|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-160 |
1.59e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.76 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLASPLK--MGYVPEi 72
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvaRDPAEVRrrIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIP-FTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:COG1131 81 EPALYPdLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170
....*....|..
gi 2182225815 152 G---QKRKVMWK 160
Cdd:COG1131 161 GldpEARRELWE 172
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-152 |
2.36e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 139.86 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL------KMGYVPeitps 75
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrRIGYLP----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 ripftlEE---YP--------IHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFL 144
Cdd:COG4152 78 ------EErglYPkmkvgeqlVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
....*...
gi 2182225815 145 ILDEPLSG 152
Cdd:COG4152 152 ILDEPFSG 159
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-152 |
7.58e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 7.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL-----KMGYVP---EIT 73
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPrrarrRIGYVPqraEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 PSrIPFTLEE------YPiHMGKIRGMDKQHlRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:COG1121 88 WD-FPITVRDvvlmgrYG-RRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
....*
gi 2182225815 148 EPLSG 152
Cdd:COG1121 165 EPFAG 169
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-152 |
1.65e-40 |
|
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: 136.14 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------KMGYVPEI 72
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-151 |
9.77e-39 |
|
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: 132.09 E-value: 9.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------------KLASplKMGY 68
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsrrELAR--RIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VPEITPSRIPFTLEE------YPiHMGKIRGMDKQHlRQRIDCLLEMFHLQ--ADRRtaIAELSKGMKQKVIIMQSLIEE 140
Cdd:COG1120 80 VPQEPPAPFGLTVRElvalgrYP-HLGLFGRPSAED-REAVEEALERTGLEhlADRP--VDELSGGERQRVLIARALAQE 155
|
170
....*....|.
gi 2182225815 141 TDFLILDEPLS 151
Cdd:COG1120 156 PPLLLLDEPTS 166
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-151 |
4.86e-38 |
|
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: 129.13 E-value: 4.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNK----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK-----MGYVPE 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 iTPSRIPF-TLEE---YPIhmgKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:cd03293 81 -QDALLPWlTVLDnvaLGL---ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
....
gi 2182225815 148 EPLS 151
Cdd:cd03293 157 EPFS 160
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-152 |
5.76e-38 |
|
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: 128.94 E-value: 5.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL------KMGYVPEITP 74
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdiaarnRIGYLPEERG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 75 SRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-152 |
1.23e-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: 125.34 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKM-----GYVPEIT--P 74
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkriGYVPQRRsiD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 75 SRIPFTLEE------YPiHMGKIRGMDKQHlRQRIDCLLE---MFHLqADRRtaIAELSKGMKQKVIIMQSLIEETDFLI 145
Cdd:cd03235 81 RDFPISVRDvvlmglYG-HKGLFRRLSKAD-KAKVDEALErvgLSEL-ADRQ--IGELSGGQQQRVLLARALVQDPDLLL 155
|
....*..
gi 2182225815 146 LDEPLSG 152
Cdd:cd03235 156 LDEPFAG 162
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-160 |
2.10e-36 |
|
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: 123.66 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---------KLASPLKMGYVPEi 72
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkePEEVKRRIGYLPE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIP-FTLEEYpihmgkirgmdkqhlrqridcllemfhlqadrrtaiAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03230 81 EPSLYEnLTVREN------------------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170
....*....|..
gi 2182225815 152 G---QKRKVMWK 160
Cdd:cd03230 125 GldpESRREFWE 136
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-151 |
4.77e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 4.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY----KLASP-LKMGYVP-E 71
Cdd:COG1116 9 ELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkPVTGPgPDRGVVFqE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 itpsripFTLeeYP-------IHMG-KIRGMDKQHLRQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVIIMQSLIEET 141
Cdd:COG1116 89 -------PAL--LPwltvldnVALGlELRGVPKAERRERARELLELVGLAgfEDAYP--HQLSGGMRQRVAIARALANDP 157
|
170
....*....|
gi 2182225815 142 DFLILDEPLS 151
Cdd:COG1116 158 EVLLMDEPFG 167
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-153 |
1.43e-33 |
|
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: 117.57 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYV 69
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 ---PE---ITPS---RIPFTLEeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEE 140
Cdd:cd03225 81 fqnPDdqfFGPTveeEVAFGLE--------NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170
....*....|...
gi 2182225815 141 TDFLILDEPLSGQ 153
Cdd:cd03225 153 PDILLLDEPTAGL 165
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-152 |
2.86e-32 |
|
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: 114.24 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV-------YKLASPLK-MGYV---P 70
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyQKNIEALRrIGALieaP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRipfTLEEYPIHMGKIRGMDKqhlrQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:cd03268 82 GFYPNL---TARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
..
gi 2182225815 151 SG 152
Cdd:cd03268 155 NG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-151 |
1.27e-31 |
|
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: 111.76 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVPe 71
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslspkelarKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 itpsripftleeypihmgkirgmdkQHLRqridcLLEMFHLqADRRtaIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03214 80 -------------------------QALE-----LLGLAHL-ADRP--FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-152 |
2.79e-31 |
|
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: 111.52 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIhKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-----KLASPLKM----GYVPEI 72
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdVLKQPQKLrrriGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-151 |
3.71e-31 |
|
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: 111.46 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYkLASPLKMGYVPEITPSRIPF- 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL-IDGRDVTGVPPERRNIGMVFq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 --TLeeYPiHM---------GKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:cd03259 80 dyAL--FP-HLtvaeniafgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
...
gi 2182225815 149 PLS 151
Cdd:cd03259 157 PLS 159
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-158 |
7.51e-31 |
|
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: 110.89 E-value: 7.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------------KLASplKMGY 68
Cdd:COG1122 2 ELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkknlrELRR--KVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 V---PE---ITPsripfTLEE----YPIHMgkirGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLI 138
Cdd:COG1122 80 VfqnPDdqlFAP-----TVEEdvafGPENL----GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180
....*....|....*....|....
gi 2182225815 139 EETDFLILDEPLSGQ----KRKVM 158
Cdd:COG1122 151 MEPEVLVLDEPTAGLdprgRRELL 174
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-151 |
3.17e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.11 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---KLASPLK-----MGYVPeit 73
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgRDVTGLPpekrnVGMVF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 psripftlEEYPI--HM--------G-KIRGMDKQHLRQRIDCLLEMFHLQ--ADRRtaIAELSKGMKQKVIIMQSLIEE 140
Cdd:COG3842 84 --------QDYALfpHLtvaenvafGlRMRGVPKAEIRARVAELLELVGLEglADRY--PHQLSGGQQQRVALARALAPE 153
|
170
....*....|.
gi 2182225815 141 TDFLILDEPLS 151
Cdd:COG3842 154 PRVLLLDEPLS 164
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-152 |
3.69e-30 |
|
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: 108.72 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK---------MGYV-- 69
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdaredyrrrLAYLgh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 -PEITPSripFTLEEYPIHMGKIRGMDKQhlRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:COG4133 83 aDGLKPE---LTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
....
gi 2182225815 149 PLSG 152
Cdd:COG4133 158 PFTA 161
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-153 |
6.98e-30 |
|
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: 113.46 E-value: 6.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK-----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---------------KLA 61
Cdd:COG1123 262 EVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltklsrrslrELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 62 SplKMGYV---------PEITPSRIpftLEEYPIHMGkirGMDKQHLRQRIDCLLEMFHLQADRRTA-IAELSKGMKQKV 131
Cdd:COG1123 342 R--RVQMVfqdpysslnPRMTVGDI---IAEPLRLHG---LLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRV 413
|
170 180
....*....|....*....|..
gi 2182225815 132 IIMQSLIEETDFLILDEPLSGQ 153
Cdd:COG1123 414 AIARALALEPKLLILDEPTSAL 435
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-149 |
3.79e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVP----EITPSR 76
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVKIGYFDqhqeELDPDK 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 77 ipfTLEEypiHMGKIR-GMDKQHLRQridcLLEMFHLQADR-RTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:COG0488 395 ---TVLD---ELRDGApGGTEQEVRG----YLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-151 |
7.59e-29 |
|
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: 103.50 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY----------KLASPLKMGYVPEiTPSRIPF-TLEEY 84
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltddeRKSLRKEIGYVFQ-DPQLFPRlTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2182225815 85 PIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAI----AELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-165 |
9.74e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.58 E-value: 9.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------KMGYVPE 71
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsrarharqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 ITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170
....*....|....*..
gi 2182225815 152 G---QKRKVMWKRFSCL 165
Cdd:PRK13537 168 GldpQARHLMWERLRSL 184
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-165 |
2.36e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------KMGYVPE 71
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpararlaraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 ITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170
....*....|....*..
gi 2182225815 152 G---QKRKVMWKRFSCL 165
Cdd:PRK13536 202 GldpHARHLIWERLRSL 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-149 |
2.49e-28 |
|
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: 104.11 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN----KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL------------- 64
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 -KMGYV-------PEITpsripfTLE--EYPIHmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIM 134
Cdd:cd03255 82 rHIGFVfqsfnllPDLT------ALEnvELPLL---LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170
....*....|....*
gi 2182225815 135 QSLIEETDFLILDEP 149
Cdd:cd03255 153 RALANDPKIILADEP 167
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-150 |
1.11e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 103.24 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------------KLA---SPLK 65
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvattpsrELAkrlAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 66 MgyVPEITpSRIpfTLEE------YPIHMGKIRGMDKQHLRQRIDCL-LEMFhlqADRRtaIAELSKGMKQKVIIMQSLI 138
Cdd:COG4604 82 Q--ENHIN-SRL--TVRElvafgrFPYSKGRLTAEDREIIDEAIAYLdLEDL---ADRY--LDELSGGQRQRAFIAMVLA 151
|
170
....*....|..
gi 2182225815 139 EETDFLILDEPL 150
Cdd:COG4604 152 QDTDYVLLDEPL 163
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-149 |
1.25e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYkLASPLKMGYVPEITPSRIPFTLE 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-IPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 83 EYpIHMGKIRGMDKQHLRQRI--------DCLLEMFHLQ----------ADRRTA----------------IAELSKGMK 128
Cdd:COG0488 80 DT-VLDGDAELRALEAELEELeaklaepdEDLERLAELQeefealggweAEARAEeilsglgfpeedldrpVSELSGGWR 158
|
170 180
....*....|....*....|.
gi 2182225815 129 QKVIIMQSLIEETDFLILDEP 149
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEP 179
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-152 |
1.27e-27 |
|
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: 102.58 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKL----VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-----------KLASPL-- 64
Cdd:cd03257 3 EVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrRLRKIRrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 KMGYVPE-----ITPS-RIPFTLEEyPIhmgKIRGMDKQHLRQRIDCLLEMFHLQADRRTA---IAELSKGMKQKVIIMQ 135
Cdd:cd03257 83 EIQMVFQdpmssLNPRmTIGEQIAE-PL---RIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIAR 158
|
170
....*....|....*..
gi 2182225815 136 SLIEETDFLILDEPLSG 152
Cdd:cd03257 159 ALALNPKLLIADEPTSA 175
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-149 |
1.31e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASP---LKMG----- 67
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvRIRSPrdaIALGigmvh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 ----YVPeitpsriPFTLEEyPIHMG----KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIE 139
Cdd:COG3845 87 qhfmLVP-------NLTVAE-NIVLGleptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170
....*....|
gi 2182225815 140 ETDFLILDEP 149
Cdd:COG3845 159 GARILILDEP 168
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-153 |
1.64e-27 |
|
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: 102.58 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------------KLASPLKMGY 68
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VpeitpsripF---------TLEE---YPIHMGkiRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQS 136
Cdd:cd03261 82 L---------FqsgalfdslTVFEnvaFPLREH--TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170
....*....|....*..
gi 2182225815 137 LIEETDFLILDEPLSGQ 153
Cdd:cd03261 151 LALDPELLLYDEPTAGL 167
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-149 |
1.85e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.04 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKL----VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------------KLASpL 64
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserELAR-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 ---KMGYV-------PEITpsripfTLE--EYPIHmgkIRGMDKQHLRQRIDCLLEMFHLqADRRTA-IAELSKGMKQKV 131
Cdd:COG1136 84 rrrHIGFVfqffnllPELT------ALEnvALPLL---LAGVSRKERRERARELLERVGL-GDRLDHrPSQLSGGQQQRV 153
|
170
....*....|....*...
gi 2182225815 132 IIMQSLIEETDFLILDEP 149
Cdd:COG1136 154 AIARALVNRPKLILADEP 171
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-152 |
3.16e-27 |
|
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: 101.85 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------------YKLASpLKMGYV 69
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmHKRAR-LGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
...
gi 2182225815 150 LSG 152
Cdd:cd03218 161 FAG 163
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-160 |
5.07e-27 |
|
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: 101.04 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---------KLASPLKMGYV 69
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PE--ITPSRipFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:cd03263 81 PQfdALFDE--LTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170
....*....|....*.
gi 2182225815 148 EPLSG---QKRKVMWK 160
Cdd:cd03263 159 EPTSGldpASRRAIWD 174
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-151 |
7.76e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.30 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSG------EVYKLASPL---KMGYVPei 72
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlngRDLFTNLPPrerRVGFVF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 tpsripftlEEY---PiHM--------G-KIRGMDKQHLRQRIDCLLEMFHLQ--ADRRtaIAELSKGMKQKVIIMQSLI 138
Cdd:COG1118 82 ---------QHYalfP-HMtvaeniafGlRVRPPSKAEIRARVEELLELVQLEglADRY--PSQLSGGQRQRVALARALA 149
|
170
....*....|...
gi 2182225815 139 EETDFLILDEPLS 151
Cdd:COG1118 150 VEPEVLLLDEPFG 162
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-152 |
2.18e-26 |
|
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: 97.70 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkmgyvpeitpsripftl 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2182225815 82 eeypIHMGKIRGMDKQHLRQRIdcllemfhlqadrrTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd00267 58 ----IDGKDIAKLPLEELRRRI--------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-149 |
3.08e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------YKLASP---LKMG----- 67
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlldgepVRFRSPrdaQAAGiaiih 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 ----YVPEitpsripFTLEE------YPIHMGKIrgmDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSL 137
Cdd:COG1129 86 qelnLVPN-------LSVAEniflgrEPRRGGLI---DWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170
....*....|..
gi 2182225815 138 IEETDFLILDEP 149
Cdd:COG1129 156 SRDARVLILDEP 167
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-153 |
3.43e-26 |
|
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: 99.28 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------------KLASPLKMGY 68
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditglsekeLYELRRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VpeitpsripF---------TLEE---YPIHMGkiRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQS 136
Cdd:COG1127 87 L---------FqggalfdslTVFEnvaFPLREH--TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170
....*....|....*..
gi 2182225815 137 LIEETDFLILDEPLSGQ 153
Cdd:COG1127 156 LALDPEILLYDEPTAGL 172
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-151 |
5.26e-26 |
|
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: 98.46 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPlkmgyVPEITPSRIPFTL 81
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-----ITNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 82 --EEYPI--HMG---------KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:cd03300 77 vfQNYALfpHLTvfeniafglRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
...
gi 2182225815 149 PLS 151
Cdd:cd03300 157 PLG 159
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-157 |
7.44e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.58 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVPE 71
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 iTPSRIPFTLEEypiHMGKIRGMDKQHL-RQRIDCLLEMFHLQAD-RRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:COG4619 82 -EPALWGGTVRD---NLPFPFQLRERKFdRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170
....*....|..
gi 2182225815 150 LSG----QKRKV 157
Cdd:COG4619 158 TSAldpeNTRRV 169
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-149 |
8.69e-26 |
|
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: 96.34 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkmgyvpeitpsripftL 81
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL----------------------V 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 82 EEYPIHMGKIRGMdkqhLRQRIdcllEMFHlqadrrtaiaELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:cd03216 60 DGKEVSFASPRDA----RRAGI----AMVY----------QLSVGERQMVEIARALARNARLLILDEP 109
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-152 |
1.06e-25 |
|
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: 97.50 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLASP----LKMGYVP 70
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditGLPPHerarAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 E---ITPSripFTLEEyPIHMGKIRGmDKQHLRQRIDCLLEMFHLQADRRTAIA-ELSKGMKQKVIIMQSLIEETDFLIL 146
Cdd:cd03224 82 EgrrIFPE---LTVEE-NLLLGAYAR-RRAKRKARLERVYELFPRLKERRKQLAgTLSGGEQQMLAIARALMSRPKLLLL 156
|
....*.
gi 2182225815 147 DEPLSG 152
Cdd:cd03224 157 DEPSEG 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-151 |
2.57e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.99 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLAsPLK--MGYVPEi 72
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdvtDLP-PKDrnIAMVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 tpSripFTLeeYPiHM--------G-KIRGMDKQHLRQRIDCLLEMFHLQA--DRRtaIAELSKGMKQKVIIMQSLIEET 141
Cdd:COG3839 83 --S---YAL--YP-HMtvyeniafPlKLRKVPKAEIDRRVREAAELLGLEDllDRK--PKQLSGGQRQRVALGRALVREP 152
|
170
....*....|
gi 2182225815 142 DFLILDEPLS 151
Cdd:COG3839 153 KVFLLDEPLS 162
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-152 |
2.66e-25 |
|
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: 96.28 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNK----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---------KLASPLKMG 67
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkePAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 YVPEITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCL---LEMFHLqADRRTaiAELSKGMKQKVIIMQSLIEETDFL 144
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELadrLGMEEL-LDRRV--GGFSTGMRQKVAIARALVHDPPVL 158
|
....*...
gi 2182225815 145 ILDEPLSG 152
Cdd:cd03266 159 LLDEPTTG 166
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-149 |
3.29e-25 |
|
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: 94.05 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVPeitpsripftl 81
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVKIGYFE----------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 82 eeypihmgkirgmdkqhlrqridcllemfhlqadrrtaiaELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:cd03221 70 ----------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-152 |
3.38e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 10 YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKlASPLKMGYVPEIT--PSRIPFTLEEYpIH 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-AGGARVAYVPQRSevPDSLPLTVRDL-VA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 88 MGKI--RGMDKQHL---RQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:NF040873 80 MGRWarRGLWRRLTrddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-152 |
7.67e-25 |
|
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: 96.03 E-value: 7.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKL----VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMG 67
Cdd:COG1124 3 EVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrrkafrrRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 YV---------PEITPSRIpftLEEyPIhmgKIRGMDKQhlRQRIDCLLEMFHLQA---DRRtaIAELSKGMKQKVIIMQ 135
Cdd:COG1124 83 MVfqdpyaslhPRHTVDRI---LAE-PL---RIHGLPDR--EERIAELLEQVGLPPsflDRY--PHQLSGGQRQRVAIAR 151
|
170
....*....|....*..
gi 2182225815 136 SLIEETDFLILDEPLSG 152
Cdd:COG1124 152 ALILEPELLLLDEPTSA 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-152 |
7.80e-25 |
|
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: 93.99 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkMGYVPeitpsrip 78
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-------IDGVD-------- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 79 ftleeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADrrtAIAE--LSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03228 66 ------------LRDLDLESLRKNIAYVPQDPFLFSG---TIREniLSGGQRQRIAIARALLRDPPILILDEATSA 126
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-152 |
2.08e-24 |
|
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: 94.43 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------------YKLAsplKMGYV 69
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglppHEIA---RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 -----PEITPSripFTLEE-----------YPIHMGKIRGMDKQHlRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVII 133
Cdd:cd03219 79 rtfqiPRLFPE---LTVLEnvmvaaqartgSGLLLARARREEREA-RERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170
....*....|....*....
gi 2182225815 134 MQSLIEETDFLILDEPLSG 152
Cdd:cd03219 155 ARALATDPKLLLLDEPAAG 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-152 |
3.18e-24 |
|
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: 92.64 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkmgyvpeitpsripft 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL---------------------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 81 leeypIHMGKIRGMDKQH--LRQRIDCLLE----MFHLQADRRTAIAeLSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03229 59 -----IDGEDLTDLEDELppLRRRIGMVFQdfalFPHLTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-158 |
3.48e-24 |
|
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: 93.09 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK-------MGYVPEiT 73
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksIGYVMQ-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 PSRIPFT---LEEYpihmgkIRGMDKQHLR-QRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:cd03226 80 VDYQLFTdsvREEL------LLGLKELDAGnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
....*....
gi 2182225815 150 LSGQKRKVM 158
Cdd:cd03226 154 TSGLDYKNM 162
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-152 |
4.92e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.56 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------------YKLASpLKMGYV 69
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfldgedithlpmHKRAR-LGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEiTPS--R-------IPFTLEeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEE 140
Cdd:COG1137 84 PQ-EASifRkltvednILAVLE--------LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170
....*....|..
gi 2182225815 141 TDFLILDEPLSG 152
Cdd:COG1137 155 PKFILLDEPFAG 166
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-151 |
2.64e-23 |
|
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: 94.97 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPD---SGEVYKLASPL----------KM 66
Cdd:COG1123 6 EVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelsealrgrRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 67 GYVPE-----ITPSRIPFTLEEYPihmgKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEET 141
Cdd:COG1123 86 GMVFQdpmtqLNPVTVGDQIAEAL----ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170
....*....|
gi 2182225815 142 DFLILDEPLS 151
Cdd:COG1123 162 DLLIADEPTT 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-151 |
3.58e-23 |
|
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: 91.09 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIK-----PDSGEVY------------KLASP 63
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLldgkdiydldvdVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 64 LKMGYVPEiTPSRIPFTLEEyPIHMG-KIRGM-DKQHLRQRIDCLLEMFHL--QADRRTAIAELSKGMKQKVIIMQSLIE 139
Cdd:cd03260 81 RRVGMVFQ-KPNPFPGSIYD-NVAYGlRLHGIkLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170
....*....|..
gi 2182225815 140 ETDFLILDEPLS 151
Cdd:cd03260 159 EPEVLLLDEPTS 170
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-161 |
4.16e-23 |
|
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: 90.89 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGE-------VYKLASPLK--MGYVP- 70
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREVRrrIGIVFq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRIPFTLEEYPIHmGKIRGMDKQHLRQRIDCLLEMFHL--QADRRtaIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:cd03265 81 DLSVDDELTGWENLYIH-ARLYGVPGAERRERIDELLDFVGLleAADRL--VKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170
....*....|....*.
gi 2182225815 149 PLSG---QKRKVMWKR 161
Cdd:cd03265 158 PTIGldpQTRAHVWEY 173
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1-152 |
8.93e-23 |
|
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: 90.15 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL------KMGYVPEITP 74
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrkdlhKIGSLIESPP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 75 SRIPFTLEEYPIHMGKIRGMDKQhlrqRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-149 |
1.05e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.73 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN-KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLasplkmGY-VPEITPSRIPF 79
Cdd:COG2884 3 RFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN------GQdLSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 ------------------TLEE---YPIhmgKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLI 138
Cdd:COG2884 77 lrrrigvvfqdfrllpdrTVYEnvaLPL---RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170
....*....|.
gi 2182225815 139 EETDFLILDEP 149
Cdd:COG2884 154 NRPELLLADEP 164
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-151 |
1.35e-22 |
|
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: 89.24 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklaspLKMGYVPEITPSR--IP 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY-----IGGRDVTDLPPKDrdIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 FTLEEYPI--HMG---------KIRGMDKQHLRQRIDCLLEMFHLQA--DRRTaiAELSKGMKQKVIIMQSLIEETDFLI 145
Cdd:cd03301 76 MVFQNYALypHMTvydniafglKLRKVPKDEIDERVREVAELLQIEHllDRKP--KQLSGGQRQRVALGRAIVREPKVFL 153
|
....*.
gi 2182225815 146 LDEPLS 151
Cdd:cd03301 154 MDEPLS 159
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-165 |
3.44e-22 |
|
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: 88.36 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYR----------------------NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 59 ---KLASPLKM--GYVPEitpsripFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVII 133
Cdd:cd03220 81 vrgRVSSLLGLggGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAF 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2182225815 134 MQSLIEETDFLILDEPLSG-----QKRkvMWKRFSCL 165
Cdd:cd03220 154 AIATALEPDILLIDEVLAVgdaafQEK--CQRRLREL 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-151 |
3.81e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.60 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---KLASPLKM--GYVPEitpsri 77
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngRVSALLELgaGFHPE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 78 pFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEmFhlqadrrtaiAEL-----------SKGMKQKV---IIMQSlieETDF 143
Cdd:COG1134 103 -LTGRENIYLNGRLLGLSRKEIDEKFDEIVE-F----------AELgdfidqpvktySSGMRARLafaVATAV---DPDI 167
|
....*...
gi 2182225815 144 LILDEPLS 151
Cdd:COG1134 168 LLVDEVLA 175
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-152 |
1.81e-21 |
|
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: 87.06 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLasplkMGY------VPEITPs 75
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRL-----FGErrggedVWELRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 RI----PFTLEEYPIHMgKIRGM----------------DKQhlRQRIDCLLEMFHLQ--ADRRtaIAELSKGMKQKVII 133
Cdd:COG1119 79 RIglvsPALQLRFPRDE-TVLDVvlsgffdsiglyreptDEQ--RERARELLELLGLAhlADRP--FGTLSQGEQRRVLI 153
|
170
....*....|....*....
gi 2182225815 134 MQSLIEETDFLILDEPLSG 152
Cdd:COG1119 154 ARALVKDPELLILDEPTAG 172
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-151 |
2.77e-21 |
|
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: 86.10 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASPL------- 64
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdlTLLSGKelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 KMGYVPE---ITPSRIPFTLEEYPIhmgKIRGMDKQHLRQRIDCLLEMFHLqADRRTA-IAELSKGMKQKVIIMQSLIEE 140
Cdd:cd03258 83 RIGMIFQhfnLLSSRTVFENVALPL---EIAGVPKAEIEERVLELLELVGL-EDKADAyPAQLSGGQKQRVGIARALANN 158
|
170
....*....|.
gi 2182225815 141 TDFLILDEPLS 151
Cdd:cd03258 159 PKVLLCDEATS 169
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-156 |
2.77e-21 |
|
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: 86.62 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---KLASPLK-----MGYV--- 69
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggEDATDVPvqernVGFVfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 ----PEITPS-RIPFTLEEYPihmgKIRGMDKQHLRQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVIIMQSLIEETD 142
Cdd:cd03296 83 yalfRHMTVFdNVAFGLRVKP----RSERPPEAEIRAKVHELLKLVQLDwlADRYP--AQLSGGQRQRVALARALAVEPK 156
|
170
....*....|....*..
gi 2182225815 143 FLILDEP---LSGQKRK 156
Cdd:cd03296 157 VLLLDEPfgaLDAKVRK 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-151 |
4.76e-21 |
|
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: 86.33 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY----KLASP-------LKMGY 68
Cdd:TIGR04520 2 EVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdglDTLDEenlweirKKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 V---PE------ITPSRIPFTLEEypihmgkiRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIE 139
Cdd:TIGR04520 82 VfqnPDnqfvgaTVEDDVAFGLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170
....*....|..
gi 2182225815 140 ETDFLILDEPLS 151
Cdd:TIGR04520 154 RPDIIILDEATS 165
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-151 |
1.07e-20 |
|
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: 85.04 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN-KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVP 70
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQ----ADRRTaiAELSKGMKQKVIIMQSLIEETDFLIL 146
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaefADRYP--HELSGGQQQRVGVARALAADPPLLLM 159
|
....*
gi 2182225815 147 DEPLS 151
Cdd:cd03295 160 DEPFG 164
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-161 |
1.24e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.68 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSG-------EVYKL-ASPLKMGYVPE- 71
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgtDVSRLhARDRKVGFVFQh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 ------ITPS-RIPFTLEEYPIHmgkiRGMDKQHLRQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVIIMQSLIEETD 142
Cdd:PRK10851 83 yalfrhMTVFdNIAFGLTVLPRR----ERPNAAAIKAKVTQLLEMVQLAhlADRYP--AQLSGGQKQRVALARALAVEPQ 156
|
170 180
....*....|....*....|....
gi 2182225815 143 FLILDEP---LSGQKRKVM--WKR 161
Cdd:PRK10851 157 ILLLDEPfgaLDAQVRKELrrWLR 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-152 |
1.46e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 6 ITKYYRN-KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK-------MGYVP--EITPS 75
Cdd:PRK15056 12 VTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqknlVAYVPqsEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 RIPFTLEEYPI-----HMGKIRgMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK15056 92 SFPVLVEDVVMmgrygHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
..
gi 2182225815 151 SG 152
Cdd:PRK15056 171 TG 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-152 |
1.65e-20 |
|
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: 84.31 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 10 YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplKMGYVPEitpSRIPFTLEEYPIHMG 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR------VAGLVPW---KRRKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 90 K-------------------IRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:cd03267 102 QktqlwwdlpvidsfyllaaIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
..
gi 2182225815 151 SG 152
Cdd:cd03267 182 IG 183
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-149 |
1.71e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELR--NITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKM----------GY 68
Cdd:PRK11231 1 MTLRteNLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrqlarrlAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VPEI--TPSRIpfTLEE--------YPIHMGKIRGMDKQHLRQRIDcLLEMFHLqADRRtaIAELSKGMKQKVIIMQSLI 138
Cdd:PRK11231 81 LPQHhlTPEGI--TVRElvaygrspWLSLWGRLSAEDNARVNQAME-QTRINHL-ADRR--LTDLSGGQRQRAFLAMVLA 154
|
170
....*....|.
gi 2182225815 139 EETDFLILDEP 149
Cdd:PRK11231 155 QDTPVVLLDEP 165
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-152 |
4.79e-20 |
|
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: 85.66 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkmgyvpeitpsripf 79
Cdd:COG2274 475 ELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL--------------------- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 tLEEYPihmgkIRGMDKQHLRQRI-----------DCLLE---MFHLQAD--------RRTAIAE--------------- 122
Cdd:COG2274 534 -IDGID-----LRQIDPASLRRQIgvvlqdvflfsGTIREnitLGDPDATdeeiieaaRLAGLHDfiealpmgydtvvge 607
|
170 180 190
....*....|....*....|....*....|....
gi 2182225815 123 ----LSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:COG2274 608 ggsnLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-157 |
5.19e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.89 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVykLASPLKMGYVPeitPSRIPFT 80
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI--MLDGVDLSHVP---PYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 L--EEYPI--HMG---------KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:PRK11607 95 MmfQSYALfpHMTveqniafglKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170
....*....|
gi 2182225815 148 EPLSGQKRKV 157
Cdd:PRK11607 175 EPMGALDKKL 184
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-151 |
4.34e-19 |
|
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: 80.69 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN-KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEITPSR--IP 78
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 FTLEEYPI----------------HMGKIRGM----DKQHLRQRIDCL-----LEMFHLQADrrtaiaELSKGMKQKVII 133
Cdd:cd03256 82 MIFQQFNLierlsvlenvlsgrlgRRSTWRSLfglfPKEEKQRALAALervglLDKAYQRAD------QLSGGQQQRVAI 155
|
170
....*....|....*...
gi 2182225815 134 MQSLIEETDFLILDEPLS 151
Cdd:cd03256 156 ARALMQQPKLILADEPVA 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-152 |
4.77e-19 |
|
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: 80.03 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 18 NVSFSIhKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEITPS---RIPFTLEEYPI--HMG--- 89
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrKIGLVFQQYALfpHLNvre 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2182225815 90 ----KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03297 95 nlafGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-151 |
6.02e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------YKLASPLK---MG-Y-V 69
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpCARLTPAKahqLGiYlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PE---ITPS-----RIPFTLeeyPIHMGKIRGMdkQHLRQRIDCllemfHLQADRRTAIAELSKgmKQKVIIMQSLIEET 141
Cdd:PRK15439 92 PQeplLFPNlsvkeNILFGL---PKRQASMQKM--KQLLAALGC-----QLDLDSSAGSLEVAD--RQIVEILRGLMRDS 159
|
170
....*....|
gi 2182225815 142 DFLILDEPLS 151
Cdd:PRK15439 160 RILILDEPTA 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-151 |
1.78e-18 |
|
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: 78.34 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY----KLASPL--------KMGYV 69
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglKLTDDKkninelrqKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 -------PEITpsripfTLE---EYPIhmgKIRGMDKQHLRQRIDCLLEMFHLqADRRTA-IAELSKGMKQKVIIMQSLI 138
Cdd:cd03262 82 fqqfnlfPHLT------VLEnitLAPI---KVKGMSKAEAEERALELLEKVGL-ADKADAyPAQLSGGQQQRVAIARALA 151
|
170
....*....|...
gi 2182225815 139 EETDFLILDEPLS 151
Cdd:cd03262 152 MNPKVMLFDEPTS 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-152 |
2.93e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYR-NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEI------- 72
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrkfvglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 ---TPSRIPFTLEEYPIHMGKIR-GMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:PRK13652 84 fqnPDDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
....
gi 2182225815 149 PLSG 152
Cdd:PRK13652 164 PTAG 167
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-151 |
5.98e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMG------------- 67
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsttaalaagvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 -----YVPEITPSRIPFtLEEYPIHMGKIrgmDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETD 142
Cdd:PRK11288 85 yqelhLVPEMTVAENLY-LGQLPHKGGIV---NRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
....*....
gi 2182225815 143 FLILDEPLS 151
Cdd:PRK11288 161 VIAFDEPTS 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-151 |
3.36e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.07 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASplkmgyvpEITPSRIP-- 78
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--------DVTHRSIQqr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 ---FTLEEYPI--HMG---------KIRGMDKQHLRQRIDCLLEMFHLQ--ADRrtAIAELSKGMKQKVIIMQSLIEETD 142
Cdd:PRK11432 79 dicMVFQSYALfpHMSlgenvgyglKMLGVPKEERKQRVKEALELVDLAgfEDR--YVDQISGGQQQRVALARALILKPK 156
|
....*....
gi 2182225815 143 FLILDEPLS 151
Cdd:PRK11432 157 VLLFDEPLS 165
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-151 |
3.58e-17 |
|
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: 76.14 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 18 NVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL--------------KMGYVPE---ITPSR---- 76
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrkelrelrrkKISMVFQsfaLLPHRtvle 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 77 -IPFTLEeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03294 122 nVAFGLE--------VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-158 |
4.00e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYkLASPLKMGYVPEITPSRIPFtl 81
Cdd:PRK09452 16 ELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-LDGQDITHVPAENRHVNTVF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 82 EEYPI--HMG---------KIRGMDKQHLRQRIDCLLEMFHLQ--ADRRtaIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:PRK09452 93 QSYALfpHMTvfenvafglRMQKTPAAEITPRVMEALRMVQLEefAQRK--PHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170
....*....|...
gi 2182225815 149 PLSG---QKRKVM 158
Cdd:PRK09452 171 SLSAldyKLRKQM 183
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-152 |
5.81e-17 |
|
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: 76.72 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV---------YKLASPLK-MGYVP 70
Cdd:COG4988 338 ELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASWRRqIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EiTPSRIPFTLEEYpIHMGKiRGMDKQHLRQ-----RIDCLLEMfhLQADRRTAIAE----LSKGMKQKVIIMQSLIEET 141
Cdd:COG4988 418 Q-NPYLFAGTIREN-LRLGR-PDASDEELEAaleaaGLDEFVAA--LPDGLDTPLGEggrgLSGGQAQRLALARALLRDA 492
|
170
....*....|.
gi 2182225815 142 DFLILDEPLSG 152
Cdd:COG4988 493 PLLLLDEPTAH 503
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-151 |
6.52e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklASPLKMGYVPeitPSR--IPFT 80
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF--IGEKRMNDVP---PAErgVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 LEEYPI--HMG---------KIRGMDKQHLRQRIDCLLEMFHLQA--DRRTaiAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:PRK11000 81 FQSYALypHLSvaenmsfglKLAGAKKEEINQRVNQVAEVLQLAHllDRKP--KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
....
gi 2182225815 148 EPLS 151
Cdd:PRK11000 159 EPLS 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-151 |
8.25e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.81 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------------YKLASPLKMgyV 69
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwspAELARRRAV--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEITPSRIPFTLEEYpIHMGKI-RGMDKQHLRQ-------RIDCLlemfHLqADRRtaIAELSKGMKQKV----IIMQ-- 135
Cdd:PRK13548 82 PQHSSLSFPFTVEEV-VAMGRApHGLSRAEDDAlvaaalaQVDLA----HL-AGRD--YPQLSGGEQQRVqlarVLAQlw 153
|
170
....*....|....*.
gi 2182225815 136 SLIEETDFLILDEPLS 151
Cdd:PRK13548 154 EPDGPPRWLLLDEPTS 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-152 |
1.44e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVPE---ITPSrIPF 79
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLRIGYVPQklyLDTT-LPL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 80 TLEeypihmgkiRGMDKQHLRQRIDCLLEMFHLQADR--RTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK09544 85 TVN---------RFLRLRPGTKKEDILPALKRVQAGHliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-149 |
1.70e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 10 YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLasplkmGYVPeiTPSRIPF---------- 79
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL------GYVP--FKRRKEFarrigvvfgq 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 80 ---------TLEEYPIHmGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:COG4586 104 rsqlwwdlpAIDSFRLL-KAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-152 |
2.59e-16 |
|
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: 73.01 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK----------MGYV 69
Cdd:cd03245 4 EFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqldpadlrrnIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEiTPSRIPFTLEEyPIHMGKIRGMDKQHLRQ-RIDCLLEMFHLQA---DRRtaIAE----LSKGMKQKVIIMQSLIEET 141
Cdd:cd03245 84 PQ-DVTLFYGTLRD-NITLGAPLADDERILRAaELAGVTDFVNKHPnglDLQ--IGErgrgLSGGQRQAVALARALLNDP 159
|
170
....*....|.
gi 2182225815 142 DFLILDEPLSG 152
Cdd:cd03245 160 PILLLDEPTSA 170
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-152 |
2.62e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.34 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLASP------L 64
Cdd:COG1135 3 ELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltALSERelraarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 KMGYVPE---ITPSRipfTLEE---YPIhmgKIRGMDKQHLRQRIDCLLEMFHLqADRRTA-IAELSKGMKQKVIIMQSL 137
Cdd:COG1135 83 KIGMIFQhfnLLSSR---TVAEnvaLPL---EIAGVPKAEIRKRVAELLELVGL-SDKADAyPSQLSGGQKQRVGIARAL 155
|
170
....*....|....*
gi 2182225815 138 IEETDFLILDEPLSG 152
Cdd:COG1135 156 ANNPKVLLCDEATSA 170
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-149 |
3.07e-16 |
|
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: 73.93 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYY--RNKLV--LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKP---DSGEVY----KLASpLKMGYVP 70
Cdd:COG0444 3 EVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgeDLLK-LSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRI------PFT-----------LEE-YPIHmgkiRGMDKQHLRQRIDCLLEMFHLQADRRTAIA---ELSKGMKQ 129
Cdd:COG0444 82 KIRGREIqmifqdPMTslnpvmtvgdqIAEpLRIH----GGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQ 157
|
170 180
....*....|....*....|
gi 2182225815 130 KVIIMQSLIEETDFLILDEP 149
Cdd:COG0444 158 RVMIARALALEPKLLIADEP 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-151 |
3.11e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEI------ 72
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVrrqvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 ---TPSR----------IPFTLEEypihmgkiRGMDKQHLRQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVIIMQSL 137
Cdd:PRK13635 86 vfqNPDNqfvgatvqddVAFGLEN--------IGVPREEMVERVDQALRQVGMEdfLNREP--HRLSGGQKQRVAIAGVL 155
|
170
....*....|....
gi 2182225815 138 IEETDFLILDEPLS 151
Cdd:PRK13635 156 ALQPDIIILDEATS 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-151 |
4.68e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV-----------YKLASPLKMGYV 69
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEITPSRIPFTLEEyPIHMGK--------IRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEET 141
Cdd:PRK09700 86 YQELSVIDELTVLE-NLYIGRhltkkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170
....*....|
gi 2182225815 142 DFLILDEPLS 151
Cdd:PRK09700 165 KVIIMDEPTS 174
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-149 |
5.43e-16 |
|
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: 72.06 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLV-LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV----------YKLASPL---KM 66
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlRGRAIPYlrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 67 GYVPE---ITPSR-----IPFTLEeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLI 138
Cdd:cd03292 81 GVVFQdfrLLPDRnvyenVAFALE--------VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170
....*....|.
gi 2182225815 139 EETDFLILDEP 149
Cdd:cd03292 153 NSPTILIADEP 163
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-151 |
9.52e-16 |
|
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: 71.60 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNkLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASPLK--MGYVPE- 71
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkdiTNLPPEKrdISYVPQn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 --ITPSRIPFTLEEYPIhmgKIRGMDKQHLRQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:cd03299 80 yaLFPHMTVYKNIAYGL---KKRKVDKKEIERKVLEIAEMLGIDhlLNRKP--ETLSGGEQQRVAIARALVVNPKILLLD 154
|
....
gi 2182225815 148 EPLS 151
Cdd:cd03299 155 EPFS 158
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-152 |
1.09e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKL----ASPlkmGYVPEITPsRI 77
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLggdmADA---RHRRAVCP-RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 78 PF-----------TL--EEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQ--ADRrtAIAELSKGMKQKVIIMQSLIEETD 142
Cdd:NF033858 79 AYmpqglgknlypTLsvFENLDFFGRLFGQDAAERRRRIDELLRATGLApfADR--PAGKLSGGMKQKLGLCCALIHDPD 156
|
170
....*....|
gi 2182225815 143 FLILDEPLSG 152
Cdd:NF033858 157 LLILDEPTTG 166
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-151 |
1.10e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKL-VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkmgyvpeITPSRIPfT 80
Cdd:PRK11650 5 KLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW-------------IGGRVVN-E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 LEE--------------YPiHMG---------KIRGMDKQHLRQRIDCLLEMFHLQA--DRRTaiAELSKGMKQKVIIMQ 135
Cdd:PRK11650 71 LEPadrdiamvfqnyalYP-HMSvrenmayglKIRGMPKAEIEERVAEAARILELEPllDRKP--RELSGGQRQRVAMGR 147
|
170
....*....|....*.
gi 2182225815 136 SLIEETDFLILDEPLS 151
Cdd:PRK11650 148 AIVREPAVFLFDEPLS 163
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-149 |
1.18e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 8 KYYRNKL---VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL--------------KMGYVP 70
Cdd:PRK11629 14 RYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaakaelrnqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRIPFTLEE---YPIHMGkirGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:PRK11629 94 QFHHLLPDFTALEnvaMPLLIG---KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
..
gi 2182225815 148 EP 149
Cdd:PRK11629 171 EP 172
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-149 |
1.30e-15 |
|
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: 71.34 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklaspLKMGYVPEITPSR---------IPFTLEEYPI 86
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI-----LEGKQITEPGPDRmvvfqnyslLPWLTVRENI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 87 HMG---KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:TIGR01184 76 ALAvdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-149 |
1.55e-15 |
|
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: 72.66 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVPE----ITPSR 76
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIGETVKLAYVDQsrdaLDPNK 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 77 IPFtlEEYP-----IHMGKIRGMDKQHLRQridcllemFHLQ-ADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:TIGR03719 402 TVW--EEISggldiIKLGKREIPSRAYVGR--------FNFKgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-149 |
1.60e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKyyrnKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASP-----LKMGYV 69
Cdd:COG1129 257 LEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvRIRSPrdairAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PE----------------ITPSRIPftleeypiHMGKIRGMDKQHLRQRIDCLLEMFHLQA-DRRTAIAELSKGMKQKVI 132
Cdd:COG1129 333 PEdrkgeglvldlsirenITLASLD--------RLSRGGLLDRRRERALAEEYIKRLRIKTpSPEQPVGNLSGGNQQKVV 404
|
170
....*....|....*..
gi 2182225815 133 IMQSLIEETDFLILDEP 149
Cdd:COG1129 405 LAKWLATDPKVLILDEP 421
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-149 |
1.78e-15 |
|
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: 69.77 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITkyyrNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------YKLASP-----LKMGYV 69
Cdd:cd03215 5 LEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEItldgkpVTRRSPrdairAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEitpsripftleeypihmgkirgmDkqhlRQRIDCLLEMfhlqadrrtAIAE-------LSKGMKQKVIIMQSLIEETD 142
Cdd:cd03215 81 PE-----------------------D----RKREGLVLDL---------SVAEnialsslLSGGNQQKVVLARWLARDPR 124
|
....*..
gi 2182225815 143 FLILDEP 149
Cdd:cd03215 125 VLILDEP 131
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-150 |
1.94e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLkmGYVPEITpsRIPFtlE 82
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL--AEAREDT--RLMF--Q 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 83 EYPIHMGKiRGMD------KQHLRQRIDCLLEMFHLqADRRTAI-AELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK11247 89 DARLLPWK-KVIDnvglglKGQWRDAALQALAAVGL-ADRANEWpAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-151 |
3.96e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.53 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNIT-KYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMG 67
Cdd:PRK13650 5 IEVKNLTfKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 ---------YVPEITPSRIPFTLEEypihmgkiRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLI 138
Cdd:PRK13650 85 mvfqnpdnqFVGATVEDDVAFGLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170
....*....|...
gi 2182225815 139 EETDFLILDEPLS 151
Cdd:PRK13650 157 MRPKIIILDEATS 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-149 |
4.69e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVPEITPSRIPFTLEE- 83
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraasrRVASVPQDTSLSFEFDVRQv 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 84 -----YPiHMGKIRGM---DKQHLRQRIDCL-LEMFhlqADRrtAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK09536 98 vemgrTP-HRSRFDTWtetDRAAVERAMERTgVAQF---ADR--PVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-69 |
6.47e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 6.47e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYV 69
Cdd:PRK11819 326 EAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-KIGETVKLAYV 392
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-151 |
6.95e-15 |
|
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: 69.04 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK---LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMgYVPEITPSRIP 78
Cdd:cd03248 13 KFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ-YEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 FTLEEYPIHMGKIR-----GM------------DKQHLRQRIDCLLEMFHLQADRRTaiAELSKGMKQKVIIMQSLIEET 141
Cdd:cd03248 92 LVGQEPVLFARSLQdniayGLqscsfecvkeaaQKAHAHSFISELASGYDTEVGEKG--SQLSGGQKQRVAIARALIRNP 169
|
170
....*....|
gi 2182225815 142 DFLILDEPLS 151
Cdd:cd03248 170 QVLILDEATS 179
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-70 |
9.94e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.58 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV---------YKLASpL--KMGYV 69
Cdd:COG1132 341 EFENVSfSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTLES-LrrQIGVV 419
|
.
gi 2182225815 70 P 70
Cdd:COG1132 420 P 420
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-152 |
1.62e-14 |
|
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: 67.34 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyklasplkmgyvpeitpsrip 78
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--------------------- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 79 fTLEEYPIHMGkirgmdKQHLRQRIDCLLEMFHLQAD--RRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03247 60 -TLDGVPVSDL------EKALSSLISVLNQRPYLFDTtlRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-152 |
3.74e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 5 NITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLAS-----PLK------MGYVPEit 73
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHararrgIGYLPQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 PSRIPFTLEEYPIHMG--KIR-GMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK10895 86 EASIFRRLSVYDNLMAvlQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
..
gi 2182225815 151 SG 152
Cdd:PRK10895 166 AG 167
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-151 |
3.76e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 4 RNITKYYRN---------KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------- 64
Cdd:PRK10419 7 SGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 -----------KMGYV-PEITPSRIpftLEEyPihMGKIRGMDKQHLRQRIDCLLEMFHLQ---ADRRTaiAELSKGMKQ 129
Cdd:PRK10419 87 frrdiqmvfqdSISAVnPRKTVREI---IRE-P--LRHLLSLDKAERLARASEMLRAVDLDdsvLDKRP--PQLSGGQLQ 158
|
170 180
....*....|....*....|..
gi 2182225815 130 KVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVS 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-148 |
6.22e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.90 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYY----RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KL-ASPL----- 64
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdltALsEKELrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 KMGYVPE---ITPSR-----IPFTLEeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQS 136
Cdd:PRK11153 83 QIGMIFQhfnLLSSRtvfdnVALPLE--------LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170
....*....|..
gi 2182225815 137 LIEETDFLILDE 148
Cdd:PRK11153 155 LASNPKVLLCDE 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-151 |
9.07e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGlIKPD---SGEVYKLASPLK------------ 65
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQasnirdteragi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 66 ------MGYVPEITPSRIPFTLEEypIHMGKIrgMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIE 139
Cdd:PRK13549 85 aiihqeLALVKELSVLENIFLGNE--ITPGGI--MDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170
....*....|..
gi 2182225815 140 ETDFLILDEPLS 151
Cdd:PRK13549 161 QARLLILDEPTA 172
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-152 |
9.52e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 9.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 10 YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---KMGYV------------PEIT- 73
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLalrqqvatvfqdPEQQi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 -----PSRIPFTLEEYpihmgkirGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:PRK13638 91 fytdiDSDIAFSLRNL--------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
....
gi 2182225815 149 PLSG 152
Cdd:PRK13638 163 PTAG 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-149 |
1.36e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------------- 64
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeagigii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 --KMGYVPEITPSRIPFTLEEYPIHMGKIrgmDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETD 142
Cdd:PRK10762 85 hqELNLIPQLTIAENIFLGREFVNRFGRI---DWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
....*..
gi 2182225815 143 FLILDEP 149
Cdd:PRK10762 162 VIIMDEP 168
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-151 |
1.38e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV----YKLASP--------LKMGYV 69
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdgLKVNDPkvderlirQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 -------PEITpsripfTLEEY---PIHmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIE 139
Cdd:PRK09493 83 fqqfylfPHLT------ALENVmfgPLR---VRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170
....*....|..
gi 2182225815 140 ETDFLILDEPLS 151
Cdd:PRK09493 154 KPKLMLFDEPTS 165
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-151 |
1.53e-13 |
|
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: 64.54 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkMGYVPeitpsripf 79
Cdd:cd03246 2 EVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-------LDGAD--------- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182225815 80 tleeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADrrtAIAE--LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03246 66 -----------ISQWDPNELGDHVGYLPQDDELFSG---SIAEniLSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-149 |
1.82e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------YKLASPL---------- 64
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhFDFSKTPsdkairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 KMGYV-------PEITpsrIPFTLEEYPIhmgKIRGMDKQHLRQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVIIMQ 135
Cdd:PRK11124 83 NVGMVfqqynlwPHLT---VQQNLIEAPC---RVLGLSKDQALARAEKLLERLRLKpyADRFP--LHLSGGQQQRVAIAR 154
|
170
....*....|....
gi 2182225815 136 SLIEETDFLILDEP 149
Cdd:PRK11124 155 ALMMEPQVLLFDEP 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-150 |
1.90e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 10 YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK------------MGYVPEITPSri 77
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlctyqkqlcfVGHRSGINPY-- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 78 pFTLEE---YPIHMGKIrgmdkqhlRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK13540 89 -LTLREnclYDIHFSPG--------AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-148 |
2.14e-13 |
|
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: 66.75 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKL-----VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklasplkMGYVPeITPSr 76
Cdd:COG4615 329 ELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL-------LDGQP-VTAD- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 77 ipfTLEEYPIHMGKI--------R--GMDKQHLRQRIDCLLEMFHLqaDRRTAIA-------ELSKGMKQKVIIMQSLIE 139
Cdd:COG4615 400 ---NREAYRQLFSAVfsdfhlfdRllGLDGEADPARARELLERLEL--DHKVSVEdgrfsttDLSQGQRKRLALLVALLE 474
|
....*....
gi 2182225815 140 ETDFLILDE 148
Cdd:COG4615 475 DRPILVFDE 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-151 |
2.50e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKR-------------QIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVPEI 72
Cdd:PRK10575 14 LRNVSFRVPGRtllhplsltfpagKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIPFTLEE------YPIH--MGKIRGMDKQHLRQRIDclleMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFL 144
Cdd:PRK10575 94 LPAAEGMTVRElvaigrYPWHgaLGRFGAADREKVEEAIS----LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
....*..
gi 2182225815 145 ILDEPLS 151
Cdd:PRK10575 170 LLDEPTS 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-149 |
2.67e-13 |
|
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: 65.12 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 8 KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVykLASPLKMGYVPEITPSRIPFTLEEypIH 87
Cdd:cd03237 7 KKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDTVSYKPQYIKADYEGTVRD--LL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182225815 88 MGKIRGMDKQ-HLRQRIDCLLEMFHLqADRRtaIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:cd03237 83 SSITKDFYTHpYFKTEIAKPLQIEQI-LDRE--VPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-159 |
2.73e-13 |
|
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: 66.58 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYR--NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK---------MGYVPE 71
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldavrqsLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 ITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170
....*....|.
gi 2182225815 152 G---QKRKVMW 159
Cdd:TIGR01257 1091 GvdpYSRRSIW 1101
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-151 |
3.33e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.52 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYY--------RNKLV---LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLAS- 62
Cdd:COG4608 9 EVRDLKKHFpvrgglfgRTVGVvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditGLSGr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 63 ---PL--KMGYV---------PEITPSRIpftLEEyPIhmgKIRGM-DKQHLRQRIDCLLEMFHL---QADRRTaiAELS 124
Cdd:COG4608 89 elrPLrrRMQMVfqdpyaslnPRMTVGDI---IAE-PL---RIHGLaSKAERRERVAELLELVGLrpeHADRYP--HEFS 159
|
170 180
....*....|....*....|....*..
gi 2182225815 125 KGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVS 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-57 |
3.57e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 3.57e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2182225815 4 RNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-149 |
4.74e-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: 65.59 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGL--IKPDSGEV-YKLASPLKMGYV--PEITPS 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiYHVALCEKCGYVerPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 RIPF---TLEEYPIHMGKIRGMDKQHLRQRIDC--------------------------------------LLEMFHLQa 114
Cdd:TIGR03269 81 PCPVcggTLEPEEVDFWNLSDKLRRRIRKRIAImlqrtfalygddtvldnvlealeeigyegkeavgravdLIEMVQLS- 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2182225815 115 DRRTAIA-ELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:TIGR03269 160 HRITHIArDLSGGEKQRVVLARQLAKEPFLFLADEP 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-151 |
6.61e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVL---------ENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMG-YVP 70
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRIPF--------------TLEEYPIHMGKirGMDKQHLRQRIDCLLEMFHLQADRRTAIAE-LSKGMKQKVIIMQ 135
Cdd:PRK15112 85 RSQRIRMIFqdpstslnprqrisQILDFPLRLNT--DLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLAR 162
|
170
....*....|....*.
gi 2182225815 136 SLIEETDFLILDEPLS 151
Cdd:PRK15112 163 ALILRPKVIIADEALA 178
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-149 |
6.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.34 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASPL-----KMGYVPEITPSRIPFT 80
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtSDEENLwdirnKAGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 LEEYPIHMG-KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK13633 102 IVEEDVAFGpENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-58 |
9.69e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 9.69e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 2 ELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:PRK13632 9 KVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK 67
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-152 |
1.02e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKL-----VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV--------YKLASPLKMG 67
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 YVPEITPSR-----------------IPFTLEEY--------------PIHMgkirGMDKQHLRQRIDCLLEMFHLQAD- 115
Cdd:PRK13651 83 VLEKLVIQKtrfkkikkikeirrrvgVVFQFAEYqlfeqtiekdiifgPVSM----GVSKEEAKKRAAKYIELVGLDESy 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2182225815 116 -RRTAIaELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK13651 159 lQRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAG 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-57 |
1.27e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 1.27e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI 59
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-152 |
1.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.49 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKL-----VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGE--VYKLASPLKMGYVPEITPS 75
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGDYAIPANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 R----IPFTLEEY--------------PIHMGKirgmDKQHLRQRIDCLLEMFHLQAD--RRTAIaELSKGMKQKVIIMQ 135
Cdd:PRK13645 89 RkeigLVFQFPEYqlfqetiekdiafgPVNLGE----NKQEAYKKVPELLKLVQLPEDyvKRSPF-ELSGGQKRRVALAG 163
|
170
....*....|....*..
gi 2182225815 136 SLIEETDFLILDEPLSG 152
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGG 180
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-58 |
1.57e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.18 E-value: 1.57e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182225815 1 MELRNITKYY-----RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-57 |
1.97e-12 |
|
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: 64.02 E-value: 1.97e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 2 ELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:COG4987 335 ELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-156 |
2.00e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL--------------KMGYVPE---ITPSRI 77
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeearaklrakHVGFVFQsfmLIPTLN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 78 PFTLEEYPihmGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSGQKRK 156
Cdd:PRK10584 105 ALENVELP---ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-151 |
2.03e-12 |
|
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: 62.51 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 20 SFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVykLASPLKMGYVPeitPSRIPFTL------------EEYPIH 87
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV--LINGVDVTAAP---PADRPVSMlfqennlfahltVEQNVG 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 88 MGKIRGMdkqHL----RQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03298 93 LGLSPGL---KLtaedRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-152 |
2.30e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK------------MG 67
Cdd:PRK13639 2 LETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllevrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 YVPEITPSRI--PFTLEEY---PIHMgkirGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETD 142
Cdd:PRK13639 82 IVFQNPDDQLfaPTVEEDVafgPLNL----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170
....*....|
gi 2182225815 143 FLILDEPLSG 152
Cdd:PRK13639 158 IIVLDEPTSG 167
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-151 |
2.69e-12 |
|
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: 62.25 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV---------YKLASPLKM-GYVP 70
Cdd:cd03253 2 EFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdireVTLDSLRRAiGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSripF--TLeEYPIHMGKIRGMDKQHLR----QRIDCLLEMFHLQADrrTAIAE----LSKGMKQKVIIMQSLIEE 140
Cdd:cd03253 82 QDTVL---FndTI-GYNIRYGRPDATDEEVIEaakaAQIHDKIMRFPDGYD--TIVGErglkLSGGEKQRVAIARAILKN 155
|
170
....*....|.
gi 2182225815 141 TDFLILDEPLS 151
Cdd:cd03253 156 PPILLLDEATS 166
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-156 |
2.78e-12 |
|
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: 63.31 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGlIKPD---SGEVYKLASPLK------------ 65
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKasnirdteragi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 66 ------MGYVPEITPSRIPFTLEEYpIHMGKIrgMDKQHLRQRIDCLLEMFHLQADRRT-AIAELSKGMKQKVIIMQSLI 138
Cdd:TIGR02633 81 viihqeLTLVPELSVAENIFLGNEI-TLPGGR--MAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALN 157
|
170
....*....|....*...
gi 2182225815 139 EETDFLILDEPLSGQKRK 156
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEK 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-151 |
2.79e-12 |
|
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: 61.72 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklaSPLKMGYVPEiTPSRIPFTLEEyPIHMGKI 91
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS---VPGSIAYVSQ-EPWIQNGTIRE-NILFGKP 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 92 rgMDKQHLRQRID--CL---LEMFHLqADrRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03250 92 --FDEERYEKVIKacALepdLEILPD-GD-LTEIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-151 |
3.13e-12 |
|
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: 62.25 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK--LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV---------YKLASpL--KMGY 68
Cdd:cd03251 2 EFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrdYTLAS-LrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VPEITpsrIPF--TLEEyPIHMGKIRGMDKQ--------HLRQRIDCLLEMFHlqadrrTAIAE----LSKGMKQKVIIM 134
Cdd:cd03251 81 VSQDV---FLFndTVAE-NIAYGRPGATREEveeaaraaNAHEFIMELPEGYD------TVIGErgvkLSGGQRQRIAIA 150
|
170
....*....|....*..
gi 2182225815 135 QSLIEETDFLILDEPLS 151
Cdd:cd03251 151 RALLKDPPILILDEATS 167
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-148 |
3.73e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGyvpeitpsripf 79
Cdd:PRK10522 323 LELRNVTfAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE------------ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 TLEEYPIHMGKI--------RGMDKQH---LRQRIDCLLEMFHLQ-----ADRRTAIAELSKGMKQKVIIMQSLIEETDF 143
Cdd:PRK10522 391 QPEDYRKLFSAVftdfhlfdQLLGPEGkpaNPALVEKWLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 2182225815 144 LILDE 148
Cdd:PRK10522 471 LLLDE 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-149 |
4.34e-12 |
|
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: 63.03 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYY-RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYV---PEITPSRIP 78
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-RPQPGIKVGYLpqePQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 F-TLEEypihmgkirGM-DKQHLRQRID---------------CLLEMFHLQA----------DRRTAIA---------- 121
Cdd:TIGR03719 86 ReNVEE---------GVaEIKDALDRFNeisakyaepdadfdkLAAEQAELQEiidaadawdlDSQLEIAmdalrcppwd 156
|
170 180 190
....*....|....*....|....*....|..
gi 2182225815 122 ----ELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-149 |
4.75e-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: 62.88 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 22 SIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKlasPLKMGYVPEITPSRIPFTLEEYpihmgkIRGMDKQHL-- 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLKISYKPQYISPDYDGTVEEF------LRSANTDDFgs 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 100 ---------RQRIDCLLEMfhlqadrrtAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:COG1245 433 syykteiikPLGLEKLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-58 |
4.81e-12 |
|
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: 61.68 E-value: 4.81e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2182225815 2 ELRNITKYY---RNKL-VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:COG4181 10 ELRGLTKTVgtgAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR 70
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-152 |
4.83e-12 |
|
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: 61.35 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVykLASPLKMGYVPEITPSRIpft 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--LLNGGPLDFQRDSIARGL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 leEYPIHMGKIRGM----------DKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:cd03231 76 --LYLGHAPGIKTTlsvlenlrfwHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
..
gi 2182225815 151 SG 152
Cdd:cd03231 154 TA 155
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-151 |
4.87e-12 |
|
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: 61.73 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYR--NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVykLASPLKMGYV-PEITPSRI 77
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVDGHDLALAdPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 78 PFTLEEYPIHMGKIR--------GMDkqhlRQRIDCLLEM-------FHLQADRRTAIAE----LSKGMKQKVIIMQSLI 138
Cdd:cd03252 79 GVVLQENVLFNRSIRdnialadpGMS----MERVIEAAKLagahdfiSELPEGYDTIVGEqgagLSGGQRQRIAIARALI 154
|
170
....*....|...
gi 2182225815 139 EETDFLILDEPLS 151
Cdd:cd03252 155 HNPRILIFDEATS 167
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-149 |
5.60e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK-----MGYVPE---I 72
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaeRGVVFQnegL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSR-----IPFTLEeypihmgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:PRK11248 82 LPWRnvqdnVAFGLQ--------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
..
gi 2182225815 148 EP 149
Cdd:PRK11248 154 EP 155
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-152 |
6.74e-12 |
|
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: 62.30 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK-LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVP 70
Cdd:TIGR02857 323 EFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadadswrdQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EiTPSRIPFTLEEyPIHMGK--------IRGMDKQHLRQRIDCLLEMFHLQADRRTaiAELSKGMKQKVIIMQSLIEETD 142
Cdd:TIGR02857 403 Q-HPFLFAGTIAE-NIRLARpdasdaeiREALERAGLDEFVAALPQGLDTPIGEGG--AGLSGGQAQRLALARAFLRDAP 478
|
170
....*....|
gi 2182225815 143 FLILDEPLSG 152
Cdd:TIGR02857 479 LLLLDEPTAH 488
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-149 |
7.41e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNK----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEvYKLA----SPLKMGYVPEI 72
Cdd:PRK10535 5 LELKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-YRVAgqdvATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIPFTLEEYPI--HMGKIR---------GMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEET 141
Cdd:PRK10535 84 RREHFGFIFQRYHLlsHLTAAQnvevpavyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
....*...
gi 2182225815 142 DFLILDEP 149
Cdd:PRK10535 164 QVILADEP 171
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-152 |
8.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.40 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL------------KMGYVPEiTPSRIPFTLEE 83
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmklreSVGMVFQ-DPDNQLFSASV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2182225815 84 YP-IHMGKIR-GMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK13636 101 YQdVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-150 |
8.49e-12 |
|
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: 60.45 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITkYYRNKLVL-ENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyklasplkmgyvpEITPSRIPF 79
Cdd:TIGR01189 1 LAARNLA-CSRGERMLfEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-------------RWNGTPLAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 TLEEYPIHM---GKIRGMdKQHL----------------RQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEE 140
Cdd:TIGR01189 67 QRDEPHENIlylGHLPGL-KPELsalenlhfwaaihggaQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170
....*....|
gi 2182225815 141 TDFLILDEPL 150
Cdd:TIGR01189 146 RPLWILDEPT 155
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-152 |
9.37e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-----------KLASPLK-MGYVpeitpsripFT 80
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditdkkvKLSDIRKkVGLV---------FQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 LEEYPIHMGKI----------RGMDKQHLRQRIDCLLEMFHLQAD--RRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:PRK13637 91 YPEYQLFEETIekdiafgpinLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
....
gi 2182225815 149 PLSG 152
Cdd:PRK13637 171 PTAG 174
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-151 |
9.68e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.29 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKL-VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYV 69
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaenekwvrsKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEiTPSRIPF--TLEE----YPIHMgkirGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDF 143
Cdd:PRK13647 85 FQ-DPDDQVFssTVWDdvafGPVNM----GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
....*...
gi 2182225815 144 LILDEPLS 151
Cdd:PRK13647 160 IVLDEPMA 167
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-149 |
9.68e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 23 IHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklaSPLKMGYVPEITPSRIPFTLEEYpihMGKIRGM-DKQHLRQ 101
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELKISYKPQYIKPDYDGTVEDL---LRSITDDlGSSYYKS 435
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2182225815 102 RIDCLLEMFHLqADRRtaIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK13409 436 EIIKPLQLERL-LDKN--VKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-153 |
1.08e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.93 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklaspLKMGYVPEITPSR---- 76
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIL-----FDGENIPAMSRSRlytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 77 ----------------------IPFTLEEYPihmgkirGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIM 134
Cdd:PRK11831 83 rkrmsmlfqsgalftdmnvfdnVAYPLREHT-------QLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170
....*....|....*....
gi 2182225815 135 QSLIEETDFLILDEPLSGQ 153
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQ 174
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-152 |
1.15e-11 |
|
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: 60.36 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPD---SGEVYKLASPLK-------MGYVPE---ITPSripF 79
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKpdqfqkcVAYVRQddiLLPG---L 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2182225815 80 TLEEYPIHMGKIRGMDKQHLRQR----IDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-46 |
1.20e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.82 E-value: 1.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKII 46
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-149 |
1.25e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVPEitpSRIPF- 79
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-GLAKGIKLGYFAQ---HQLEFl 388
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2182225815 80 TLEEYPI-HMGKIRgmdKQHLRQRIDCLLEMFHLQADRRTAIAE-LSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK10636 389 RADESPLqHLARLA---PQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-152 |
1.44e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV---------YKLASPLK--MGYV 69
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkditdWQTAKIMReaVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEITPSRIPFTLEEyPIHMGKIRGmDKQHLRQRIDCLLEMFHLQADRRTAIA-ELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:PRK11614 86 PEGRRVFSRMTVEE-NLAMGGFFA-ERDQFQERIKWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
....
gi 2182225815 149 PLSG 152
Cdd:PRK11614 164 PSLG 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-149 |
4.74e-11 |
|
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: 59.82 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRN------KLVlENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLAS----------PL 64
Cdd:TIGR03269 280 IKVRNVSKRYISvdrgvvKAV-DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmtkpgPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 KMGYVPEItpsrIPFTLEEYPIH--------MGKIRGMD--KQHLRQRIDCLLEMFHLQADRRTAI-----AELSKGMKQ 129
Cdd:TIGR03269 359 GRGRAKRY----IGILHQEYDLYphrtvldnLTEAIGLElpDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERH 434
|
170 180
....*....|....*....|
gi 2182225815 130 KVIIMQSLIEETDFLILDEP 149
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEP 454
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
2-151 |
4.98e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.61 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVleNVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyklaspLKMGY-VPEITPSRIPFT 80
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI------LWNGQdLTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 leeypihmgkirgMDKQ------HL--------------------RQRIDCLLEMFHLQ--ADRRTaiAELSKGMKQKVI 132
Cdd:COG3840 75 -------------MLFQennlfpHLtvaqniglglrpglkltaeqRAQVEQALERVGLAglLDRLP--GQLSGGQRQRVA 139
|
170
....*....|....*....
gi 2182225815 133 IMQSLIEETDFLILDEPLS 151
Cdd:COG3840 140 LARCLVRKRPILLLDEPFS 158
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-151 |
5.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.38 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNK--LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK----------MGY 68
Cdd:PRK13648 8 IVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnfeklrkhIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 V---PE------ITPSRIPFTLEEYPIHMGKIRGMDKQHLRQridclLEMFHlQADRRTaiAELSKGMKQKVIIMQSLIE 139
Cdd:PRK13648 88 VfqnPDnqfvgsIVKYDVAFGLENHAVPYDEMHRRVSEALKQ-----VDMLE-RADYEP--NALSGGQKQRVAIAGVLAL 159
|
170
....*....|..
gi 2182225815 140 ETDFLILDEPLS 151
Cdd:PRK13648 160 NPSVIILDEATS 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-151 |
7.07e-11 |
|
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: 58.39 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK-LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---------KLASPLKM-GYVP 70
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdiSRKSLRSMiGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EiTPSRIPFTLEEyPIHMGKIRGMDK--QHLRQRIDCLLEMFHLQADRRTAIAE----LSKGMKQKVIIMQSLIEETDFL 144
Cdd:cd03254 84 Q-DTFLFSGTIME-NIRLGRPNATDEevIEAAKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKIL 161
|
....*..
gi 2182225815 145 ILDEPLS 151
Cdd:cd03254 162 ILDEATS 168
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-157 |
7.25e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMgYVPEI-------- 72
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-LKPEIyrqqvsyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 --TPSRIPFTLEEYPIHMGKIRGmdKQHLRQRIDCLLEMFHL-QADRRTAIAELSKGMKQKViimqSLIEETDF----LI 145
Cdd:PRK10247 87 aqTPTLFGDTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRI----SLIRNLQFmpkvLL 160
|
170
....*....|....*.
gi 2182225815 146 LDEPLSG----QKRKV 157
Cdd:PRK10247 161 LDEITSAldesNKHNV 176
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-151 |
8.22e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.63 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIG--GLIKPD---SGEV----YKLASPL------- 64
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIvyngHNIYSPRtdtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 -KMGYVPEiTPSRIPFTLEEYPIHMGKIRGM-DKQHLRQRIDCLLE---MFHLQADR--RTAIAeLSKGMKQKVIIMQSL 137
Cdd:PRK14239 86 kEIGMVFQ-QPNPFPMSIYENVVYGLRLKGIkDKQVLDEAVEKSLKgasIWDEVKDRlhDSALG-LSGGQQQRVCIARVL 163
|
170
....*....|....
gi 2182225815 138 IEETDFLILDEPLS 151
Cdd:PRK14239 164 ATSPKIILLDEPTS 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-149 |
1.39e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYY-RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYkLASPLKMGYV---PEITPSRIP 78
Cdd:PRK11819 9 MNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-PAPGIKVGYLpqePQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 F-TLEEypihmgkirGM-DKQHLRQR--------------IDCLL-EMFHLQA----------DRR-------------- 117
Cdd:PRK11819 88 ReNVEE---------GVaEVKAALDRfneiyaayaepdadFDALAaEQGELQEiidaadawdlDSQleiamdalrcppwd 158
|
170 180 190
....*....|....*....|....*....|..
gi 2182225815 118 TAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-149 |
1.89e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYV----PEITPSRi 77
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLEVAYFdqhrAELDPEK- 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2182225815 78 pfTLEEyPIHMGK----IRGMDKQHLRQRIDCLlemFH-LQAdrRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK11147 399 --TVMD-NLAEGKqevmVNGRPRHVLGYLQDFL---FHpKRA--MTPVKALSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-152 |
3.66e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 18 NVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------KMGYVPEitpsriPFTL-EEYPI- 86
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiatrrRVGYMSQ------AFSLyGELTVr 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 87 -----HmGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKViimqSL----IEETDFLILDEPLSG 152
Cdd:NF033858 358 qnlelH-ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRL----SLavavIHKPELLILDEPTSG 427
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-58 |
4.18e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 4.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL 59
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-149 |
4.23e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVPEITPSRIPFT--------------- 80
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIVARLQQDPPRNVEGTvydfvaegieeqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 LEEYpiH-----------------MGKIRGM-DKQHLRQ---RIDCLLEMFHLQADrrTAIAELSKGMKQKVIIMQSLIE 139
Cdd:PRK11147 98 LKRY--HdishlvetdpseknlneLAKLQEQlDHHNLWQlenRINEVLAQLGLDPD--AALSSLSGGWLRKAALGRALVS 173
|
170
....*....|
gi 2182225815 140 ETDFLILDEP 149
Cdd:PRK11147 174 NPDVLLLDEP 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-64 |
4.54e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 4.54e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 1 MELRNITKYYRN-KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL 64
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL 405
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-158 |
5.13e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 14 LVLENVSFSIHKRQIIALV------------GKNGSGKSTLLKIIGGLIKPDSGEVY-------KLASPLkMGYVPEITP 74
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYykncninNIAKPY-CTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 75 SRIPFTLEEYPIHMGKIrgmdkQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE---PLS 151
Cdd:PRK13541 81 LKLEMTVFENLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEvetNLS 155
|
....*..
gi 2182225815 152 GQKRKVM 158
Cdd:PRK13541 156 KENRDLL 162
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-149 |
7.53e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVPEITPSRIP--F 79
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-KWSENANIGYYAQDHAYDFEndL 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2182225815 80 TLEEYpihMGKIR--GMDKQHLRQRIDCLLemFHlQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK15064 400 TLFDW---MSQWRqeGDDEQAVRGTLGRLL--FS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-152 |
9.54e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNK-----LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV-----YKLASPLKMGYVP 70
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRIP------------FTLEEYP---------IHMGKIR-GMDKQHLRQRIDCLLEMFHLQAD--RRTAIaELSKG 126
Cdd:PRK13631 102 NPYSKKIKnfkelrrrvsmvFQFPEYQlfkdtiekdIMFGPVAlGVKKSEAKKLAKFYLNKMGLDDSylERSPF-GLSGG 180
|
170 180
....*....|....*....|....*.
gi 2182225815 127 MKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAG 206
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1-152 |
1.42e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.85 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRnklvLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIkPDSGEVYKLASPL----------KMGYVP 70
Cdd:COG4138 1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsdwsaaelarHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 EITPSRIPFTLEEYpIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKV----IIMQ---SLIEETDF 143
Cdd:COG4138 76 QQQSPPFAMPVFQY-LALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVrlaaVLLQvwpTINPEGQL 154
|
....*....
gi 2182225815 144 LILDEPLSG 152
Cdd:COG4138 155 LLLDEPMNS 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-149 |
1.91e-09 |
|
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: 55.08 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKS-TLLKIIG----GLIKPdSGEV-YKLASPLKMgyvPE-----ITPSRIPFTLEE 83
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTALSILRllpdPAAHP-SGSIlFDGQDLLGL---SErelrrIRGNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 84 -----YPIH-----MGKI----RGMDKQHLRQRIDCLLEMFHLQADRRTAIA---ELSKGMKQKVIIMQSLIEETDFLIL 146
Cdd:COG4172 101 pmtslNPLHtigkqIAEVlrlhRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLIA 180
|
...
gi 2182225815 147 DEP 149
Cdd:COG4172 181 DEP 183
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-151 |
2.23e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVyklasplKMGYVpEITPSRipft 80
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI-------RVGDI-TIDTAR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 81 leeypiHMGKIRGMDKQhLRQRIDCLLEMFHL------------------QADRRTAIA--------------------E 122
Cdd:PRK11264 72 ------SLSQQKGLIRQ-LRQHVGFVFQNFNLfphrtvleniiegpvivkGEPKEEATArarellakvglagketsyprR 144
|
170 180
....*....|....*....|....*....
gi 2182225815 123 LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-151 |
2.32e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV---------YKLASplkmgyv 69
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghdlrdYTLAS------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 peitpSRIPFTLEEYPIHM------GKIR-GMDKQHLRQRIDCLLEMFH-------LQADRRTAIAE----LSKGMKQKV 131
Cdd:PRK11176 415 -----LRNQVALVSQNVHLfndtiaNNIAyARTEQYSREQIEEAARMAYamdfinkMDNGLDTVIGEngvlLSGGQRQRI 489
|
170 180
....*....|....*....|
gi 2182225815 132 IIMQSLIEETDFLILDEPLS 151
Cdd:PRK11176 490 AIARALLRDSPILILDEATS 509
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-152 |
2.60e-09 |
|
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: 53.71 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKL------VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKP--DSGEV-------YKLASPLKM 66
Cdd:cd03213 5 SFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrplDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 67 GYVPE---ITPSripFTLEEYPIHMGKIRGmdkqhlrqridcllemfhlqadrrtaiaeLSKGMKQKVIIMQSLIEETDF 143
Cdd:cd03213 85 GYVPQddiLHPT---LTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSL 132
|
....*....
gi 2182225815 144 LILDEPLSG 152
Cdd:cd03213 133 LFLDEPTSG 141
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-152 |
2.63e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLvlENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASPLK-----MGYVP 70
Cdd:PRK09700 267 EVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdiSPRSPLDavkkgMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 E------------------ITPSripFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRtaIAELSKGMKQKVI 132
Cdd:PRK09700 345 EsrrdngffpnfsiaqnmaISRS---LKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQN--ITELSGGNQQKVL 419
|
170 180
....*....|....*....|
gi 2182225815 133 IMQSLIEETDFLILDEPLSG 152
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRG 439
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-149 |
3.47e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNIT-KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------YKLASP-----LKMGYV 69
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrldgedITGLSPrerrrLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEitpSR-----IP-FTLEE-------YPIHMGKIRGMDKQHLRQRIDCLLEMFHLQA-DRRTAIAELSKGMKQKVIIMQ 135
Cdd:COG3845 339 PE---DRlgrglVPdMSVAEnlilgryRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTpGPDTPARSLSGGNQQKVILAR 415
|
170
....*....|....
gi 2182225815 136 SLIEETDFLILDEP 149
Cdd:COG3845 416 ELSRDPKLLIAAQP 429
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-149 |
4.11e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 5 NITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLAS---PLKMGYVPE--I 72
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWldgehiqHYASkevARRIGLLAQnaT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 73 TPSRIpfTLEE------YPihmgkirgmdKQHLRQRIDCLLEMFHLQADRRTAIAE--------LSKGMKQKVIIMQSLI 138
Cdd:PRK10253 92 TPGDI--TVQElvargrYP----------HQPLFTRWRKEDEEAVTKAMQATGITHladqsvdtLSGGQRQRAWIAMVLA 159
|
170
....*....|.
gi 2182225815 139 EETDFLILDEP 149
Cdd:PRK10253 160 QETAIMLLDEP 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-151 |
4.23e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 27 QIIALVGKNGSGKSTLLKIIGGLIKPDSG---------EVYK------LASPLKMGYVPEITPSRIPFTLEEYPIHM-GK 90
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdEVLKrfrgteLQNYFKKLYNGEIKVVHKPQYVDLIPKVFkGK 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182225815 91 IRGM-DKQHLRQRIDCLLEMFHLQA--DRRtaIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK13409 180 VRELlKKVDERGKLDEVVERLGLENilDRD--ISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-48 |
4.41e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 4.41e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGG 48
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-58 |
4.45e-09 |
|
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: 53.27 E-value: 4.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL 62
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-151 |
4.59e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK-------------MGYVPEI----TP 74
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhylhrqvalVGQEPVLfsgsVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 75 SRIPFTLEEYPihMGKIRGMDKQHLRQriDCLLEMFHlqaDRRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:TIGR00958 573 ENIAYGLTDTP--DEEIMAAAKAANAH--DFIMEFPN---GYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
.
gi 2182225815 151 S 151
Cdd:TIGR00958 646 S 646
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-59 |
4.88e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 4.88e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2182225815 3 LRNITKYYR----NK----------------LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYK 59
Cdd:PRK13546 7 IKNVTKEYRiyrtNKermkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR 83
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-152 |
5.03e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.15 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIK--PDSGEV-YKLASPLKMgyvpEIT----- 73
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSIlLDGEDILEL----SPDerara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 --------PSRIP-FTLEEYpIH--MGKIRG--MDKQHLRQRIDCLLEMFHLQAD--RRTAIAELSKGMKQKVIIMQSLI 138
Cdd:COG0396 78 giflafqyPVEIPgVSVSNF-LRtaLNARRGeeLSAREFLKLLKEKMKELGLDEDflDRYVNEGFSGGEKKRNEILQMLL 156
|
170
....*....|....
gi 2182225815 139 EETDFLILDEPLSG 152
Cdd:COG0396 157 LEPKLAILDETDSG 170
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-151 |
5.59e-09 |
|
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: 53.52 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 27 QIIALVGKNGSGKSTLLKIIGGLIKPDSG------------------EVYKLASPLKMGyvpEITPSRIPFTLEEYPIHM 88
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgsELQNYFTKLLEG---DVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 89 -GKIRG-MDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03236 104 kGKVGElLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-149 |
6.24e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 9 YYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY---KLASPLKMGYVPEITpSRIPFTLEEYP 85
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsgHDITRLKNREVPFLR-RQIGMIFQDHH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 86 IHMGK-----------IRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK10908 90 LLMDRtvydnvaipliIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-151 |
7.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.07 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKL-VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKP----------DSGEVYKLASPLKM-GY 68
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPqkgkvlvsgiDTGDFSKLQGIRKLvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 V---PEItpSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLI 145
Cdd:PRK13644 82 VfqnPET--QFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
....*.
gi 2182225815 146 LDEPLS 151
Cdd:PRK13644 160 FDEVTS 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-149 |
7.96e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEvYKLASPLKMGYVPEITPSRIPFTLE-------EY- 84
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS-YTFPGNWQLAWVNQETPALPQPALEyvidgdrEYr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 85 -------------------PIHmGKIRGMDKQHLRQRIDCLLEMFHLQADRRT-AIAELSKGMKQKVIIMQSLIEETDFL 144
Cdd:PRK10636 93 qleaqlhdanerndghaiaTIH-GKLDAIDAWTIRSRAASLLHGLGFSNEQLErPVSDFSGGWRMRLNLAQALICRSDLL 171
|
....*
gi 2182225815 145 ILDEP 149
Cdd:PRK10636 172 LLDEP 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-151 |
8.00e-09 |
|
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: 53.53 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIkPDSGEVYKLASPL-------------KMGYV---------PEIT 73
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdglsrralrplrrRMQVVfqdpfgslsPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 PSRIpftLEEyP--IHMgkiRGMDKQHLRQRIDCLLEMFHLQADRRTA-IAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:COG4172 381 VGQI---IAE-GlrVHG---PGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
.
gi 2182225815 151 S 151
Cdd:COG4172 454 S 454
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-165 |
9.39e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.71 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------------KLASPL--KMGYVPEITPSRIP 78
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkknKKLKPLrkKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 79 FTLEEYPIHMGKIR-GMDKQHLRQRIDCLLEMFHLQADRRT-AIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG---Q 153
Cdd:PRK13634 100 EETVEKDICFGPMNfGVSEEDAKQKAREMIELVGLPEELLArSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGldpK 179
|
170
....*....|..
gi 2182225815 154 KRKVMWKRFSCL 165
Cdd:PRK13634 180 GRKEMMEMFYKL 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-151 |
1.21e-08 |
|
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: 52.86 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 27 QIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYK---------------LASPLKMGYVPEITPSRIPFTLEEYP-IHMGK 90
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfrgteLQDYFKKLANGEIKVAHKPQYVDLIPkVFKGT 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182225815 91 IRG-MDKQHLRQRIDCLLEMFHLQA--DRRtaIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:COG1245 180 VRElLEKVDERGKLDELAEKLGLENilDRD--ISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-151 |
1.41e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 8 KYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKM-----GYVP-------EITPS 75
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdGQLKvadknqlRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 RIPFTLEEYPI--HMG----------KIRGMDKQHLRQRIDCLLEMFHL-QADRRTAIAELSKGMKQKVIIMQSLIEETD 142
Cdd:PRK10619 93 RLTMVFQHFNLwsHMTvlenvmeapiQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
....*....
gi 2182225815 143 FLILDEPLS 151
Cdd:PRK10619 173 VLLFDEPTS 181
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-152 |
1.43e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGliKPD----SGEV-YKLASPLKMGyvPEITPS 75
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDIlFKGESILDLE--PEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 76 RIPFTLEEYPIHMGKIRGMD----------KQHLRQRIDCL---------LEMFHLQAD--RRTAIAELSKGMKQKVIIM 134
Cdd:CHL00131 84 LGIFLAFQYPIEIPGVSNADflrlaynskrKFQGLPELDPLefleiinekLKLVGMDPSflSRNVNEGFSGGEKKRNEIL 163
|
170
....*....|....*...
gi 2182225815 135 QSLIEETDFLILDEPLSG 152
Cdd:CHL00131 164 QMALLDSELAILDETDSG 181
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-57 |
1.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 1.63e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI 64
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-151 |
1.73e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKI---IGGLIKP--DSGEVYKLASPLkmgYVPEITP- 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNL---YAPDVDPv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 75 ---SRI--------PFTLEEYP-IHMG-KIRGMdkqhlRQRIDCLLEMFHLQA-------DR-RTAIAELSKGMKQKVII 133
Cdd:PRK14243 88 evrRRIgmvfqkpnPFPKSIYDnIAYGaRINGY-----KGDMDELVERSLRQAalwdevkDKlKQSGLSLSGGQQQRLCI 162
|
170
....*....|....*...
gi 2182225815 134 MQSLIEETDFLILDEPLS 151
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCS 180
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1-152 |
2.34e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRnklvLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIkPDSGEVYKLASPLKMGYVPEIT------- 73
Cdd:PRK03695 1 MQLNDVAVSTR----LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELArhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 74 -PSRIPFTLEEYpiHMGKIRGMDKQHLRQ---RIDCLLEMFHLQADRRTAIAELSKGMKQKV----IIMQ---SLIEETD 142
Cdd:PRK03695 76 qQQTPPFAMPVF--QYLTLHQPDKTRTEAvasALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaaVVLQvwpDINPAGQ 153
|
170
....*....|
gi 2182225815 143 FLILDEPLSG 152
Cdd:PRK03695 154 LLLLDEPMNS 163
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-152 |
2.36e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------YKLASP---LKMGYVpEITPSR---------- 76
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldgheVVTRSPqdgLANGIV-YISEDRkrdglvlgms 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 77 ----IPFT-LEEYPIHMGKIRGMDKQhlrQRIDCLLEMFHLQA-DRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK10762 347 vkenMSLTaLRYFSRAGGSLKHADEQ---QAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
..
gi 2182225815 151 SG 152
Cdd:PRK10762 424 RG 425
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-149 |
2.37e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.45 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIK--PD---SGEVY------------KLASP 63
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYldgqdifkmdviELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 64 LKMGY-VPEITPSRIPFTLEEYPIHMGKIRGmDKQHLRQRIDCLLEMFHLQ---ADRRTAIA-ELSKGMKQKVIIMQSLI 138
Cdd:PRK14247 84 VQMVFqIPNPIPNLSIFENVALGLKLNRLVK-SKKELQERVRWALEKAQLWdevKDRLDAPAgKLSGGQQQRLCIARALA 162
|
170
....*....|.
gi 2182225815 139 EETDFLILDEP 149
Cdd:PRK14247 163 FQPEVLLADEP 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-152 |
5.46e-08 |
|
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: 49.83 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGL--IKPDSGEVY------KLASP---LKMGyvp 70
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILfkgediTDLPPeerARLG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 71 eIT-----PSRIP-FTLEEYpihmgkIRGMDKQhlrqridcllemfhlqadrrtaiaeLSKGMKQKVIIMQSLIEETDFL 144
Cdd:cd03217 79 -IFlafqyPPEIPgVKNADF------LRYVNEG-------------------------FSGGEKKRNEILQLLLLEPDLA 126
|
....*...
gi 2182225815 145 ILDEPLSG 152
Cdd:cd03217 127 ILDEPDSG 134
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-157 |
5.89e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKST----LLKIIgglikPDSGEVYKLASPLKMGYVPEITP--SRI------PF 79
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPvrHRIqvvfqdPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 TLEEYPIHMGKI---------RGMDKQHLRQRIDCLLEMFHLQADRRTAI-AELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK15134 373 SSLNPRLNVLQIieeglrvhqPTLSAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
....*...
gi 2182225815 150 LSGQKRKV 157
Cdd:PRK15134 453 TSSLDKTV 460
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-148 |
6.20e-08 |
|
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: 50.10 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKL--VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVykLASPLKMGYVP-EITPSRI 77
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI--EIDGIDISTIPlEDLRSSL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 78 PFTLEEYPIHMGKIRGMdkqhlrqridclLEMFHLQADR--RTA--IAE----LSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:cd03369 85 TIIPQDPTLFSGTIRSN------------LDPFDEYSDEeiYGAlrVSEgglnLSQGQRQLLCLARALLKRPRVLVLDE 151
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-151 |
6.73e-08 |
|
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: 51.06 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGevyKLASPLKMGYVPEiTPSRIPFTLEEypihmGKIRGM 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG---KIKHSGRISFSPQ-TSWIMPGTIKD-----NIIFGL 511
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 95 DKQHLRQRI---DCLLE--MFHLQADRRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:TIGR01271 512 SYDEYRYTSvikACQLEedIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-151 |
7.07e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNIT-KYYRNKLV--LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMG 67
Cdd:PRK13642 5 LEVENLVfKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaenvwnlrrKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 YVPEITPSRIPFTLEEYPIHMG-KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLIL 146
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDDVAFGmENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
....*
gi 2182225815 147 DEPLS 151
Cdd:PRK13642 165 DESTS 169
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-149 |
7.24e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVlENVSFSIHKRQIIALVGKNGSGKS-TLLKIIGGL---IKPDSGEVYKLASPLKMGYVPEITPSR 76
Cdd:PRK10418 5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 77 I---------PF-TLEEYPIHMGKIRGmdKQHLRQRIDCLLEMFHLQADRRTAIA---ELSKGMKQKVIIMQSLIEETDF 143
Cdd:PRK10418 84 ImqnprsafnPLhTMHTHARETCLALG--KPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPF 161
|
....*.
gi 2182225815 144 LILDEP 149
Cdd:PRK10418 162 IIADEP 167
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-57 |
9.26e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.99 E-value: 9.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2182225815 14 LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 62
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-151 |
1.14e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.80 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKL-ASPLKMG---------- 67
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKItVDGITLTaktvwdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 68 -----------YVPEITPSRIPFTLEEypihmgkiRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQS 136
Cdd:PRK13640 86 vgivfqnpdnqFVGATVGDDVAFGLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170
....*....|....*
gi 2182225815 137 LIEETDFLILDEPLS 151
Cdd:PRK13640 158 LAVEPKIIILDESTS 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-151 |
1.39e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASplkMGYVPE-------ITPSRIPFTLEEyp 85
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS---IAYVPQqawimnaTVRGNILFFDEE-- 747
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2182225815 86 ihmgkirgmDKQHLRQRIDCLlemfHLQADRR-------TAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PTZ00243 748 ---------DAARLADAVRVS----QLEADLAqlgggleTEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-149 |
1.69e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 14 LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASpLKMG-----YVPEITPSRIP--FTLEEYPi 86
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-VRMAvfsqhHVDGLDLSSNPllYMMRCFP- 600
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182225815 87 hmgkirGMDKQHLRQRIDCLLEMFHLQADrrtAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PLN03073 601 ------GVPEQKLRAHLGSFGVTGNLALQ---PMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-158 |
1.73e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 28 IIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPL---------------KMGYVpeITPSRIpftleeYPiH---MG 89
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRVlfdaekgiclppekrRIGYV--FQDARL------FP-HykvRG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 90 KIR-GMDKQHLRQ--RIDCLLEMFHLqADRRTaiAELSKGMKQKVIIMQSLIEETDFLILDEPLSG----QKRKVM 158
Cdd:PRK11144 96 NLRyGMAKSMVAQfdKIVALLGIEPL-LDRYP--GSLSGGEKQRVAIGRALLTAPELLLMDEPLASldlpRKRELL 168
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-151 |
1.76e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 20 SFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYklaspLKMGYVPEITPSRIP-------------FTLEE--- 83
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-----LNGQDHTTTPPSRRPvsmlfqennlfshLTVAQnig 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182225815 84 YPIHMG-KIRGMDKQHLRQR-----IDCLLEMFHlqadrrtaiAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK10771 94 LGLNPGlKLNAAQREKLHAIarqmgIEDLLARLP---------GQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-149 |
1.79e-07 |
|
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: 49.67 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEITpSRIPFTLEEYPIHMGKIRgm 94
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVR-- 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182225815 95 dkQHLR-QRIDC-------LLEMFHLQADRR-------TAIAE----LSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:TIGR02868 427 --ENLRlARPDAtdeelwaALERVGLADWLRalpdgldTVLGEggarLSGGERQRLALARALLADAPILLLDEP 498
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-152 |
2.50e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 17 ENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------KLASP---LKMGYV--PE------ITP----- 74
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpiDIRSPrdaIRAGIMlcPEdrkaegIIPvhsva 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 75 ------SRIPFTLEEYPIHMGKIRGMDKQHLRQ-RIDcllemfhlQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:PRK11288 350 dninisARRHHLRAGCLINNRWEAENADRFIRSlNIK--------TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
....*
gi 2182225815 148 EPLSG 152
Cdd:PRK11288 422 EPTRG 426
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-151 |
3.20e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.47 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDS---------GEVYKLASPL------- 64
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLardirks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 65 --KMGYVPE---------ITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCL--LEMFHLQADRrtaIAELSKGMKQKV 131
Cdd:PRK09984 85 raNTGYIFQqfnlvnrlsVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALtrVGMVHFAHQR---VSTLSGGQQQRV 161
|
170 180
....*....|....*....|
gi 2182225815 132 IIMQSLIEETDFLILDEPLS 151
Cdd:PRK09984 162 AIARALMQQAKVILADEPIA 181
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-57 |
4.14e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 4.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 2 ELRNITKYyrnklVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIK--PDSGEV 57
Cdd:COG2401 37 ELRVVERY-----VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV 89
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-149 |
4.51e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.91 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIkpDSGEVYKLASPLKMG----YVPEITPSR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLL--ELNEEARVEGEVRLFgrniYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 77 I------------PF---TLEEYPIHMGKIRGM--DKQHLRQRIDCLLEMFHLQADRRTAI----AELSKGMKQKVIIMQ 135
Cdd:PRK14267 83 VrrevgmvfqypnPFphlTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLndypSNLSGGQRQRLVIAR 162
|
170
....*....|....
gi 2182225815 136 SLIEETDFLILDEP 149
Cdd:PRK14267 163 ALAMKPKILLMDEP 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-57 |
4.56e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.28 E-value: 4.56e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 1 MELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-149 |
5.18e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 5 NITKYYRNKLVLENVS--FSIHKRqiIALVGKNGSGKSTLLKIIGGLIKPDSGEVyKLASPLKMGYVpeitpSRIPFTLE 82
Cdd:PRK15064 6 NITMQFGAKPLFENISvkFGGGNR--YGLIGANGCGKSTFMKILGGDLEPSAGNV-SLDPNERLGKL-----RQDQFAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 83 EYP----IHMGKIRGMDKQHLRQRIDCLLEMF--------HLQA-----DRRTA---------------------IAELS 124
Cdd:PRK15064 78 EFTvldtVIMGHTELWEVKQERDRIYALPEMSeedgmkvaDLEVkfaemDGYTAearagelllgvgipeeqhyglMSEVA 157
|
170 180
....*....|....*....|....*
gi 2182225815 125 KGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK15064 158 PGWKLRVLLAQALFSNPDILLLDEP 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-151 |
6.32e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 3 LRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEITPSRIPFTLE 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 83 E-----------------YPihmgkIRGM--DKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDF 143
Cdd:PRK10982 81 ElnlvlqrsvmdnmwlgrYP-----TKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
....*...
gi 2182225815 144 LILDEPLS 151
Cdd:PRK10982 156 VIMDEPTS 163
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-148 |
6.59e-07 |
|
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: 47.15 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNK---LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-------KLASPL---KMGY 68
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirDLNLRWlrsQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VPEiTPSRIPFTLEEyPIHMGK---IRGMDKQHLRQR-----IDCLLEMFHLQADRRTaiAELSKGMKQKVIIMQSLIEE 140
Cdd:cd03249 82 VSQ-EPVLFDGTIAE-NIRYGKpdaTDEEVEEAAKKAnihdfIMSLPDGYDTLVGERG--SQLSGGQKQRIAIARALLRN 157
|
....*...
gi 2182225815 141 TDFLILDE 148
Cdd:cd03249 158 PKILLLDE 165
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-152 |
6.65e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 20 SFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASplkmgyvpeiTPSRIPF-----------------TLE 82
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFS----------HITRLSFeqlqklvsdewqrnntdMLS 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 83 EYPIHMGKIRG---MDKQHLRQRIDCLLEMFHLQA--DRRtaIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK10938 93 PGEDDTGRTTAeiiQDEVKDPARCEQLAQQFGITAllDRR--FKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-165 |
6.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.42 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV------------YKLASPL--KMGYVPEITPSRIPFTL 81
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskQKEIKPVrkKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 82 EEYPIHMGKIR-GMDKQHLRQRIDCLLEMFHLQAD-RRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG---QKRK 156
Cdd:PRK13643 102 VLKDVAFGPQNfGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGldpKARI 181
|
....*....
gi 2182225815 157 VMWKRFSCL 165
Cdd:PRK13643 182 EMMQLFESI 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-151 |
8.08e-07 |
|
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: 47.63 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASplkMGYVPE---ITPSripfTLEEyPIHMGKir 92
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---VAYVPQqawIQND----SLRE-NILFGK-- 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 93 GMDKQHLRQRIDCL-----LEMfhLQADRRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:TIGR00957 724 ALNEKYYQQVLEACallpdLEI--LPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-136 |
8.15e-07 |
|
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: 46.21 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 25 KRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLKMGYVPEITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRID 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110
....*....|....*....|....*....|....
gi 2182225815 105 CLL--EMFHLqADRRTAIAELSKGMKQKVIIMQS 136
Cdd:smart00382 81 VLIldEITSL-LDAEQEALLLLLEELRLLLLLKS 113
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-43 |
8.44e-07 |
|
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: 47.16 E-value: 8.44e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2182225815 1 MELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLL 43
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLL 47
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-152 |
8.68e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYY---RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLK-IIGGLIKPDSGEVY------KLASPLK----- 65
Cdd:PRK13549 260 LEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFidgkpvKIRNPQQaiaqg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 66 MGYVPE----------------ITPSripfTLEEYpIHMGKIRGMDKQHLRQRidcllEMFHLQ---ADRRTAIAELSKG 126
Cdd:PRK13549 340 IAMVPEdrkrdgivpvmgvgknITLA----ALDRF-TGGSRIDDAAELKTILE-----SIQRLKvktASPELAIARLSGG 409
|
170 180
....*....|....*....|....*.
gi 2182225815 127 MKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRG 435
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-151 |
9.15e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.49 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKY-YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYkLASPLKMGYVPEiTPSRIPF 79
Cdd:COG4178 363 LALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-RPAGARVLFLPQ-RPYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 80 TLEE---YPihmGKIRGMDKQHLRQ-----RIDCLLEMFHLQADRRtaiAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:COG4178 441 TLREallYP---ATAEAFSDAELREaleavGLGHLAERLDEEADWD---QVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-152 |
9.54e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 2 ELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGG---------LI----KPDSGEV---------Yk 59
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndLTlfgrRRGSGETiwdikkhigY- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 60 LASPLKMGYvpEITPSRIPFTLEEYPIHMGKIRGM-DKQhlRQRIDCLLEMFHLqaDRRTAIA---ELSKGMKQKVIIMQ 135
Cdd:PRK10938 341 VSSSLHLDY--RVSTSVRNVILSGFFDSIGIYQAVsDRQ--QKLAQQWLDILGI--DKRTADApfhSLSWGQQRLALIVR 414
|
170
....*....|....*..
gi 2182225815 136 SLIEETDFLILDEPLSG 152
Cdd:PRK10938 415 ALVKHPTLLILDEPLQG 431
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-149 |
1.01e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.77 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 9 YYRNKL-VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPLK----------MGYVPEITPSRI 77
Cdd:PRK13543 19 FSRNEEpVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrgdrsrfmayLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2182225815 78 pfTLEEypIHMgkIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK13543 99 --TLEN--LHF--LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-149 |
1.06e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRN----KLVLENVSFSIHKRQIIALVGKNGSGKS-TLLKIIGGLikPDSGEVYKLASPLKMG----YVPE 71
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSGDIRFHGesllHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 -----ITPSRIPFTLEE-----YPIH---------MGKIRGMDKQHLRQRI-DCLLEMFHLQADRRTA--IAELSKGMKQ 129
Cdd:PRK15134 84 qtlrgVRGNKIAMIFQEpmvslNPLHtlekqlyevLSLHRGMRREAARGEIlNCLDRVGIRQAAKRLTdyPHQLSGGERQ 163
|
170 180
....*....|....*....|
gi 2182225815 130 KVIIMQSLIEETDFLILDEP 149
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEP 183
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-151 |
1.30e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLAS----PLKMGYVPEITpsripfTLEEYPIHmGKI 91
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaaliAISSGLNGQLT------GIENIELK-GLM 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 92 RGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK13545 113 MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-158 |
1.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.70 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY------------KLASPL--KMGYVPEITPSRIPFTL 81
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdKYIRPVrkRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 82 EEYPIHMG-KIRGMDKQHLRQR-IDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG----QKR 155
Cdd:PRK13646 103 VEREIIFGpKNFKMNLDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGldpqSKR 182
|
...
gi 2182225815 156 KVM 158
Cdd:PRK13646 183 QVM 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-151 |
1.61e-06 |
|
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: 46.17 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY-KLASPLKMGYVPEITPSRIPF------------TLE 82
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwSNKNESEPSFEATRSRNRYSVayaaqkpwllnaTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 83 EYPIHMGKIRgmdkqhlRQRIDCLLEMFHLQAD-------RRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:cd03290 97 ENITFGSPFN-------KQRYKAVTDACSLQPDidllpfgDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-159 |
4.91e-06 |
|
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: 45.39 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYY--RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL---------KMGYV 69
Cdd:TIGR01257 1938 LRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisdvhqNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQ--ADRRTAIaeLSKGMKQKVIIMQSLIEETDFLILD 147
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSlyADRLAGT--YSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170
....*....|....*
gi 2182225815 148 EPLSG---QKRKVMW 159
Cdd:TIGR01257 2096 EPTTGmdpQARRMLW 2110
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-152 |
5.46e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 14 LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLA---SPLKMGYVPEITPSRIPFTLEEYPI--HM 88
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALmpHM 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182225815 89 G---------KIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK10070 122 TvldntafgmELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-159 |
5.84e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSG--KSTLLKIIGGlikPDSGE---------VYKLASPLKMG-Y 68
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrf*twcANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 69 VPEITPSRIPFTLEEYPIHMGKIRGMDKQHLRQRIDCLLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170
....*....|....
gi 2182225815 149 PLSG---QKRKVMW 159
Cdd:NF000106 171 PTTGldpRTRNEVW 184
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-57 |
7.18e-06 |
|
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: 44.81 E-value: 7.18e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-149 |
8.98e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.45 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIkPDSGEV----YKLASPLKMGYVPEIT-----PSRIPFTLEE 83
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingIELRELDPESWRKHLSwvgqnPQLPHGTLRD 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182225815 84 yPIHMGKIRgMDKQHLRQRID--CLLEMFHLQAD-RRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PRK11174 442 -NVLLGNPD-ASDEQLQQALEnaWVSEFLPLLPQgLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEP 512
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-151 |
9.23e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 44.70 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL----------KMGYVpeitpSRIPFTL 81
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswrsRLAVV-----SQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 82 EEY---PIHMGKiRGMDKQHLRQ--RIDCLLE-MFHLQADRRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PRK10789 402 SDTvanNIALGR-PDATQQEIEHvaRLASVHDdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-151 |
9.24e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 9 YYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGL-------IKPDSGEVY-----------KLASPLKMGY-V 69
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydskIKVDGKVLYfgkdifqidaiKLRKEVGMVFqQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 70 PEITPSRIPFTLEEYPIHMGKIRgmDKQHLRQRIDCLLEMFHLQA---DRRTAIA-ELSKGMKQKVIIMQSLIEETDFLI 145
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIK--EKREIKKIVEECLRKVGLWKevyDRLNSPAsQLSGGQQQRLTIARALALKPKVLL 176
|
....*.
gi 2182225815 146 LDEPLS 151
Cdd:PRK14246 177 MDEPTS 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-43 |
1.21e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 1.21e-05
10 20 30
....*....|....*....|....*....|
gi 2182225815 14 LVLENVSFSIHKRQIIALVGKNGSGKSTLL 43
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLL 1353
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-48 |
1.24e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.66 E-value: 1.24e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2182225815 11 RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGG 48
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-152 |
1.64e-05 |
|
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: 42.53 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 11 RNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPlKMGYVPEiTPSRIPFTLEE---YPIH 87
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-DLLFLPQ-RPYLPLGTLREqliYPWD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182225815 88 MgkirgmdkqhlrqridcllemfhlqadrrtaiaELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03223 90 D---------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-57 |
2.64e-05 |
|
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: 43.36 E-value: 2.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 1 MELRNITKYYRN--KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDsGEV 57
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEI 1275
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-57 |
2.70e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.03 E-value: 2.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2182225815 2 ELRNITKYYRNKL-VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK13657 336 EFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-58 |
2.81e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.03 E-value: 2.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 1 MELRNITKYYRNK--------LV--LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkperLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELY 73
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-55 |
6.83e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 6.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2182225815 1 MELRNIT-KYYRNklvLENVSFSIHKrQIIALVGKNGSGKSTLLKIIGGLIKPDSG 55
Cdd:COG3593 1 MKLEKIKiKNFRS---IKDLSIELSD-DLTVLVGENNSGKSSILEALRLLLGPSSS 52
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-57 |
7.13e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 7.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 1 MELRNITKYYRNKL--VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI 1296
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-165 |
1.36e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 13 KLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPdsGEVYKLASPLKMGYVPEItPSRIPFTLEEYPIHMGKI- 91
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH--AETSSVVIRGSVAYVPQV-SWIFNATVRENILFGSDFe 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 92 -----RGMDKQHLRQRIDCLlemfhlQADRRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLSGQKRKVMWKRF 162
Cdd:PLN03232 707 serywRAIDVTALQHDLDLL------PGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
....
gi 2182225815 163 -SCL 165
Cdd:PLN03232 781 dSCM 784
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-151 |
1.42e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASplKMGYVPEItpSRI-------------PFTLE 82
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG--TVAYVPQV--SWIfnatvrdnilfgsPFDPE 708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182225815 83 EYPihmgkiRGMDKQHLRQRIDCLlemfhlQADRRTAIAE----LSKGMKQKVIIMQSLIEETDFLILDEPLS 151
Cdd:PLN03130 709 RYE------RAIDVTALQHDLDLL------PGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
14-150 |
1.67e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.43 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 14 LVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKL-ASPLKMGYVPEITPSripFTLEEYPIHMGKIR 92
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLrGDALPLGANSFILPG---LTGEENARMMASLY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 93 GMDKQHLRQRIDCLLEMFHLQADRrtaIAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK15177 78 GLDGDEFSHFCYQLTQLEQCYTDR---VSEYSVTMKTHLAFAINLLLPCRLYIADGKL 132
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-46 |
1.72e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 1.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2182225815 1 MELRNITKY-YRNklvLENVSFSIHK-RQIIALVGKNGSGKSTLLKII 46
Cdd:COG3950 1 MRIKSLTIEnFRG---FEDLEIDFDNpPRLTVLVGENGSGKTTLLEAI 45
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-152 |
1.96e-04 |
|
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: 39.92 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKII-----GGLIKpdsGEVYKLASPLKM------GYVpeitpsripft 80
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKnfqrstGYV----------- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2182225815 81 lEEYPIHMGkirgmdKQHLRQRIdclleMFHlqADRRtaiaELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:cd03232 85 -EQQDVHSP------NLTVREAL-----RFS--ALLR----GLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-57 |
2.33e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 2.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 1 MELRNITKYYRNKLVLE---NVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI 442
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-148 |
2.84e-04 |
|
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: 40.12 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 12 NKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKlASPLKMGYVPEiTPSRIPFTLEE---YP--I 86
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK-PAKGKLFYVPQ-RPYMTLGTLRDqiiYPdsS 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 87 HMGKIRGMDKQHLRQRIDcLLEMFHLqADRR---TAIA----ELSKGMKQKVIIMQSLIEETDFLILDE 148
Cdd:TIGR00954 542 EDMKRRGLSDKDLEQILD-NVQLTHI-LEREggwSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-86 |
3.10e-04 |
|
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: 39.68 E-value: 3.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2182225815 28 IIALVGKNGSGKSTLLKIIgGLIKPDSGEVYKLASPLKMGYVPEITPSRIPFTLEEYPI 86
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEAL-RFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPI 58
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-57 |
3.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 39.73 E-value: 3.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2182225815 16 LENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV 57
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV 64
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-53 |
4.11e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 39.50 E-value: 4.11e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2182225815 15 VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPD 53
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN 60
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-151 |
4.94e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 10 YRNKL--VLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEV----YKLAsplKMGYV------------PE 71
Cdd:PLN03232 1244 YRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddCDVA---KFGLTdlrrvlsiipqsPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 72 ITPSRIPFTLEEYPIH--MGKIRGMDKQHLRQRIDclLEMFHLQADRRTAIAELSKGMKQKVIIMQSLIEETDFLILDEP 149
Cdd:PLN03232 1321 LFSGTVRFNIDPFSEHndADLWEALERAHIKDVID--RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
..
gi 2182225815 150 LS 151
Cdd:PLN03232 1399 TA 1400
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
10-52 |
8.55e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.49 E-value: 8.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2182225815 10 YRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKP 52
Cdd:COG1106 13 FKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNL 55
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-151 |
9.18e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 38.53 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 19 VSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVYKLASPL-KMGYV---------------------PEITPSR 76
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDewravrsdiqmifqdplaslnPRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182225815 77 I---PftLEEYPIHmgkirgMDKQHLRQRIDCLLEMFHL---QADRRTaiAELSKGMKQKVIIMQSLIEETDFLILDEPL 150
Cdd:PRK15079 120 IiaeP--LRTYHPK------LSRQEVKDRVKAMMLKVGLlpnLINRYP--HEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
.
gi 2182225815 151 S 151
Cdd:PRK15079 190 S 190
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
31-46 |
2.04e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 37.05 E-value: 2.04e-03
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-46 |
2.21e-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: 36.86 E-value: 2.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2182225815 1 MELRNITKYYRNklvlENVSFS-IHKRQIIALVGKNGSGKSTLLKII 46
Cdd:cd03279 6 LELKNFGPFREE----QVIDFTgLDNNGLFLICGPTGAGKSTILDAI 48
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
20-47 |
3.48e-03 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 36.51 E-value: 3.48e-03
10 20
....*....|....*....|....*...
gi 2182225815 20 SFSIHKRQIIALVGKNGSGKSTLLKIIG 47
Cdd:cd03283 19 DIDMEKKNGILITGSNMSGKSTFLRTIG 46
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-58 |
5.16e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 36.23 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2182225815 1 MELRNITKYYRNKLVLENVSFSIHKRQIIALVGKNGSGKSTLLKIIGGLIKPDSGEVY 58
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRY 79
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
117-152 |
5.24e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 36.25 E-value: 5.24e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2182225815 117 RTAIAELSKGMKQKVIIMQSLIEETDFLILDEPLSG 152
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-43 |
5.70e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 35.76 E-value: 5.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2182225815 2 ELRNItKYYRNKLVLEnvsFSihkRQIIALVGKNGSGKSTLL 43
Cdd:COG0419 6 RLENF-RSYRDTETID---FD---DGLNLIVGPNGAGKSTIL 40
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-47 |
7.03e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 36.06 E-value: 7.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2182225815 2 ELRNitkyYRNklvLENVSFSIHkrQIIALVGKNGSGKSTLLKIIG 47
Cdd:COG4637 6 RIKN----FKS---LRDLELPLG--PLTVLIGANGSGKSNLLDALR 42
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-43 |
7.88e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 35.90 E-value: 7.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2182225815 2 ELRNitkyYRNklvLENVSFSIHKRqIIALVGKNGSGKSTLL 43
Cdd:COG1195 6 SLTN----FRN---YESLELEFSPG-INVLVGPNGQGKTNLL 39
|
|
| |
