKKTLITGKNGAGKSTMLEAL 47
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
126-192 |
4.76e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 4.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487961256 126 SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREkKKTVIFIthSQQLPE 192
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI--SSELPE 467
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-201 |
8.17e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.81 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 30 GESGSGKSTLLRMLNDLQSptSGTieYNGKSILDYPPIQL-------RREVVMLGQTPPIF-DGTIKDNLLMGLRFSEKP 101
Cdd:TIGR02633 34 GENGAGKSTLMKILSGVYP--HGT--WDGEIYWSGSPLKAsnirdteRAGIVIIHQELTLVpELSVAENIFLGNEITLPG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 102 FPNDDAL-----QGALTTVSLDK-KLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALdgdTERRVMKQFTLLAR 175
Cdd:TIGR02633 110 GRMAYNAmylraKNLLRELQLDAdNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL---TEKETEILLDIIRD 186
|
170 180
....*....|....*....|....*...
gi 487961256 176 EKKKTV--IFITHSQQLPEEIADDIIEI 201
Cdd:TIGR02633 187 LKAHGVacVYISHKLNEVKAVCDTICVI 214
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-213 |
1.23e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 126 SSLSGGEKQRLAFARII---LMDpPVYLLDEPTSALD-GDTER--RVMKQFtllaREKKKTVIFITHSQQLPeEIADDII 199
Cdd:PRK00635 475 ATLSGGEQERTALAKHLgaeLIG-ITYILDEPSIGLHpQDTHKliNVIKKL----RDQGNTVLLVEHDEQMI-SLADRII 548
|
90
....*....|....
gi 487961256 200 EISKTNGATRKEVL 213
Cdd:PRK00635 549 DIGPGAGIFGGEVL 562
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
128-198 |
1.50e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 1.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487961256 128 LSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVMKQFTLLAREKKKTVIFITHSQQLPEEIADDI 198
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
26-209 |
1.78e-03 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 38.05 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLL------------RM----LNDL-------QSPTSGTIEYNGKSILDYPpiQLRREvvmlgqtppi 82
Cdd:cd03274 28 SAIVGPNGSGKSNVIdsmlfvfgfrasKMrqkkLSDLihnsaghPNLDSCSVEVHFQEIIDKP--LLKSK---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 83 fdgtikdnllmGLRFSEKPFPnddALQGALTTVSL-DKKLEDNASSLSGGEKQ----RLAFARIILMDPPVYLLDEPTSA 157
Cdd:cd03274 96 -----------GIDLDHNRFL---ILQGEVEQIAQmPKKSWKNISNLSGGEKTlsslALVFALHHYKPTPLYVMDEIDAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487961256 158 LDgdterrvMKQFTLLA---REKKKTVIFITHSqqLPE---EIADDIIEISKTNGATR 209
Cdd:cd03274 162 LD-------FRNVSIVAnyiKERTKNAQFIVIS--LRNnmfELADRLVGIYKTNNCTK 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
128-192 |
1.87e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.83 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487961256 128 LSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkqFTLLAREKKKTVIFITHSQQLPE 192
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI---YQLINQFKAEGLSIILVSSEMPE 457
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-187 |
1.95e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.26 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 28 IIGESGSGKSTLLRMLNDLQSPTSGTIEYNGksilDYPPIQLrrEVVMLGQTPPIFDGTIKdNLLMGlrFSEKPFpndDA 107
Cdd:PRK13546 55 LVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAI--SAGLSGQLTGIENIEFK-MLCMG--FKRKEI---KA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 108 LQGALTTVS-LDKKLEDNASSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGD-TERRVMKQFTLlaREKKKTVIFIT 185
Cdd:PRK13546 123 MTPKIIEFSeLGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQKCLDKIYEF--KEQNKTIFFVS 200
|
..
gi 487961256 186 HS 187
Cdd:PRK13546 201 HN 202
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-202 |
2.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 105 DDALQGALTTVSLDK-----KLEdnasSLSGGEKQRLAFARI----ILMDPPVYLLDEPTSALDGDTERRVMKqftlLAR 175
Cdd:TIGR02169 1051 DDPFAGGLELSAKPKgkpvqRLE----AMSGGEKSLTALSFIfaiqRYKPSPFYAFDEVDMFLDGVNVERVAK----LIR 1122
|
90 100
....*....|....*....|....*...
gi 487961256 176 EKKKTVIFITHSQQLPE-EIADDIIEIS 202
Cdd:TIGR02169 1123 EKAGEAQFIVVSLRSPMiEYADRAIGVT 1150
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-62 |
3.02e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 3.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487961256 1 MFIlKDITYKDILHIPYLQI---QKEKTTCIIGESGSGKSTLLRMLND-LQSPTSGTIEYNGKSIL 62
Cdd:COG3950 1 MRI-KSLTIENFRGFEDLEIdfdNPPRLTVLVGENGSGKTTLLEAIALaLSGLLSRLDDVKFRKLL 65
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
26-186 |
3.45e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.30 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 26 TCIIGESGSGKSTLL---------------RMLNDLQSPTSG------TIEYNGKSIldyppiQLRR---EVVMLGQTPP 81
Cdd:COG0419 26 NLIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEeasvelEFEHGGKRY------RIERrqgEFAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 82 ifdGTIKDNL--LMGL----RFSEKPFPNDDALQGALTTVSLDKKLE----------DNASSLSGGEKQRLAFARIILMd 145
Cdd:COG0419 100 ---SERKEALkrLLGLeiyeELKERLKELEEALESALEELAELQKLKqeilaqlsglDPIETLSGGERLRLALADLLSL- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487961256 146 ppvyLLDepTSALDGDTERRVMKQFTLLArekkktviFITH 186
Cdd:COG0419 176 ----ILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
54-186 |
4.89e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 54 IEYNGKSILDyppiqlrrevvmlgqtppIFDGTIKDnllmGLRFsekpFPNDDALQGALTT---VSLDK-KLEDNASSLS 129
Cdd:COG0178 775 VKYKGKNIAD------------------VLDMTVEE----ALEF----FENIPKIARKLQTlqdVGLGYiKLGQPATTLS 828
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487961256 130 GGEKQRLAFARiILMDPP----VYLLDEPTSALDGDTERRVMKQFTLLaREKKKTVIFITH 186
Cdd:COG0178 829 GGEAQRVKLAS-ELSKRStgktLYILDEPTTGLHFHDIRKLLEVLHRL-VDKGNTVVVIEH 887
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
103-210 |
5.49e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 37.64 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 103 PNDDALQGALTTVSLDKKLEDNASSLSGGEKQRLAFARI--ILM-DP-PVYLLDEPTSALDGDTERRVMKqftlLAREKK 178
Cdd:pfam02463 1053 PDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIfaIQKyKPaPFYLLDEIDAALDDQNVSRVAN----LLKELS 1128
|
90 100 110
....*....|....*....|....*....|....
gi 487961256 179 KT--VIFITHSQQLPEEiADDIIEISKTNGATRK 210
Cdd:pfam02463 1129 KNaqFIVISLREEMLEK-ADKLVGVTMVENGVST 1161
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
28-43 |
5.59e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.48 E-value: 5.59e-03
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
118-209 |
6.76e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.48 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487961256 118 DKKLEDNASSLSGGEK------QRLAFARIILMDPPVYL----LDEPTSALDGDTERRVMKQFTLLAREKKKtVIFITHS 187
Cdd:cd03279 114 DRFLARPVSTLSGGETflaslsLALALSEVLQNRGGARLealfIDEGFGTLDPEALEAVATALELIRTENRM-VGVISHV 192
|
90 100
....*....|....*....|..
gi 487961256 188 QQLPEEIaDDIIEISKTNGATR 209
Cdd:cd03279 193 EELKERI-PQRLEVIKTPGGSR 213
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
22-59 |
7.57e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 7.57e-03
10 20 30
....*....|....*....|....*....|....*....
gi 487961256 22 KEKTTCIIGESGSGKSTLL-RMLNDLQSPTSGTIEYNGK 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLnALLPELVLATGEISEKLGR 122
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
126-186 |
7.72e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 36.79 E-value: 7.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487961256 126 SSLSGGEKQRLAFARIILMDPPVYLLDEPTSALDGDTERRVmkQFTLLARekKKTVIFITH 186
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWL--EDVLNER--NSTMIIISH 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-186 |
9.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 36.96 E-value: 9.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487961256 119 KKLEdNASSLSGGEKQRLA----FArIILMDP-PVYLLDEPTSALD-GDTER--RVMKQFTllareKKKTVIFITH 186
Cdd:TIGR02168 1082 KKNQ-NLSLLSGGEKALTAlallFA-IFKVKPaPFCILDEVDAPLDdANVERfaNLLKEFS-----KNTQFIVITH 1150
|
|
| |
