|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-201 |
3.52e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 201.45 E-value: 3.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ--DKIGYVPQ 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRCFKALCKAPLSNV--LIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEAreRIDELLELFGLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739682787 157 GIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:COG1131 161 GLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-201 |
4.05e-60 |
|
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: 186.45 E-value: 4.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK--IGYVPQ 79
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRcfkalckaplsnvlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:cd03230 81 EPSLYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739682787 160 LKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03230 128 PESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNN 170
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-199 |
1.01e-59 |
|
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: 187.76 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK--KQRQDKIGYVP 78
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENIRCFKALCKAPLSNV--LIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPT 155
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELkkRIEELIELLGLEEfLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739682787 156 VGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-196 |
4.13e-56 |
|
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: 177.70 E-value: 4.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKC--IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL--SKKQRQDKIGYV 77
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRCFKALCKAPLS--NVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEP 154
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSeiKEEVELLLRVLGLTDkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739682787 155 TVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQI 196
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRI 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-199 |
4.55e-50 |
|
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: 161.98 E-value: 4.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENlQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR--QDKIGYVPQ 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQklRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRCFKALCKAPLSNV--LIDEYARQLNLNER-TMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVkaRVDEVLELVNLGDRaKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739682787 157 GIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQIKVI 199
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVL 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-191 |
1.33e-49 |
|
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: 160.72 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK--QRQDKIGYVP 78
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAreDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENIRCFKALCKAPLSNVLIDEYARQLNLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVG 157
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 739682787 158 IDLKSRFDIHNLLNTM-KRERLIILTTHHLDEVEA 191
Cdd:COG4133 162 LDAAGVALLAELIAAHlARGGAVLLTTHQPLELAA 196
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-196 |
7.91e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.17 E-value: 7.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRqdKIGYVPQD 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR--RIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEH--MTVNE--------NIRCFKALCKAP-------LSNVLIDEYARQLnlnertmtISNLSGGTKRKvnVLI--G 141
Cdd:COG1121 84 AEVDWDfpITVRDvvlmgrygRRGLFRRPSRADreavdeaLERVGLEDLADRP--------IGELSGGQQQR--VLLarA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 142 LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQI 196
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRV 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-199 |
1.84e-42 |
|
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: 142.66 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-KQRQDKIGYVPQD 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIrCF---KALCKAPLSNVLIDEYARQLNL-NERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03259 81 YALFPHLTVAENI-AFglkLRGVPKAEIRARVRELLELVGLeGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739682787 157 GIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:cd03259 160 ALDAKLREELREELKELQRELGIttIYVTHDQEEALALADRIAVM 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-201 |
6.42e-41 |
|
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: 139.17 E-value: 6.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQD---KIG 75
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisGLSEAELYRlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALFEHMTVNENIrCFKALCKAPLSNVLIDEYARQ-LNL-----NERTMTiSNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:cd03261 81 MLFQSGALFDSLTVFENV-AFPLREHTRLSEEEIREIVLEkLEAvglrgAEDLYP-AELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYD 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-201 |
9.37e-41 |
|
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: 136.93 E-value: 9.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-----KQRQDKIGY 76
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRcfkalckaplsnvlideYArqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------LG--------------LSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739682787 157 GIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-205 |
2.27e-40 |
|
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: 137.28 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRqdKIGYVPQdIA 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK--RIGYVPQ-RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 83 LFEH---MTVNE-----------NIRCFKALCKAplsnvLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:cd03235 78 SIDRdfpISVRDvvlmglyghkgLFRRLSKADKA-----KVDEALERVGLSElADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGNDPFY 205
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-201 |
2.53e-40 |
|
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: 137.46 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK-KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYV 77
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQ--DIALFEhMTVNENIrCFkalckAPLSNVL--------IDEYARQLNLNE-RTMTISNLSGGTKRKVnVLIGLLS-N 145
Cdd:COG1122 81 FQnpDDQLFA-PTVEEDV-AF-----GPENLGLpreeirerVEEALELVGLEHlADRPPHELSGGQKQRV-AIAGVLAmE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVIGN 201
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-201 |
4.73e-40 |
|
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: 136.44 E-value: 4.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDKIGYV 77
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDialFEHMTVNENIR---CFkALCKAPLS----NVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:cd03225 81 FQN---PDDQFFGPTVEeevAF-GLENLGLPeeeiEERVEEALELVGLEGlRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLED 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-213 |
2.90e-38 |
|
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: 132.41 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQD---KI 74
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditGLSEKELYElrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENI----RCFKALCKAplsnvLIDEYAR----QLNLNE-RTMTISNLSGGTKRKVnvliGL--- 142
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVafplREHTDLSEA-----EIRELVLekleLVGLPGaADKMPSELSGGMRKRV----ALara 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 143 -LSNPQILILDEPTVGIDLKSRFDIHNLLNTMkRERL---IILTTHHLDEVEALADQI------KVIGNDPFyRELLEDK 212
Cdd:COG1127 156 lALDPEILLYDEPTAGLDPITSAVIDELIREL-RDELgltSVVVTHDLDSAFAIADRVavladgKIIAEGTP-EELLASD 233
|
.
gi 739682787 213 H 213
Cdd:COG1127 234 D 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-201 |
3.27e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ----RQdKIGYV 77
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewRR-QVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEhMTVNENIRCFKALCKAPLSNVLIDEYARQLNLNERTM--TISNLSGGTKRKVNVLIGLLSNPQILILDEPT 155
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILdkPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739682787 156 VGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-203 |
4.99e-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: 131.44 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR----KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQdkIGYV 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD--RGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENI----------------RCFKALCKAPLSNVLiDEYARQlnlnertmtisnLSGGTKRKVNVLIG 141
Cdd:cd03293 79 FQQDALLPWLTVLDNValglelqgvpkaeareRAEELLELVGLSGFE-NAYPHQ------------LSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 142 LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL--IILTTHHLDEVEALADQIKVIGNDP 203
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGktVLLVTHDIDEAVFLADRVVVLSARP 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-201 |
1.28e-37 |
|
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: 128.52 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDKIGYVPQ 79
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlplEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 dialfehmtvnenircfkalckaplsnvlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739682787 160 LKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd00267 113 PASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-201 |
3.10e-37 |
|
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: 127.94 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYVPQ 79
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEhmtvnenircfkalckaplsnvlIDEYARQlnlnertmTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:cd03214 81 ALELLG-----------------------LAHLADR--------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739682787 160 LKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03214 130 IAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKD 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-201 |
1.45e-36 |
|
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: 125.96 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGY 76
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFeHMTVNENIrcfkalckaplsnvlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03228 81 VPQDPFLF-SGTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739682787 157 GIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEaLADQIKVIGN 201
Cdd:cd03228 126 ALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-199 |
2.60e-36 |
|
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: 127.10 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKkciFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR--QD 72
Cdd:cd03265 1 IEVENLVKKYGD---FEAVR----GVSFRVrrgeifgLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRevRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 KIGYVPQDIALFEHMTVNENIRCFKALCKAPLSNVL--IDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRerIDELLDFVGLLEaADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAII 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-203 |
4.15e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.51 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC----IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRqdKIGY 76
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP--DRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRcF--------KALCKAplsnvLIDEYARQLNLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:COG1116 85 VFQEPALLPWLTVLDNVA-LglelrgvpKAERRE-----RARELLELVGLAGFEDAyPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 148 ILILDEPTVGIDLKSRFDIHN-LLNTMKRERL-IILTTHHLDEVEALADQIKVIGNDP 203
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDeLLRLWQETGKtVLFVTHDVDEAVFLADRVVVLSARP 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-196 |
7.49e-36 |
|
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: 126.70 E-value: 7.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQDKIGYV 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaSLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIrcfkALCKAPLSNVL----------IDEYARQLNLNE-RTMTISNLSGGTKRKvnVLIG--LLS 144
Cdd:COG1120 81 PQEPPAPFGLTVRELV----ALGRYPHLGLFgrpsaedreaVEEALERTGLEHlADRPVDELSGGERQR--VLIAraLAQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQI 196
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYADRL 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-199 |
8.95e-36 |
|
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: 125.56 E-value: 8.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC----IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK--I 74
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARrrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIRCFKAL--CKAPLSNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILIL 151
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLygLKGDELTARLEELADRLGMEElLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 152 DEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-199 |
3.15e-35 |
|
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: 124.54 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK----- 67
Cdd:cd03257 1 LLEVKNLSVSFPtGGGSVKALD----DVSFSIkkgetlgLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 68 -KQRQDKIGYVPQDI--ALFEHMTV----NENIRCFKALCKAPLSNVLIDEYARQLNLNERTMT--ISNLSGGTKRKVNV 138
Cdd:cd03257 77 rKIRRKEIQMVFQDPmsSLNPRMTIgeqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNryPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 139 LIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVM 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-211 |
3.77e-35 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 127.52 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 30 TVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL--SKK-------QRQdkIGYVPQDIALFEHMTVNENIRCFKALC 100
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARgiflpphRRR--IGYVFQEARLFPHLSVRGNLLYGRKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 101 KAPLSNVLIDEYARQLNLN---ERtmTISNLSGGTKRKvnVLIG--LLSNPQILILDEPTVGIDLKSRFDIHNLLntmkr 175
Cdd:COG4148 106 PRAERRISFDEVVELLGIGhllDR--RPATLSGGERQR--VAIGraLLSSPRLLLMDEPLAALDLARKAEILPYL----- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 176 ERL-------IILTTHHLDEVEALADQI------KVIGNDPFyRELLED 211
Cdd:COG4148 177 ERLrdeldipILYVSHSLDEVARLADHVvlleqgRVVASGPL-AEVLSR 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-156 |
5.38e-35 |
|
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: 121.60 E-value: 5.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 17 FESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYVPQDIALFEHMTVNENI 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 94 RcFKALCKAPL---SNVLIDEYARQLNLNER-----TMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:pfam00005 81 R-LGLLLKGLSkreKDARAEEALEKLGLGDLadrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-199 |
9.70e-35 |
|
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: 128.87 E-value: 9.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHY--RKKCIFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ 71
Cdd:COG1123 260 LLEVRNLSKRYpvRGKGGVRAVD----DVSLTLrrgetlgLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 D------KIGYVPQD--IALFEHMTVNENI----RCFKALCKAPLSNvLIDEYARQLNLNERTMT--ISNLSGGTKRKVN 137
Cdd:COG1123 336 SlrelrrRVQMVFQDpySSLNPRMTVGDIIaeplRLHGLLSRAERRE-RVAELLERVGLPPDLADryPHELSGGQRQRVA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 138 VLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER----LIIltTHHLDEVEALADQIKVI 199
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltyLFI--SHDLAVVRYIADRVAVM 478
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-199 |
1.52e-34 |
|
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: 122.40 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 6 NLSKHYRKKCIFESLDMTFE-NLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL--SKKQ-----RQDKIGYV 77
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKinlppQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRCFKALCKAPLSNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739682787 157 GIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVM 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-199 |
2.09e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRqdKIGYV 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtDLPPKDR--NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIrcfkA----LCKAPLSNV--LIDEYARQLNLNE---RtmTISNLSGGTKRKVNvlIG--LLSNP 146
Cdd:COG3839 81 FQSYALYPHMTVYENI----AfplkLRKVPKAEIdrRVREAAELLGLEDlldR--KPKQLSGGQRQRVA--LGraLVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 147 QILILDEPTVGIDLKSR-------FDIHNLLN-TMkrerliILTTHhlDEVEA--LADQIKVI 199
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRvemraeiKRLHRRLGtTT------IYVTH--DQVEAmtLADRIAVM 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-199 |
2.90e-34 |
|
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: 121.23 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQdKIGYVPQDI 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-RIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 ALFEHMTVNENIRCFKALCKAPLSNVL--IDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGI 158
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARrrIDEWLERLELSEyANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739682787 159 DLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:cd03269 160 DPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLL 201
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
3.06e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.83 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK---QRQdkIGYV 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRN--VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRcF--------KALCKAPLSNVL----IDEYARQLnlnertmtISNLSGGTKRKV---NVLIgl 142
Cdd:COG3842 83 FQDYALFPHLTVAENVA-FglrmrgvpKAEIRARVAELLelvgLEGLADRY--------PHQLSGGQQQRValaRALA-- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 143 lSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQI 196
Cdd:COG3842 152 -PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGItfIYVTHDQEEALALADRI 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-201 |
3.66e-34 |
|
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: 122.22 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHY----RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---K 73
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 IGYVPQDI--ALFEHMTVNENIRCFKALCKAPLSNVLIDEYARQLNLNE--RTMTISNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPsfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVIGN 201
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLREERGLtyLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-196 |
2.31e-33 |
|
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: 119.13 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKC----IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQ----R 70
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisKLSEKElaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 QDKIGYVPQDIALFEHMTVNENIRCfkALCKAPLSNVLIDEYARQL----NLNER-TMTISNLSGGTKRKVNVLIGLLSN 145
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVEL--PLLLAGVPKKERRERAEELlervGLGDRlNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHlDEVEALADQI 196
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHD-PELAEYADRI 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-199 |
2.71e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 122.25 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR--QDKIGYVPQ 79
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARlaRARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRCFKALCK-------APLSNVLidEYARqlnLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQILIL 151
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGmstreieAVIPSLL--EFAR---LESKADArVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 152 DEPTVGIDLKSRFDI-HNLLNTMKRERLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13536 197 DEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-196 |
3.12e-33 |
|
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: 126.10 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRkkcifESLDMTFENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQ 71
Cdd:COG2274 474 IELENVSFRYP-----GDSPPVLDNISLTIkpgervaIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 DKIGYVPQDIALFeHMTVNENIRCFKAlcKAPLSNVL-------IDEYARQL------NLNERTmtiSNLSGGTKRKvnV 138
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENITLGDP--DATDEEIIeaarlagLHDFIEALpmgydtVVGEGG---SNLSGGQRQR--L 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 139 LI--GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVeALADQI 196
Cdd:COG2274 621 AIarALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI-RLADRI 679
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-201 |
5.60e-33 |
|
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: 124.49 E-value: 5.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY-RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQDKIGYV 77
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFeHMTVNENIRCFK------ALCKApLSNVLIDEYARQLN------LNERTmtiSNLSGGTKRKVNVLIGLLSN 145
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLGRpdasdeELEAA-LEAAGLDEFVAALPdgldtpLGEGG---RGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVeALADQIKVIGN 201
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDD 546
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-196 |
7.53e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 7.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKK----CIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQ---- 69
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisSLSERElarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIGYVPQDIALFEHMTVNENIRCFKALCKAPLS--NVLIDEYARQLNLNER-TMTISNLSGGTKRKVNVLIGLLSNP 146
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKerRERARELLERVGLGDRlDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 147 QILILDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLdEVEALADQI 196
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDP-ELAARADRV 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-201 |
8.85e-33 |
|
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: 117.74 E-value: 8.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK-IGYVPQD 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIRCFKALCKAPLSNvlIDEYARQLnlnERTMTISN--------LSGGTKRKVNVLIGLLSNPQILILD 152
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDE--IDERVREV---AELLQIEHlldrkpkqLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 153 EPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-199 |
1.09e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.64 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE----QLSKKQRqdKIGYV 77
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRER--RVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIrCFkALCKAPLSNVLIDEYARQL-------NLNERtmTISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:COG1118 81 FQHYALFPHMTVAENI-AF-GLRVRPPSKAEIRARVEELlelvqleGLADR--YPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLntmkRERL------IILTTHHLDEVEALADQIKVI 199
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWL----RRLHdelggtTVFVTHDQEEALELADRVVVM 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-201 |
1.16e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.91 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ--DKIGYVPQ 79
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHarQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRCF-------KALCKAPLSNVLidEYARQLNLNErtMTISNLSGGTKRKVNVLIGLLSNPQILILD 152
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFgryfglsAAAARALVPPLL--EFAKLENKAD--AKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739682787 153 EPTVGIDLKSRFDI-HNLLNTMKRERLIILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK13537 164 EPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-194 |
6.58e-32 |
|
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: 115.61 E-value: 6.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGYV 77
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIR-----CFKALCKAPLSNVL-----IDEYARQLNlnertmtiSNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:cd03224 81 PEGRRIFPELTVEENLLlgayaRRRAKRKARLERVYelfprLKERRKQLA--------GTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALAD 194
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIAD 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-201 |
1.03e-31 |
|
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: 115.86 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK-KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQDKIGYV 77
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdirEQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRCFKALCKAPLSNvlIDEYARQL----NLNERTMT---ISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEK--IRERADELlalvGLDPAEFAdryPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-201 |
1.20e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.75 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRqDKIGYVPQD 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-RRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIRCFKALCKAPLSNVL--IDEYARQLNLNER-TMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVG 157
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKrrADEWLERLGLGDRaNKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739682787 158 ID------LKsrfDIhnLLNTMKRERLIILTTHHLDEVEALADQIKVIGN 201
Cdd:COG4152 160 LDpvnvelLK---DV--IRELAAKGTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-199 |
1.64e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.74 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL---SKKQRQDK-IGYVPQDIALFEHMTVNENIrcfkALCKAPLSNV 107
Cdd:COG1129 35 LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAgIAIIHQELNLVPNLSVAENI----FLGREPRRGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 108 LID---------EYARQLNLNER-TMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKsrfDIHNLLNTMKreR 177
Cdd:COG1129 111 LIDwramrrrarELLARLGLDIDpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER---EVERLFRIIR--R 185
|
170 180
....*....|....*....|....*...
gi 739682787 178 L------IILTTHHLDEVEALADQIKVI 199
Cdd:COG1129 186 LkaqgvaIIYISHRLDEVFEIADRVTVL 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-199 |
5.30e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.59 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKkciFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS----KKQ 69
Cdd:COG3845 5 ALELRGITKRFGG---VVAND----DVSLTVrpgeihaLLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIGYVPQDIALFEHMTVNENIrcfkALCKAPLSNVLID---------EYARQLNLN---ERtmTISNLSGGTKRKVN 137
Cdd:COG3845 78 IALGIGMVHQHFMLVPNLTVAENI----VLGLEPTKGGRLDrkaararirELSERYGLDvdpDA--KVEDLSVGEQQRVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 138 VLIGLLSNPQILILDEPTVGI------DLksrFDIhnlLNTMKRERL-IILTTHHLDEVEALADQIKVI 199
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLtpqeadEL---FEI---LRRLAAEGKsIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-199 |
6.43e-31 |
|
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: 113.59 E-value: 6.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK-IGYVPQD 80
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENI-----------RCFKALCKAPLSNVL----IDEYARQLNlnertmtiSNLSGGTKRKVNVLIGLLSN 145
Cdd:cd03296 83 YALFRHMTVFDNVafglrvkprseRPPEAEIRAKVHELLklvqLDWLADRYP--------AQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHhlDEVEAL--ADQIKVI 199
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVttVFVTH--DQEEALevADRVVVM 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-184 |
6.73e-31 |
|
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: 113.13 E-value: 6.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQ---LTKGEIRYFGEQLSKKQRQDKIGYVPQDIALFEHMTVNEN 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 93 IRcFKALCKAP-------LSNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRF 164
Cdd:cd03234 102 LT-YTAILRLPrkssdaiRKKRVEDVLLRDLALTRiGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180
....*....|....*....|.
gi 739682787 165 D-IHNLLNTMKRERLIILTTH 184
Cdd:cd03234 181 NlVSTLSQLARRNRIVILTIH 201
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-199 |
7.25e-31 |
|
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: 113.02 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK----KQRQDKIGYV 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRCfkALCKAPLSNVLIDEYARQLnLNE------RTMTISNLSGGTKRKVNVLIGLLSNPQILIL 151
Cdd:cd03218 81 PQEASIFRKLTVEENILA--VLEIRGLSKKEREEKLEEL-LEEfhithlRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 152 DEPTVGIDLKSRFDIHNLLNTMKRERLIILTT-HHLDEVEALADQIKVI 199
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYII 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-201 |
9.14e-31 |
|
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: 112.31 E-value: 9.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-KQRQDKIGYVPQD 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIRCFKALCKAPLSNvlIDEYARQLNL-NERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKR--IDEVLDVVGLkDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739682787 160 LKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03268 159 PDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINK 201
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-199 |
1.04e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 115.59 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 20 LDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---------QLSKKQRqdKIGYVPQDIALFEHMTVN 90
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiFLPPEKR--RIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 91 ENIRCFKALCKAPLSNVLIDEYARQLNLN---ERTmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIH 167
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERVIELLGIGhllGRL--PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|....
gi 739682787 168 NLLNTMKRERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:TIGR02142 172 PYLERLHAEFGIpiLYVSHSLQEVLRLADRVVVL 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-201 |
2.26e-30 |
|
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: 110.72 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGL--EQLTKGEIRYFGEQLSKKQRQDKIGYVPQDIALFEHMTVNENIRcFKALCKapls 105
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLM-FAAKLR---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 106 nvlideyarqlnlnertmtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDlksRFDIHNLLNTMKRE----RLIIL 181
Cdd:cd03213 111 ---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD---SSSALQVMSLLRRLadtgRTIIC 166
|
170 180
....*....|....*....|.
gi 739682787 182 TTHHL-DEVEALADQIKVIGN 201
Cdd:cd03213 167 SIHQPsSEIFELFDKLLLLSQ 187
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-202 |
3.13e-30 |
|
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: 110.81 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLS-KHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIGYVPQDI 81
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 --ALFEHmTVNENIRcfKALCKAPLSNVLIDEYARQLNLN---ERTMTIsnLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03226 81 dyQLFTD-SVREELL--LGLKELDAGNEQAETVLKDLDLYalkERHPLS--LSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739682787 157 GIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGND 202
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
7.47e-30 |
|
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: 115.63 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGY 76
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFeHMTVNENIRCFK------ALCKApLSNVLIDEYARQLN--LNerTMTI---SNLSGGTKRKVNVLIGLLSN 145
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLARpdatdeELWAA-LERVGLGDWLAALPdgLD--TWLGeggRRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVIGNDPF-----YRELLEDKHWPFEVYN 220
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIveqgtHEELLAQNGRYRQLYQ 568
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-192 |
7.93e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD------K 73
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 IGYVPQDIALFEHMTVNENIRcF--------KALCKAPLSNVLideyaRQLNLNER-TMTISNLSGGTKRKVNVLIGLLS 144
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVA-LplrvtgksRKEIRRRVREVL-----DLVGLSDKaKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEAL 192
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTtVLIATHDLELVDRM 203
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-196 |
1.16e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 111.72 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGY 76
Cdd:COG1125 1 MIEFENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrrRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRCFKALCKAPLSNvlIDEYARQL----NLNERTMT---ISNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKER--IRARVDELlelvGLDPEEYRdryPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQI 196
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLQRElgKTIVFVTHDIDEALKLGDRI 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-201 |
1.86e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.48 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD-KIGYVPQD 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENI-----------RCFKALCKAPLSNVLidEYARQLNLNERTMtiSNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:PRK10851 83 YALFRHMTVFDNIafgltvlprreRPNAAAIKAKVTQLL--EMVQLAHLADRYP--AQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFtsVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-205 |
2.00e-29 |
|
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: 115.50 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 4 LKNLSKHYRK--KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ---RQdKIGYVP 78
Cdd:TIGR01257 931 VKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLdavRQ-SLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENIrcfkaLCKAPLSNVLIDEYARQLNL--------NERTMTISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:TIGR01257 1010 QHNILFHHLTVAEHI-----LFYAQLKGRSWEEAQLEMEAmledtglhHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQIKVIGNDPFY 205
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-196 |
3.41e-29 |
|
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: 109.19 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY-RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD------KI 74
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIRC---------------F----KALCKAPLSNVLIDEYARQlnlneRTmtiSNLSGGTKRK 135
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSgrlgrrstwrslfglFpkeeKQRALAALERVGLLDKAYQ-----RA---DQLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 136 VNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLL--NTMKRERLIILTTHHLDEVEALADQI 196
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREYADRI 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-198 |
6.43e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.19 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQdkIGYVP 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRH--VNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENI----RCFK-------ALCKAPLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:PRK09452 93 QSYALFPHMTVFENVafglRMQKtpaaeitPRVMEALRMVQLEEFAQR--------KPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHhlDEVEALA--DQIKV 198
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGItfVFVTH--DQEEALTmsDRIVV 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-199 |
1.07e-28 |
|
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: 107.67 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQ 69
Cdd:cd03258 1 MIELKNVSKVFGdTGGKVTALK----DVSLSVpkgeifgIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQD---KIGYVPQDIALFEHMTVNENIrcfkALckaPL-----SNVLIDEYARQL----NLNER-TMTISNLSGGTKRKV 136
Cdd:cd03258 77 LRKarrRIGMIFQHFNLLSSRTVFENV----AL---PLeiagvPKAEIEERVLELlelvGLEDKaDAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 137 NVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVM 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-201 |
1.59e-28 |
|
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: 107.04 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKkciFESLDMTFE--NLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQdkIGY 76
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEveRGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRD--ISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRCFKALCKAPLSNV--LIDEYARQLN----LNERTMTisnLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIerKVLEIAEMLGidhlLNRKPET---LSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLN 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-199 |
2.22e-28 |
|
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: 105.21 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 19 SLDMTFENLQLTVLLGE-------NGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS----KKQRQDKIGYVPQD---IALF 84
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEivgiaglVGNGQTELAEALFGLRPPASGEITLDGKPVTrrspRDAIRAGIAYVPEDrkrEGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 85 EHMTVNENIrcfkalckaplsnvlideyarqlnlnertmTISN-LSGGTKRKVnvLIG--LLSNPQILILDEPTVGIDLK 161
Cdd:cd03215 91 LDLSVAENI------------------------------ALSSlLSGGNQQKV--VLArwLARDPRVLILDEPTRGVDVG 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 739682787 162 SRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVI 199
Cdd:cd03215 139 AKAEIYRLIRELADAGKaVLLISSELDELLGLCDRILVM 177
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-189 |
2.64e-28 |
|
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: 107.09 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLE-QLTKGEIRYFGEQLSK------KQRqdk 73
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGedvwelRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 IGYVPQDIalfeHMTVNENIRCFKALCKAPLSNV------------LIDEYARQLNLNE-RTMTISNLSGGTKRKVnvLI 140
Cdd:COG1119 80 IGLVSPAL----QLRFPRDETVLDVVLSGFFDSIglyreptdeqreRARELLELLGLAHlADRPFGTLSQGEQRRV--LI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 141 G--LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL--IILTTHHLDEV 189
Cdd:COG1119 154 AraLVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEEI 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-198 |
3.06e-28 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 106.55 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQdkIGYVP 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditNLPPHKRP--VNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENIrCF----KALCKAPLsNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDE 153
Cdd:cd03300 79 QNYALFPHLTVFENI-AFglrlKKLPKAEI-KERVAEALDLVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739682787 154 PTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKV 198
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGItfVFVTHDQEEALTMSDRIAV 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-199 |
3.60e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 37 GAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD----KIGYVPQD---IALFEHMTVNENIR--CFKALCKAPLSN- 106
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairaGIAYVPEDrkgEGLVLDLSIRENITlaSLDRLSRGGLLDr 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 107 ----VLIDEYARQLNLneRT----MTISNLSGGTKRKVnvLIG--LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE 176
Cdd:COG1129 368 rrerALAEEYIKRLRI--KTpspeQPVGNLSGGNQQKV--VLAkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE 443
|
170 180
....*....|....*....|....
gi 739682787 177 RL-IILTTHHLDEVEALADQIKVI 199
Cdd:COG1129 444 GKaVIVISSELPELLGLSDRILVM 467
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-198 |
1.04e-27 |
|
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: 105.21 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGYV 77
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRC------------FKALCKAPLSNVLIDEYARQLNL-NERTMTISNLSGGTKRKVNVLIGLLS 144
Cdd:cd03219 81 FQIPRLFPELTVLENVMVaaqartgsglllARARREEREARERAEELLERVGLaDLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKV 198
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-199 |
8.56e-27 |
|
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: 100.58 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD----KIGYV 77
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarraGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQdialfehmtvnenircfkalckaplsnvlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVG 157
Cdd:cd03216 81 YQ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739682787 158 IDLKsrfDIHNLLNTMKRER----LIILTTHHLDEVEALADQIKVI 199
Cdd:cd03216 113 LTPA---EVERLFKVIRRLRaqgvAVIFISHRLDEVFEIADRVTVL 155
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
2.46e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.64 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK---QRQDK-IGY 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRCFkaLCKAPLSNVLIDEYARQLnLNE-------RTMTISnLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAV--LELRKLSKKEREERLEEL-LEEfgithlrKSKAYS-LSGGERRRVEIARALATNPKFI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHH 185
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-200 |
3.91e-26 |
|
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: 100.87 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK-----------KCIF----------ESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRY 60
Cdd:cd03267 1 IEVSNLSKSYRVyskepgligslKSLFkrkyrevealKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 61 FGEQLSKKQRQ--DKIGYV-PQDIALFEHMTVNENIRCFKALCKAPLSNVL--IDEYARQLNLNERTMT-ISNLSGGTKR 134
Cdd:cd03267 81 AGLVPWKRRKKflRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKkrLDELSELLDLEELLDTpVRQLSLGQRM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 135 KVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVIG 200
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-196 |
5.94e-26 |
|
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: 99.91 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ-----DKIGY 76
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENI-----------------RCFKALCKAPLSNVlIDEYARQlnlnertmtisnLSGGTKRKVNVL 139
Cdd:cd03262 81 VFQQFNLFPHLTVLENItlapikvkgmskaeaeeRALELLEKVGLADK-ADAYPAQ------------LSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 140 IGLLSNPQILILDEPTvgidlkSRFD---IHNLLNTMK---RERL-IILTTHHLDEVEALADQI 196
Cdd:cd03262 148 RALAMNPKVMLFDEPT------SALDpelVGEVLDVMKdlaEEGMtMVVVTHEMGFAREVADRV 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-199 |
8.20e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.80 E-value: 8.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 4 LKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIrYFGEQ----LSKKQRQdkIGYVPQ 79
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKrmndVPPAERG--VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRCFKALCKAPLSNV--LIDEYARQLNLN---ERTMtiSNLSGGTKRKVNVLIGLLSNPQILILDEP 154
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEInqRVNQVAEVLQLAhllDRKP--KALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 155 TVGID----LKSRFDIHNLlntMKR-ERLIILTTHhlDEVEA--LADQIKVI 199
Cdd:PRK11000 161 LSNLDaalrVQMRIEISRL---HKRlGRTMIYVTH--DQVEAmtLADKIVVL 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-199 |
8.53e-26 |
|
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: 99.59 E-value: 8.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRkkcifESLDMTFENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQ 71
Cdd:cd03245 3 IEFRNVSFSYP-----NQEIPALDNVSLTIragekvaIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 DKIGYVPQDIALFeHMTVNENI-------------RCFKALCKAPLSNVLIDEYARQLNlnERTMtisNLSGGTKRKVNV 138
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNItlgapladderilRAAELAGVTDFVNKHPNGLDLQIG--ERGR---GLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 139 LIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLdEVEALADQIKVI 199
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVM 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-196 |
1.18e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRyFGEQLskkqrqdKIGYVPQD 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV-------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALF-EHMTVNENIRcfkalckaPLSNVLIDEYARQLnL------NERTMT-ISNLSGGTKRKVNVLIGLLSNPQILILD 152
Cdd:COG0488 387 QEELdPDKTVLDELR--------DGAPGGTEQEVRGY-LgrflfsGDDAFKpVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 153 EPTVGIDLKSRfdihNLLNtmkrERL------IILTTH--HLdeVEALADQI 196
Cdd:COG0488 458 EPTNHLDIETL----EALE----EALddfpgtVLLVSHdrYF--LDRVATRI 499
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-199 |
2.07e-25 |
|
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: 103.06 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIF--ESLDMTFENLQLTVLLGENGAGKSTLLRMIAGL---EQLTKGEIRYFGE---QLSKKQRQD 72
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRdllELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 KIGYVPQDI-ALFEHMTVNENI-----------RCFKALCKAPLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLI 140
Cdd:COG1123 84 RIGMVFQDPmTQLNPVTVGDQIaealenlglsrAEARARVLELLEAVGLERRLDR--------YPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 141 GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVM 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-199 |
2.15e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.82 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK----KQRQDKIGY 76
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpaKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIrCF----KALCKAPLSNvLIDEYARQLNLNertMTISNLSGGTKRKVNVLIGLLSNPQILILD 152
Cdd:PRK15439 91 VPQEPLLFPNLSVKENI-LFglpkRQASMQKMKQ-LLAALGCQLDLD---SSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 153 EPTVGIdlkSRFDIHNLLNTMkRERL-----IILTTHHLDEVEALADQIKVI 199
Cdd:PRK15439 166 EPTASL---TPAETERLFSRI-RELLaqgvgIVFISHKLPEIRQLADRISVM 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-201 |
2.18e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.93 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTF--------------ENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIR 59
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKGALkglfrreyreveavDDISFTIepgeivgFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 60 YFGEQLSKKQRQ--DKIGYV-PQDIALFEHMTVNENIRCFKALCKAPLS--NVLIDEYARQLNLNE------RtmtisNL 128
Cdd:COG4586 81 VLGYVPFKRRKEfaRRIGVVfGQRSQLWWDLPAIDSFRLLKAIYRIPDAeyKKRLDELVELLDLGElldtpvR-----QL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 129 SGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVIGN 201
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
5.43e-25 |
|
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: 97.64 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTK-----GEIRYFGEQLSKKQRQD---- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 -KIGYVPQDIALFeHMTVNENIR------------CFKALCKAPLSNV-LIDEYARQLNLNErtmtisnLSGGTKRKVNV 138
Cdd:cd03260 81 rRVGMVFQKPNPF-PGSIYDNVAyglrlhgiklkeELDERVEEALRKAaLWDEVKDRLHALG-------LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 139 LIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQIKVigndpFYR-ELLED 211
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAF-----LLNgRLVEF 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-199 |
7.40e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 98.19 E-value: 7.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK---QRQDK-IGY 76
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLpphRIARLgIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRC----------FKALCKAPLS-------NVLIDEYARQLNLNERTMTI-SNLSGGTKRKVNV 138
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVaaharlgrglLAALLRLPRArreereaRERAEELLERVGLADRADEPaGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 139 LIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL--IILTTHHLDEVEALADQIKVI 199
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitILLIEHDMDLVMGLADRIVVL 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-155 |
8.76e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 8.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 4 LKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRyfgeqlskKQRQDKIGYVPQDIAL 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------IPKGLRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 84 FEHMTVNENI------------RCFKALCKAPLSNVLIDEYAR----------------------QLNLNERTMT--ISN 127
Cdd:COG0488 73 DDDLTVLDTVldgdaelraleaELEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsGLGFPEEDLDrpVSE 152
|
170 180
....*....|....*....|....*...
gi 739682787 128 LSGGTKRKVNVLIGLLSNPQILILDEPT 155
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-201 |
9.34e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 97.36 E-value: 9.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGY 76
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIR--CFKALCKAPLSNVLIDEYARQLNLNERTMTI-SNLSGGTKRKvnVLIG--LLSNPQILIL 151
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLlgAYARRDRAEVRADLERVYELFPRLKERRRQRaGTLSGGEQQM--LAIGraLMSRPKLLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 152 DEPTVG-----IDlksrfDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVIGN 201
Cdd:COG0410 161 DEPSLGlapliVE-----EIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLER 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-210 |
1.06e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK-KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYV 77
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFeHMTVNENIRCFK----------ALCKAplsnvLIDEYARQL------NLNERTmtiSNLSGGTK------Rk 135
Cdd:COG1132 420 PQDTFLF-SGTIRENIRYGRpdatdeeveeAAKAA-----QAHEFIEALpdgydtVVGERG---VNLSGGQRqriaiaR- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 136 vnvliGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQI------KVIG--------- 200
Cdd:COG1132 490 -----ALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRIlvlddgRIVEqgtheella 563
|
250
....*....|
gi 739682787 201 NDPFYRELLE 210
Cdd:COG1132 564 RGGLYARLYR 573
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-199 |
2.38e-24 |
|
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: 94.59 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGY 76
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIrcfkalckaplsnvlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03246 81 LPQDDELFSG-SIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739682787 157 GIDLKSRFDIHNLLNTMK-RERLIILTTHHLdEVEALADQIKVI 199
Cdd:cd03246 126 HLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVL 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-199 |
3.46e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.59 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKkciFE-SLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK---QRqdKIGY 76
Cdd:COG3840 1 MLRLDDLTYRYGD---FPlRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaER--PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIrcfkALCKAP---LSNV---LIDEYARQLNLNE---RTMtiSNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:COG3840 76 LFQENNLFPHLTVAQNI----GLGLRPglkLTAEqraQVEQALERVGLAGlldRLP--GQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLV 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
4.12e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGleQL-----TKGEIRYFGEQLSKKQ-RQDKI 74
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--TLspafsASGEVLLNGRRLTALPaEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIrCF-----------KALCKAPLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLIGLL 143
Cdd:COG4136 79 GILFQDDLLFPHLSVGENL-AFalpptigraqrRARVEQALEEAGLAGFADR--------DPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 144 SNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEAlADQIKVIGN 201
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAPA-AGRVLDLGN 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-199 |
1.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESL-----DMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRyFGEQL---SKKQRQ-- 71
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVitaGKKNKKlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 ---DKIGYVPQ--DIALFEHmTVNENIrCF----------KALCKAplsnvliDEYARQLNLNERTMTIS--NLSGGTKR 134
Cdd:PRK13634 82 plrKKVGIVFQfpEHQLFEE-TVEKDI-CFgpmnfgvseeDAKQKA-------REMIELVGLPEELLARSpfELSGGQMR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 135 KVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVM 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-199 |
4.90e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 94.76 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQ 69
Cdd:COG1135 1 MIELENLSKTFPtKGGPVTALD----DVSLTIekgeifgIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 ----RQdKIGYVPQDIALFEHMTVNENIrcfkALckaPL-----SNVLIDEYARQL----NLNER-TMTISNLSGGTKRK 135
Cdd:COG1135 77 lraaRR-KIGMIFQHFNLLSSRTVAENV----AL---PLeiagvPKAEIRKRVAELlelvGLSDKaDAYPSQLSGGQKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 136 VNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLntmKR--ERL---IILTTHHLDEVEALADQIKVI 199
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLL---KDinRELgltIVLITHEMDVVRRICDRVAVL 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-204 |
7.57e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.90 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-KQRQDKIGYVPQ 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENI-------RCFKALCKAP----LSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLIGLLSNPQI 148
Cdd:PRK11607 99 SYALFPHMTVEQNIafglkqdKLPKAEIASRvnemLGLVHMQEFAKR--------KPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 149 LILDEPTVGIDLKSRFDI-HNLLNTMKRERLI-ILTTHHLDEVEALADQIKVIGNDPF 204
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMqLEVVDILERVGVTcVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-201 |
8.31e-23 |
|
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: 91.79 E-value: 8.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 20 LDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK-IGYVPQDIALFEHMTVNENIrcfkA 98
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpVSMLFQENNLFAHLTVEQNV----G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 99 LCKAP---LSNV---LIDEYARQLNLNERTMTISN-LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLN 171
Cdd:cd03298 93 LGLSPglkLTAEdrqAIEVALARVGLAGLEKRLPGeLSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|..
gi 739682787 172 TMKRER--LIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03298 173 DLHAETkmTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
1.07e-22 |
|
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: 95.43 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR-KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL---SKKQRQDKIGYV 77
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHmTVNENIRcfkaLCKAPLSNVLIDEYARQLNLNERTMTI------------SNLSGGTKRKVNVLIGLLSN 145
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIR----LARPDASDAEIREALERAGLDEFVAALpqgldtpigeggAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLdEVEALADQIKVI 199
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-192 |
1.39e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.88 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ--RQDKIGYVPQDIALFEHMTVNENI 93
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdePHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 RCFKALCKAPLSNvlIDEYARQLNLNERTMTISN-LSGGTKRKVNVLIGLLSNPQILILDEPTVGID------LKSRFDI 166
Cdd:TIGR01189 95 HFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvalLAGLLRA 172
|
170 180
....*....|....*....|....*....
gi 739682787 167 HnllntMKRERLIILTTHH---LDEVEAL 192
Cdd:TIGR01189 173 H-----LARGGIVLLTTHQdlgLVEAREL 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-194 |
1.86e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 20 LDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRyfgeqlskKQRQDKIGYVPQDIALFEHM--TVNENI---- 93
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGGARVAYVPQRSEVPDSLplTVRDLVamgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 -----------RCFKALCKAPLSNVLIDEYA-RQLnlnertmtiSNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLK 161
Cdd:NF040873 83 warrglwrrltRDDRAAVDDALERVGLADLAgRQL---------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....
gi 739682787 162 SRFDIHNLLNTMKRE-RLIILTTHHLDEVeALAD 194
Cdd:NF040873 154 SRERIIALLAEEHARgATVVVVTHDLELV-RRAD 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-201 |
2.17e-22 |
|
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: 91.06 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKK---CIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQDKIG 75
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALFEhMTVNENIRcfkaLCKAPLSNVLIDEYARQLNLNERTMTISN------------LSGGTKRKVNVLIGLL 143
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIR----YGKPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsqLSGGQKQRIAIARALL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 144 SNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVIGN 201
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQN 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-201 |
4.73e-22 |
|
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: 88.91 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS--KKQRQDKIGYV 77
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFehmtvNENIRCfkalckaplsnvlideyarqlNLNERtmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVG 157
Cdd:cd03247 81 NQRPYLF-----DTTLRN---------------------NLGRR------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739682787 158 IDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVIGN 201
Cdd:cd03247 129 LDPITERQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLEN 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-199 |
8.08e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.83 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQdkIGY 76
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADRD--IAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNEN------IRCF-KALCKAPlsnvlIDEYARQLNLNE------RtmtisNLSGGTKRKVNVLIGLL 143
Cdd:PRK11650 81 VFQNYALYPHMSVRENmayglkIRGMpKAEIEER-----VAEAARILELEPlldrkpR-----ELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 144 SNPQILILDEPTVGIDLKSRF-------DIHNLLNTMKrerliILTTHhlDEVEA--LADQIKVI 199
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVqmrleiqRLHRRLKTTS-----LYVTH--DQVEAmtLADRVVVM 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-174 |
1.32e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.00 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKI-----G 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALFEHMTVNENIrCFKALCKAPLSNVLIDEYARQL----NLNERTMTI-SNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:PRK09493 81 MVFQQFYLFPHLTALENV-MFGPLRVRGASKEEAEKQARELlakvGLAERAHHYpSELSGGQQQRVAIARALAVKPKLML 159
|
170 180
....*....|....*....|....
gi 739682787 151 LDEPTVGIDLKSRfdiHNLLNTMK 174
Cdd:PRK09493 160 FDEPTSALDPELR---HEVLKVMQ 180
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-201 |
2.06e-21 |
|
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: 88.44 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR-KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYV 77
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHmTVNENIRCFK-----ALCKAPLSNVLIDEYARQL------NLNERTmtiSNLSGGTKRKVNVLIGLLSNP 146
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRpnatdEEVIEAAKEAGAHDFIMKLpngydtVLGENG---GNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 147 QILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVIGN 201
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDD 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-184 |
2.97e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIGYV-PQ 79
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DiALFEHMTVNENIRCFKALCKAPLSNvlIDEYARQLNLNERT-MTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGI 158
Cdd:PRK13539 82 N-AMKPALTVAENLEFWAAFLGGEELD--IAAALEAVGLAPLAhLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 739682787 159 DLKSRFDIHNLLNT-MKRERLIILTTH 184
Cdd:PRK13539 159 DAAAVALFAELIRAhLAQGGIVIAATH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-204 |
6.08e-21 |
|
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: 90.84 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL--SKKQRQDKIGYVPQDIALFEHMTVNENIRCFkalckAPLSNVLI 109
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltNISDVHQNMGYCPQFDAIDDLLTGREHLYLY-----ARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 110 DEYARQLNLNERTMTIS--------NLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLII 180
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSlyadrlagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVV 2124
|
170 180
....*....|....*....|....
gi 739682787 181 LTTHHLDEVEALADQIKVIGNDPF 204
Cdd:TIGR01257 2125 LTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-199 |
6.57e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK-IGYVPQD 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENI----------------RCFKALCKAPLSNvLIDEYARQlnlnertmtisnLSGGTKRKVNVLIGLLS 144
Cdd:PRK11432 87 YALFPHMSLGENVgyglkmlgvpkeerkqRVKEALELVDLAG-FEDRYVDQ------------ISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 145 NPQILILDEPTVGIDLksrfdihNLLNTMK---RE---RLIILT---THhlDEVEALADQIKVI 199
Cdd:PRK11432 154 KPKVLLFDEPLSNLDA-------NLRRSMRekiRElqqQFNITSlyvTH--DQSEAFAVSDTVI 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-196 |
7.50e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIryfgeqlsKKQRQDKIGYVPQD 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHM--TVNENIRCFKALCKAPLSNVLidEYARQLNLNERTMtiSNLSGGTKRKVNVLIGLLSNPQILILDEPTVGI 158
Cdd:PRK09544 76 LYLDTTLplTVNRFLRLRPGTKKEDILPAL--KRVQAGHLIDAPM--QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 739682787 159 DLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQI 196
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELdcAVLMVSHDLHLVMAKTDEV 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-198 |
8.33e-21 |
|
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: 88.19 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQ---LTKGEIRYFGE---QLS 66
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKAVD----GVSFDVrrgetlgLVGESGSGKSTLARAILGLLPppgITSGEILFDGEdllKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 67 KKQ----RQDKIGYVPQD------------------IALFEHMTVNEnircFKALCKAPLSNVLIDEYARQLNL--NErt 122
Cdd:COG0444 77 EKElrkiRGREIQMIFQDpmtslnpvmtvgdqiaepLRIHGGLSKAE----ARERAIELLERVGLPDPERRLDRypHE-- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 123 mtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER-L-IILTTHHLDEVEALADQIKV 198
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLaILFITHDLGVVAEIADRVAV 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-201 |
1.03e-20 |
|
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: 86.52 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR-KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ----RQdKIGY 76
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslRR-AIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFeHMTVNENIR--CFKAlckaplSNVLIDEYARQLNLNERTMTISN------------LSGGTKRKVNVLIGL 142
Cdd:cd03253 80 VPQDTVLF-NDTIGYNIRygRPDA------TDEEVIEAAKAAQIHDKIMRFPDgydtivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 143 LSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVeALADQIKVIGN 201
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKD 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-203 |
1.13e-20 |
|
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: 86.37 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 18 ESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIgyVPQDIALFEHMTVNENI---- 93
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV--VFQNYSLLPWLTVRENIalav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 RCFKALCKAPLSNVLIDEYARQLNLNERT-MTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHN-LLN 171
Cdd:TIGR01184 80 DRVLPDLSKSERRAIVEEHIALVGLTEAAdKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEeLMQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 739682787 172 TMKRERL-IILTTHHLDEVEALADQIKVIGNDP 203
Cdd:TIGR01184 160 IWEEHRVtVLMVTHDVDEALLLSDRVVMLTNGP 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-199 |
1.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.53 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFE-----SLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR------ 70
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEhqaihDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 -QDKIGYVPQ--DIALFEHmTVNENIRCFKALCKAPLSNVLIDEYA--RQLNLNERTMTIS--NLSGGTKRKVNVLIGLL 143
Cdd:PRK13646 83 vRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRllMDLGFSRDVMSQSpfQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 144 SNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVM 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-199 |
1.33e-20 |
|
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: 85.99 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKK---CIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ---DKIG 75
Cdd:cd03248 12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylhSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALFEHmTVNENI---------RCFKALCKAPLSNVLIDEYAR--QLNLNERTmtiSNLSGGTKRKVNVLIGLLS 144
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIayglqscsfECVKEAAQKAHAHSFISELASgyDTEVGEKG---SQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVI 199
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVL 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-202 |
1.44e-20 |
|
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: 84.04 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIryfgeqlsKKQRQDKIGYVPQdi 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVKIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 alfehmtvnenircfkalckaplsnvlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLK 161
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739682787 162 SRFDIHNLLNTMKRErlIILTTHHLDEVEALADQIKVIGND 202
Cdd:cd03221 105 SIEALEEALKEYPGT--VILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-201 |
1.50e-20 |
|
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: 85.92 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCI-FESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR------QDKI 74
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIRCFKALCKAP--LSNVLIDEYARQLNLNERTMTISN-LSGGTKRKVNVLIGLLSNPQILIL 151
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPprEIRKRVPAALELVGLSHKHRALPAeLSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 152 DEPTVGIDLKSRFDIHNLLNTM-KRERLIILTTHHLDEVEALADQIKVIGN 201
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-196 |
1.81e-20 |
|
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: 86.54 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 31 VLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQ----RQDKIGYVPQDIALFEHMTVNENI---------- 93
Cdd:cd03294 54 VIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaAMSRKElrelRRKKISMVFQSFALLPHRTVLENVafglevqgvp 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 ---RCFKALcKApLSNVLIDEYARQLnlnertmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLL 170
Cdd:cd03294 134 raeREERAA-EA-LELVGLEGWEHKY--------PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180
....*....|....*....|....*...
gi 739682787 171 NTMKRE--RLIILTTHHLDEVEALADQI 196
Cdd:cd03294 204 LRLQAElqKTIVFITHDLDEALRLGDRI 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-198 |
2.63e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.52 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 37 GAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGYVPQDI---ALFEHMTVNEN--IRCFKALCKAPLS-- 105
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangIVYISEDRkrdGLVLGMSVKENmsLTALRYFSRAGGSlk 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 106 ----NVLIDEYARQLNLNERTM--TISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL- 178
Cdd:PRK10762 368 hadeQQAVSDFIRLFNIKTPSMeqAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLs 447
|
170 180
....*....|....*....|
gi 739682787 179 IILTTHHLDEVEALADQIKV 198
Cdd:PRK10762 448 IILVSSEMPEVLGMSDRILV 467
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-185 |
2.94e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 5 KNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS----KKQRQDKIGYVPQD 80
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIRCFKALCK---APLSNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDdlsAEQREDRANELMEEFHIEHlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180
....*....|....*....|....*....
gi 739682787 157 GIDLKSRFDIHNLLNTMKRERLIILTTHH 185
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-195 |
4.50e-20 |
|
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: 84.79 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKK----CIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-------KQ 69
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedaraRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIGYVPQDIALFEHMTVNENI---------RCFKALCKAPLSNV----LIDEYARQlnlnertmtisnLSGGTKRKV 136
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVmlplelagrRDARARARALLERVglghRLDHYPAQ------------LSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 137 NVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHhlDevEALADQ 195
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTH--D--PALAAR 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-198 |
4.62e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.43 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR--KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDKIG 75
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQ-------------DIA--LfehmtvnENIRCFKALCKAplsnvLIDEYARQLNLNER-TMTISNLSGGTKRKVNVL 139
Cdd:PRK13632 87 IIFQnpdnqfigatvedDIAfgL-------ENKKVPPKKMKD-----IIDDLAKKVGMEDYlDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 140 IGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTM--KRERLIILTTHHLDEVeALADQIKV 198
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEA-ILADKVIV 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-199 |
6.30e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSkhyrkkCI------FESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLsKKQRQDK- 73
Cdd:PRK13538 1 MLEARNLA------CErderilFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-RRQRDEYh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 -----IGYVPqdiALFEHMTVNENIRCFKALcKAPLSNVLIDEYARQLNLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:PRK13538 74 qdllyLGHQP---GIKTELTALENLRFYQRL-HGPGDDEALWEALAQVGLAGFEDVpVRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 148 ILILDEPTVGID------LKSRFDIHnllntMKRERLIILTTHHldEVEALADQIKVI 199
Cdd:PRK13538 150 LWILDEPFTAIDkqgvarLEALLAQH-----AEQGGMVILTTHQ--DLPVASDKVRKL 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-197 |
1.28e-19 |
|
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: 82.93 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR--QDKIGYVPQ 79
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsiARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIALFEHMTVNENIRCFKALCkaplSNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGI 158
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADH----SDEQVEEALARVGLNGfEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739682787 159 DLKS--RFDIHnLLNTMKRERLIILTTHH-LDEVEALADQIK 197
Cdd:cd03231 157 DKAGvaRFAEA-MAGHCARGGMVVLTTHQdLGLSEAGARELD 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-185 |
1.64e-19 |
|
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: 82.29 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQ--LTKGEIRYFGEQLsKKQRQDKIGYVPQDIALFEHMTVNENIRcFKALCkapls 105
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPL-DKNFQRSTGYVEQQDVHSPNLTVREALR-FSALL----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 106 nvlideyaRQLNLNERtmtisnlsggtkRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHH 185
Cdd:cd03232 107 --------RGLSVEQR------------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-199 |
1.86e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.33 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFES--LD---MTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR-----Q 71
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKkaLDnvnIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 DKIGYVPQ--DIALFEhmtvnENIrcFKALCKAPlsnvlideyaRQLNLNE--------RTMTIS-------------NL 128
Cdd:PRK13637 83 KKVGLVFQypEYQLFE-----ETI--EKDIAFGP----------INLGLSEeeienrvkRAMNIVgldyedykdkspfEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 129 SGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVM 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-201 |
2.55e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGY 76
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQ--DIALFEhMTVNENIR---CFKALCKAPLSNvLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:PRK13652 83 VFQnpDDQIFS-PTVEQDIAfgpINLGLDEETVAH-RVSSALHMLGLEElRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-196 |
2.97e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.48 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-----KKCI--FESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRY---FGE----QLS 66
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 67 KKQ----RQDKIGYVPQ-----------DI---ALFEhMTVNENIrcfkALCKAplsnvliDEYARQLNLNERTMTIS-- 126
Cdd:COG4778 84 PREilalRRRTIGYVSQflrviprvsalDVvaePLLE-RGVDREE----ARARA-------RELLARLNLPERLWDLPpa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 127 NLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQI 196
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAVADRV 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-201 |
3.95e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR-KKCIFESLDmtfeNLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQ 69
Cdd:PRK11153 1 MIELKNISKVFPqGGRTIHALN----NVSLHIpageifgVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 ----RQdKIGYVPQDIALFEHMTVNENIrcfkALckaPL-----SNVLIDeyARQLNLNE-------RTMTISNLSGGTK 133
Cdd:PRK11153 77 lrkaRR-QIGMIFQHFNLLSSRTVFDNV----AL---PLelagtPKAEIK--ARVTELLElvglsdkADRYPAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 134 RKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRErL---IILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRE-LgltIVLITHEMDVVKRICDRVAVIDA 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-199 |
6.07e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.77 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 26 NLQL-----TVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR-------QDKIGYVPQDIALFEHMTVNENI 93
Cdd:PRK11144 18 NLTLpaqgiTAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclppeKRRIGYVFQDARLFPHYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 R--CfkalckAPLSNVLIDEYARQLN----LNERTMTisnLSGGTKRKvnVLIG--LLSNPQILILDEPTVGIDLKSRFD 165
Cdd:PRK11144 98 RygM------AKSMVAQFDKIVALLGieplLDRYPGS---LSGGEKQR--VAIGraLLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 739682787 166 IHNLLNTMKRE-RLIIL-TTHHLDEVEALADQIKVI 199
Cdd:PRK11144 167 LLPYLERLAREiNIPILyVSHSLDEILRLADRVVVL 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-201 |
1.04e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 81.78 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR---------KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---K 68
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 69 QR---QDKIGYVPQDI--ALFEHMTVNENIRcfkalckAPLSNVL-IDEYARQLNLNE--RTMTI---------SNLSGG 131
Cdd:TIGR02769 82 QRrafRRDVQLVFQDSpsAVNPRMTVRQIIG-------EPLRHLTsLDESEQKARIAEllDMVGLrsedadklpRQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739682787 132 TKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVIGN 201
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDK 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-199 |
1.56e-18 |
|
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: 80.74 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKC--IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGY 76
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFeHMTVNENIrcfkALCKAPLSNVLIDEYARQLNLNERTMTI------------SNLSGGTKRKVNVLIGLLS 144
Cdd:cd03251 81 VSQDVFLF-NDTVAENI----AYGRPGATREEVEEAARAANAHEFIMELpegydtvigergVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVI 199
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-184 |
1.59e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHY----RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-------KQ 69
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIGYVPQDIALFEHMTVNENIRcFKALCKAPLSNVLID---EYARQLNLNERTMTI-SNLSGGTKRKVNVLIGLLSN 145
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVE-LPALLRGESSRQSRNgakALLEQLGLGKRLDHLpAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTH 184
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-194 |
1.64e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 29 LTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIGYVPQ-------------DIAL---FEHMTVnen 92
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQseevdwsfpvlveDVVMmgrYGHMGW--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 93 IRCFKALCKAPLSNVLideyARQLNLNERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNT 172
Cdd:PRK15056 112 LRRAKKRDRQIVTAAL----ARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
170 180
....*....|....*....|...
gi 739682787 173 MKRE-RLIILTTHHLDEVEALAD 194
Cdd:PRK15056 188 LRDEgKTMLVSTHNLGSVTEFCD 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-214 |
2.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLT-----VLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS--------KK 68
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEegsfvALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 69 QRQdKIGYVPQ--DIALFEHmTVNENI----RCFKALCKAPLSNVLidEYARQLNLNERTMTIS--NLSGGTKRKVnVLI 140
Cdd:PRK13641 83 LRK-KVSLVFQfpEAQLFEN-TVLKDVefgpKNFGFSEDEAKEKAL--KWLKKVGLSEDLISKSpfELSGGQMRRV-AIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 141 GLLSN-PQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQI------KVIGND-PfyRELLED 211
Cdd:PRK13641 158 GVMAYePEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVlvlehgKLIKHAsP--KEIFSD 235
|
...
gi 739682787 212 KHW 214
Cdd:PRK13641 236 KEW 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-174 |
5.69e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYV 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIAL---FehmTVNENIRcfkaLCKAPLSNvlidEYARQLNLNERTMTI-----------SNLSGGTKRKVN---VLI 140
Cdd:COG4559 81 PQHSSLafpF---TVEEVVA----LGRAPHGS----SAAQDRQIVREALALvglahlagrsyQTLSGGEQQRVQlarVLA 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 739682787 141 GLLSN----PQILILDEPTvgidlkSRFDIHNLLNTMK 174
Cdd:COG4559 150 QLWEPvdggPRWLFLDEPT------SALDLAHQHAVLR 181
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
6.69e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHY----RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK--KQRqdki 74
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENI-------------RcfKALCKAPLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLIG 141
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVafglrlrgvpkaeR--RARAEELLALVGLADFARR--------RIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 142 LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKV 198
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHSVEEALFLATRLVV 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-199 |
9.88e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.95 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 4 LKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSkkQRQDKIGYVPQDIAL 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA--EAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 84 FEHMTVNENI----------RCFKALCKAPLSNVLIDEYARqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDE 153
Cdd:PRK11247 93 LPWKKVIDNVglglkgqwrdAALQALAAVGLADRANEWPAA-------------LSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739682787 154 PTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLI 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-199 |
1.13e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.40 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFES-----LDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL---SK----KQ 69
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIGYVPQ--DIALFEHmTVNENIrCF------------KALCKAPLSNVLIDEYARQLNLNErtmtisnLSGGTKRK 135
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDV-AFgpqnfgvsqeeaEALAREKLALVGISESLFEKNPFE-------LSGGQMRR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 136 VNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVI 199
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMtIVLVTHLMDDVANYADFVYVL 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-199 |
1.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFES-----LDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIG 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALF----EHMTVNENIrcFKALCKAPLSNVLIDEYARQLNLNERTM----------TISNLSGGTKRKVNVLIG 141
Cdd:PRK13643 81 PVRKKVGVVfqfpESQLFEETV--LKDVAFGPQNFGIPKEKAEKIAAEKLEMvgladefwekSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 142 LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLL 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-199 |
1.37e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGY 76
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRC----FKALCKAPL---------SNVLIDEYARQLNLNERtmtISNLSGGTKRKVNVLIGLL 143
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwremrvrAAMMLLRVGLKVDLDEK---VANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 144 SNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVM 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-159 |
1.52e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD--------- 72
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 KIGYVPQDIALFEHMTVNENircfkaLCKAP------------------LSNVLIDEYARQLNLNertmtisnLSGGTKR 134
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEN------LIEAPckvlglskeqarekamklLARLRLTDKADRFPLH--------LSGGQQQ 148
|
170 180
....*....|....*....|....*
gi 739682787 135 KVNVLIGLLSNPQILILDEPTVGID 159
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALD 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-199 |
3.05e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYR---------KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ 71
Cdd:PRK10419 3 LLNVSGLSHHYAhgglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 DK------IGYVPQDI--ALFEHMTVNENIRcfkalckAPLSNVL-IDEYARQ------LNLNERTMTISN-----LSGG 131
Cdd:PRK10419 83 QRkafrrdIQMVFQDSisAVNPRKTVREIIR-------EPLRHLLsLDKAERLarasemLRAVDLDDSVLDkrppqLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 132 TKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVM 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-201 |
3.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLskHYRKKCIFESLD---MTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ---DKIG 75
Cdd:PRK13647 5 IEVEDL--HFRYKDGTKALKglsLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDI--ALFEhMTVNENIrCF----KALCKAPLSNvLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQI 148
Cdd:PRK13647 83 LVFQDPddQVFS-STVWDDV-AFgpvnMGLDKDEVER-RVEEALKAVRMWDfRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 149 LILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-186 |
3.24e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRK-----KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK---QRQD 72
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeyKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 KIGYVPQDIAL--FEHMTVNENI-----RCFKALCKAPLSNVLIDEYARQL-----NLNER-TMTISNLSGGTKRKVNVL 139
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLalayrRGKRRGLRRGLTKKRRELFRELLatlglGLENRlDTKVGLLSGGQRQALSLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 140 IGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTM-KRERLIIL-TTHHL 186
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLmVTHNM 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-175 |
3.92e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYV 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIAL---FehmTVNENIRcfkaLCKAPLSNV------LIDEYARQLNLNE-RTMTISNLSGGTKRKVN---VLIGLLS 144
Cdd:PRK13548 82 PQHSSLsfpF---TVEEVVA----MGRAPHGLSraeddaLVAAALAQVDLAHlAGRDYPQLSGGEQQRVQlarVLAQLWE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 145 N---PQILILDEPTvgidlkSRFDI---HNLLNTMKR 175
Cdd:PRK13548 155 PdgpPRWLLLDEPT------SALDLahqHHVLRLARQ 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-195 |
4.38e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRY------FGEQLSKKQRQ--- 71
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 --DKIGYVPQDIALFEHMTVNENI-----------------RCFKALCKAPLSNVLiDEYARQlnlnertmtisnLSGGT 132
Cdd:PRK11264 83 lrQHVGFVFQNFNLFPHRTVLENIiegpvivkgepkeeataRARELLAKVGLAGKE-TSYPRR------------LSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 133 KRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQ 195
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADR 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-211 |
6.72e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.46 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR----QDKIGY 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENIRCFKALCKAPLSNVLIDE-YARQLNLNER-TMTISNLSGGTKRKVNVLIGLLSNPQILILDEP 154
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWvYELFPRLHERrIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 155 TVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVIGNDpfyRELLED 211
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMtIFLVEQNANQALKLADRGYVLENG---HVVLED 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-199 |
7.37e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLT-----KGEIRYFGEQLSKK-----QRQ 71
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPdvdpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 DKIGYVPQDIALFEHMTVNENIRCFKALCKAPLSNVLIDEYAR------------QLNLNERTmtiSNLSGGTKRKVNVL 139
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaalwdevKDRLNDYP---SNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 140 IGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFL 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
26-186 |
9.00e-17 |
|
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: 78.17 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 26 NLQLTV-----LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQDKIGYVPQDIALFeHMTVNENIR--- 94
Cdd:TIGR02868 355 SLDLPPgervaILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvsSLDQDEVRRRVSVCAQDAHLF-DTTVRENLRlar 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 95 -------CFKALCKAPLSNvLIDEYARQLNLNERTMTISnLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIH 167
Cdd:TIGR02868 434 pdatdeeLWAALERVGLAD-WLRALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
170
....*....|....*....
gi 739682787 168 NLLNTMKRERLIILTTHHL 186
Cdd:TIGR02868 512 EDLLAALSGRTVVLITHHL 530
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-197 |
9.49e-17 |
|
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: 75.26 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLE--QLTKGEIRYFGEqlskkqrqdkigyvpq 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 DIAlfeHMTVNENIRCFKALC-KAP--LSNVLIDEYARqlNLNErtmtisNLSGGTKRKVNVLIGLLSNPQILILDEPTV 156
Cdd:cd03217 65 DIT---DLPPEERARLGIFLAfQYPpeIPGVKNADFLR--YVNE------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739682787 157 GIDLKSRFDIHNLLNTMKRE-RLIILTTHHldevEALADQIK 197
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEgKSVLIITHY----QRLLDYIK 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-199 |
1.51e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQDKIGYV 77
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpisMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENI---------------RCFKALCKAPLSNVLIDEYARQLnlnertmtISNLSGGTKRKVNVLIGL 142
Cdd:PRK11231 82 PQHHLTPEGITVRELVaygrspwlslwgrlsAEDNARVNQAMEQTRINHLADRR--------LTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 143 LSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVL 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-199 |
1.99e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 37 GAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ----RQDKIGYVPQD---IALFEHMTVNENIrCFKALCKAPLSN--V 107
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSprerRRLGVAYIPEDrlgRGLVPDMSVAENL-ILGRYRRPPFSRggF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 108 L----IDEYARQLnLNE---RT----MTISNLSGGTKRKvnVLIG--LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMK 174
Cdd:COG3845 373 LdrkaIRAFAEEL-IEEfdvRTpgpdTPARSLSGGNQQK--VILAreLSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR 449
|
170 180
....*....|....*....|....*.
gi 739682787 175 RERL-IILTTHHLDEVEALADQIKVI 199
Cdd:COG3845 450 DAGAaVLLISEDLDEILALSDRIAVM 475
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-199 |
2.53e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLT--KGEIRYFGEQLSKKQRQDK----IGYVPQDIALFEHMTVNENIrcFkaLCKAPLS 105
Cdd:PRK13549 36 LCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTeragIAIIHQELALVKELSVLENI--F--LGNEITP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 106 NVLID---------EYARQLNLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIdlkSRFDIHNLLNTMK- 174
Cdd:PRK13549 112 GGIMDydamylraqKLLAQLKLDINPATpVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL---TESETAVLLDIIRd 188
|
170 180
....*....|....*....|....*...
gi 739682787 175 -RERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:PRK13549 189 lKAHGIacIYISHKLNEVKAISDTICVI 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
31-201 |
3.05e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 76.62 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 31 VLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYVPQDIALFEHmTVNENIRCF-------KALC 100
Cdd:TIGR01842 348 AIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkHIGYLPQDVELFPG-TVAENIARFgenadpeKIIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 101 KAPLSNV--LIdeyarqLNLNERTMTI-----SNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTM 173
Cdd:TIGR01842 427 AAKLAGVheLI------LRLPDGYDTVigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL 500
|
170 180
....*....|....*....|....*...
gi 739682787 174 KRERLIILTTHHLDEVEALADQIKVIGN 201
Cdd:TIGR01842 501 KARGITVVVITHRPSLLGCVDKILVLQD 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-200 |
3.24e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 37 GAGKSTLLRMIAGLEQ-LTKGEIRYFGEQLSKKQRQD----KIGYVPQD---IALFEHMTVNENIR-------CFKALCK 101
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaiaqGIAMVPEDrkrDGIVPVMGVGKNITlaaldrfTGGSRID 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 102 APLSNVLIDEYARQLNLNERT--MTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL- 178
Cdd:PRK13549 378 DAAELKTILESIQRLKVKTASpeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVa 457
|
170 180
....*....|....*....|..
gi 739682787 179 IILTTHHLDEVEALADQIKVIG 200
Cdd:PRK13549 458 IIVISSELPEVLGLSDRVLVMH 479
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-221 |
3.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFE-----SLDMTFENLQLTVLLGENGAGKSTLLRMIAGL-----EQLTKGEIRYFGEQLSKKQRQ 71
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 D---KIGYVPQ--DIALFEHmTVNENIRCFKALCKAPLSNVL--IDEYARQLNLNERTMTIS--NLSGGTKRKVNVLIGL 142
Cdd:PRK13645 87 RlrkEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYkkVPELLKLVQLPEDYVKRSpfELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 143 LSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIgndpfYRELLEDKHWPFEVYN 220
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVM-----HEGKVISIGSPFEIFS 240
|
.
gi 739682787 221 N 221
Cdd:PRK13645 241 N 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-203 |
4.08e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS--KKQRqdkiGYVP 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAER----GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENIRCFKALCKAPLSN--VLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPT 155
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQrlEIAHQMLKKVGLEGaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739682787 156 VGIDLKSRFDIHNLLNTMKRE--RLIILTTHHLDEVEALADQIKVIGNDP 203
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSPGP 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-201 |
4.84e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 6 NLSKHY---RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQL------TKGEIRYFGE---QLSKKQRQDK 73
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKdifQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 IGYVPQDIALFEHMTVNENI------------RCFKALCKAPLSNV-LIDEYARQLNlnertMTISNLSGGTKRKVNVLI 140
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIayplkshgikekREIKKIVEECLRKVgLWKEVYDRLN-----SPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 141 GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYN 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-199 |
5.41e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 75.91 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGY 76
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrrQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIRcFKALCKAPLSNV---LIDEYARQL--NLNERTMTI-----SNLSGGTKRKVNVLIGLLSNP 146
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIA-YGRTEQADRAEIeraLAAAYAQDFvdKLPLGLDTPigengVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 147 QILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVI 199
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVM 540
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-185 |
5.78e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQLT--KGEIRYFGEQLSKkQRQDKIGYVPQDIALFEHMTVNENIrCFKALCKAPLS 105
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK-QILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 106 ------NVLIDEYARQLNLN--ERTMT----ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTM 173
Cdd:PLN03211 173 ltkqekILVAESVISELGLTkcENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170
....*....|..
gi 739682787 174 KRERLIILTTHH 185
Cdd:PLN03211 253 AQKGKTIVTSMH 264
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
6.98e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ--RQDKIGYVP 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 79 QDIALFEHMTVNENirCFKALCKAPlSNVLIDEYARQLNLNERT-MTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVG 157
Cdd:PRK13540 81 HRSGINPYLTLREN--CLYDIHFSP-GAVGITELCRLFSLEHLIdYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|
gi 739682787 158 IDLKSRFDIHNLLNTMKRERLIILTTHHLD 187
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-207 |
8.65e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.02 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFE--NLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIG 75
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNipKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQ-------------DIA--LFEHMTVNENIrcfKALCKAPLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLI 140
Cdd:PRK13648 87 IVFQnpdnqfvgsivkyDVAfgLENHAVPYDEM---HRRVSEALKQVDMLERADY--------EPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 141 GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVeALADQIKVIGNDPFYRE 207
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKE 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-200 |
9.04e-16 |
|
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: 75.25 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 37 GAGKSTLLRMIAGL-EQLTKGEIRYFGEQLSKKQRQD----KIGYVPQDI---ALFEHMTVNENIR-------CFKALCK 101
Cdd:TIGR02633 296 GAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairaGIAMVPEDRkrhGIVPILGVGKNITlsvlksfCFKMRID 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 102 APLSNVLIDEYARQLNLNERT--MTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL- 178
Cdd:TIGR02633 376 AAAELQIIGSAIQRLKVKTASpfLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVa 455
|
170 180
....*....|....*....|..
gi 739682787 179 IILTTHHLDEVEALADQIKVIG 200
Cdd:TIGR02633 456 IIVVSSELAEVLGLSDRVLVIG 477
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-201 |
9.25e-16 |
|
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: 72.91 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRkkcifESLDMTFENLQLTVLLGE-------NGAGKST----LLRMIagleQLTKGEIRYFGEQLSKKQR 70
Cdd:cd03244 3 IEFKNVSLRYR-----PNLPPVLKNISFSIKPGEkvgivgrTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 QD---KIGYVPQDIALFEHmTVNENIRCF-----KALCKApLSNVLIDEYARQLNLNERTMTI---SNLSGGTKRKVNVL 139
Cdd:cd03244 74 HDlrsRISIIPQDPVLFSG-TIRSNLDPFgeysdEELWQA-LERVGLKEFVESLPGGLDTVVEeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739682787 140 IGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVeALADQIKVIGN 201
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDK 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-201 |
1.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.57 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR-----QDKI 74
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQ--DIALFEHmTVNENIrCFKAL------------CKAPLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLI 140
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDV-AFGPLnlglskeevekrVKEALKAVGMEGFENK--------PPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739682787 141 GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVPVYADKVYVMSD 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-201 |
1.50e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEI----RYFGEQLSKKQRQDKI 74
Cdd:PTZ00265 383 IQFKNVRFHYdtRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHmTVNENIR-------------------------------CFKALCKAPLSN----------------- 106
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKyslyslkdlealsnyynedgndsqenknkrnSCRAKCAGDLNDmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 107 --------------VLIDEYARQLNLNERTMTISN---LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNL 169
Cdd:PTZ00265 542 qtikdsevvdvskkVLIHDFVSALPDKYETLVGSNaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|....
gi 739682787 170 LNTMK--RERLIILTTHHLDEVEaLADQIKVIGN 201
Cdd:PTZ00265 622 INNLKgnENRITIIIAHRLSTIR-YANTIFVLSN 654
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-162 |
1.98e-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: 74.20 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 4 LKNLSKHY-RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRyfgeqlskKQRQDKIGYVPQDIA 82
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGIKVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 83 LFEHMTVNENIRCFKALCKAPLS----------------NVLIDEYA---------------RQLnlnERTM-------- 123
Cdd:TIGR03719 79 LDPTKTVRENVEEGVAEIKDALDrfneisakyaepdadfDKLAAEQAelqeiidaadawdldSQL---EIAMdalrcppw 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739682787 124 --TISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKS 162
Cdd:TIGR03719 156 daDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-201 |
2.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.84 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESL-DMTFENLQLTVL--LGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK---QRQDKI 74
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLnDVSFHVKQGEWLsiIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQ-------------DIAL------FEHMTVNEniRCFKALCKAPLSNVLIDEYARqlnlnertmtisnLSGGTKRK 135
Cdd:PRK13650 84 GMVFQnpdnqfvgatvedDVAFglenkgIPHEEMKE--RVNEALELVGMQDFKEREPAR-------------LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 136 VNVLIGLLSNPQILILDEPTVGIDLKSRFDihnLLNTMKRER-----LIILTTHHLDEVeALADQIKVIGN 201
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLE---LIKTIKGIRddyqmTVISITHDLDEV-ALSDRVLVMKN 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-159 |
3.88e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRY------FGEQLSKKQ----RQ 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAirelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 dKIGYVPQDIALFEHMTVNENircfkaLCKAPLsNVL----------IDEYARQLNLNERTMTIS-NLSGGTKRKVNVLI 140
Cdd:PRK11124 83 -NVGMVFQQYNLWPHLTVQQN------LIEAPC-RVLglskdqalarAEKLLERLRLKPYADRFPlHLSGGQQQRVAIAR 154
|
170
....*....|....*....
gi 739682787 141 GLLSNPQILILDEPTVGID 159
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALD 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-199 |
4.22e-15 |
|
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: 73.32 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGL--EQLTKGEIRYFGEQLSKKQRQDK----I 74
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTeragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIRCFKAL---------------CKAPLSNVlideyarQLNLNERTMTISNLSGGTKRKVNVL 139
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEItlpggrmaynamylrAKNLLREL-------QLDADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 140 IGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVI 199
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVaCVYISHKLNEVKAVCDTICVI 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-195 |
5.31e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.35 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQL-----TKGEIRYFGEQLSKK-----QR 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPrtdtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 QDKIGYVPQDIALFEhMTVNENI----RCF----KALCKAPLSNVLI-----DEYARQLNLNErtmtiSNLSGGTKRKVN 137
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVvyglRLKgikdKQVLDEAVEKSLKgasiwDEVKDRLHDSA-----LGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 138 VLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQ 195
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDR 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-159 |
5.89e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.72 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQ------DKI 74
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlytvrKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENI----RCFKALCKAPL-SNVLIDEYARQLNLNERTMTiSNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVayplREHTQLPAPLLhSTVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDLI 165
|
170
....*....|
gi 739682787 150 ILDEPTVGID 159
Cdd:PRK11831 166 MFDEPFVGQD 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-199 |
6.14e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 24 FENLQLTVLLGE-------NGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDK-IGYVPQD---IALFEHMTV 89
Cdd:PRK15439 279 FRNISLEVRAGEilglagvVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstAQRLARgLVYLPEDrqsSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 90 NENIrCFKALCKAPL------SNVLIDEYARQLN--LNERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLK 161
Cdd:PRK15439 359 AWNV-CALTHNRRGFwikparENAVLERYRRALNikFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 739682787 162 SRFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVI 199
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-189 |
6.30e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQ---LSKKQRQDKIGYV 77
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHmTVNEN-IRCFKALCKAPLSNVLIDEYARqLNLNERTMT--ISNLSGGTKRKVNVLIGLLSNPQILILDEP 154
Cdd:PRK10247 87 AQTPTLFGD-TVYDNlIFPWQIRNQQPDPAIFLDDLER-FALPDTILTknIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 155 TVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEV 189
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIavLWVTHDKDEI 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-201 |
6.33e-15 |
|
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: 70.58 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGeqlskkqrqdKIGYVPQdIALFEHMTVNENIRC 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------SIAYVSQ-EPWIQNGTIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 FKALCKAPLSNVLideYARQL-----NLNERTMTI-----SNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFD 165
Cdd:cd03250 89 GKPFDEERYEKVI---KACALepdleILPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 739682787 166 I--HNLLNTMKRERLIILTTHHLDEVEAlADQIKVIGN 201
Cdd:cd03250 166 IfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-201 |
6.74e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.76 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 22 MTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-------KQRQDKIGYVPQDIALFEHMTVNENIR 94
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrEVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 95 CFKALCKAPLSNVLID--EYARQLNLNERTMTISN-LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLN 171
Cdd:PRK10070 129 FGMELAGINAEERREKalDALRQVGLENYAHSYPDeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|..
gi 739682787 172 TM--KRERLIILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK10070 209 KLqaKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-59 |
8.61e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.88 E-value: 8.61e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIR 59
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-155 |
1.07e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRyfgeqLSKKQrqdKIGYVPQDIALFEHMTVNENIRCFKALCKAPL------- 104
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEAR-----PAPGI---KVGYLPQEPQLDPEKTVRENVEEGVAEVKAALdrfneiy 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 105 ---------SNVLIDEYA---------------RQLnlnERTM----------TISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:PRK11819 110 aayaepdadFDALAAEQGelqeiidaadawdldSQL---EIAMdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
....*
gi 739682787 151 LDEPT 155
Cdd:PRK11819 187 LDEPT 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-202 |
1.24e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.06 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY---RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDKIG 75
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALFEHmTVNENI-----RCFK----ALCKAPLSNVLIDEYARQLNlNERTMTISNLSGGTKRKVNVLIGLLSNP 146
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIaygltDTPDeeimAAAKAANAHDFIMEFPNGYD-TEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 147 QILILDEPTVGIDLKSRfdiHNLLNTMKR-ERLIILTTHHLDEVEAlADQIKVIGND 202
Cdd:TIGR00958 637 RVLILDEATSALDAECE---QLLQESRSRaSRTVLLIAHRLSTVER-ADQILVLKKG 689
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-194 |
1.88e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.07 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQL-----TKGEIRYFGE-------QLSKKQ 69
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQniyerrvNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQdkIGYVPQDIALFEhMTVNENIRCFKALC----KAPLSNV---------LIDEYARQLNlnertMTISNLSGGTKRKV 136
Cdd:PRK14258 88 RQ--VSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDIvesalkdadLWDEIKHKIH-----KSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 137 NVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNT--MKRERLIILTTHHLDEVEALAD 194
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSD 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-198 |
1.98e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKI--GYV--PQD------IALfehMTVNENI-------- 93
Cdd:PRK11288 284 LFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIraGIMlcPEDrkaegiIPV---HSVADNInisarrhh 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 RCFKALCKAPLSNVLIDEYARQLNLN--ERTMTISNLSGGTKRKVnVLIGLLSNP-QILILDEPTVGIDLKSRFDIHNLL 170
Cdd:PRK11288 361 LRAGCLINNRWEAENADRFIRSLNIKtpSREQLIMNLSGGNQQKA-ILGRWLSEDmKVILLDEPTRGIDVGAKHEIYNVI 439
|
170 180
....*....|....*....|....*....
gi 739682787 171 -NTMKRERLIILTTHHLDEVEALADQIKV 198
Cdd:PRK11288 440 yELAAQGVAVLFVSSDLPEVLGVADRIVV 468
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-177 |
2.39e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 5 KNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDKIGYVPQDI 81
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyasKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 ALFEHMTVNENI------------RCFK----ALCKApLSNVLIDEYARQlnlnertmTISNLSGGTKRKVNVLIGLLSN 145
Cdd:PRK10253 91 TTPGDITVQELVargryphqplftRWRKedeeAVTKA-MQATGITHLADQ--------SVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190
....*....|....*....|....*....|..
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRER 177
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREK 193
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-184 |
2.44e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIA-----GLEQLtkGEIRYFGEQLSKKQRQDKIGYVPQDIALFEHMTVNENIRcFKALCKA 102
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAfrspkGVKGS--GSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLM-FQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 103 PLSNV------LIDEYARQLNLNERTMTI-------SNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDlksRFDIHNL 169
Cdd:TIGR00955 129 PRRVTkkekreRVDEVLQALGLRKCANTRigvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD---SFMAYSV 205
|
170
....*....|....*....
gi 739682787 170 LNTMK----RERLIILTTH 184
Cdd:TIGR00955 206 VQVLKglaqKGKTIICTIH 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-199 |
2.67e-14 |
|
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: 69.44 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR--KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS---KKQRQDKIGY 76
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIrcfkALCKAPLSNVLIDEYARQ-------LNLNERTMTI-----SNLSGGTKRKVNVLIGLLS 144
Cdd:cd03252 81 VLQENVLFNR-SIRDNI----ALADPGMSMERVIEAAKLagahdfiSELPEGYDTIvgeqgAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 145 NPQILILDEPTVGIDLKSRfdiHNLLNTMKR---ERLIILTTHHLDEVEAlADQIKVI 199
Cdd:cd03252 156 NPRILIFDEATSALDYESE---HAIMRNMHDicaGRTVIIIAHRLSTVKN-ADRIIVM 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-154 |
2.89e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 70.93 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYVPQDIALFEHmTVNENIRCF------KALCKA 102
Cdd:COG4618 363 VIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlSQWDREELGRHIGYLPQDVELFDG-TIAENIARFgdadpeKVVAAA 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 103 PLSNV--LIdeyarqLNLNERTMTI-----SNLSGGTKRkvnvLIGL----LSNPQILILDEP 154
Cdd:COG4618 442 KLAGVheMI------LRLPDGYDTRigeggARLSGGQRQ----RIGLaralYGDPRLVVLDEP 494
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-196 |
3.33e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYfgeqlSKKQrqdKIGYVPQD- 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----SENA---NIGYYAQDh 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 -------IALFEHMTVNENIRCFKALCKAPLSNVLIDEyarqlnlNERTMTISNLSGGTKRKvnVLIG--LLSNPQILIL 151
Cdd:PRK15064 392 aydfendLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQ-------DDIKKSVKVLSGGEKGR--MLFGklMMQKPNVLVM 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739682787 152 DEPTVGIDLKSrfdIHNLLNTMKR-ERLIILTTHHLDEVEALADQI 196
Cdd:PRK15064 463 DEPTNHMDMES---IESLNMALEKyEGTLIFVSHDREFVSSLATRI 505
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-187 |
3.49e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGL---EQLTKGEIRYFGEQLSKKQR------- 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 -QDKIGYVPQDIALFEHMTVNENIrCFKALCKAPLSNVLIDEYAR-QLNLNERTMT-----------ISNLSGGTKRKVN 137
Cdd:PRK09984 84 sRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPFWRTCFSWFTReQKQRALQALTrvgmvhfahqrVSTLSGGQQQRVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 138 VLIGLLSNPQILILDEPTVGIDLKS-RFDIHNLLNTMKRERL-IILTTHHLD 187
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESaRIVMDTLRDINQNDGItVVVTLHQVD 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-185 |
4.18e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 4 LKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYVPQD 80
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqplESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIrcfkALCKAPLSNVL----------IDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:PRK10575 94 LPAAEGMTVRELV----AIGRYPWHGALgrfgaadrekVEEAISLVGLKPlAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRER-LIILTTHH 185
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERgLTVIAVLH 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-199 |
4.41e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYrkkcifESLDMTFeNLQL-----TVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGE---QLSKKQRQD 72
Cdd:PRK10771 1 MLKLTDITWLY------HHLPMRF-DLTVergerVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtTTPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 KIGYvpQDIALFEHMTVNENIrcfkALCKAP-LSnvLIDEYARQLNLNERTMTISN--------LSGGTKRKVNVLIGLL 143
Cdd:PRK10771 74 SMLF--QENNLFSHLTVAQNI----GLGLNPgLK--LNAAQREKLHAIARQMGIEDllarlpgqLSGGQRQRVALARCLV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 144 SNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIIL--TTHHLDEVEALADQIKVI 199
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLlmVSHSLEDAARIAPRSLVV 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-198 |
5.30e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGYVPQDIALFEHMTVNENIrcfkALCKAPLSNV 107
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAENL----YLGQLPHKGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 108 LIDEyaRQLN------LNERTMTIS------NLSGGTKRKVNVLIGLLSNPQILILDEPTVgiDLKSRfDIHNL---LNT 172
Cdd:PRK11288 111 IVNR--RLLNyeareqLEHLGVDIDpdtplkYLSIGQRQMVEIAKALARNARVIAFDEPTS--SLSAR-EIEQLfrvIRE 185
|
170 180
....*....|....*....|....*..
gi 739682787 173 MKRE-RLIILTTHHLDEVEALADQIKV 198
Cdd:PRK11288 186 LRAEgRVILYVSHRMEEIFALCDAITV 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-199 |
6.50e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYVPQDI-ALFEHMTVNENIRCFKALCKAPLSNV 107
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrrQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 108 L--IDEYARQLNLNE-RTMTISNLSGGTKRKVnVLIGLLS-NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--IL 181
Cdd:PRK13635 118 VerVDQALRQVGMEDfLNREPHRLSGGQKQRV-AIAGVLAlQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItvLS 196
|
170
....*....|....*...
gi 739682787 182 TTHHLDEVeALADQIKVI 199
Cdd:PRK13635 197 ITHDLDEA-AQADRVIVM 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-198 |
6.90e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 6 NLSKHYRKKCIFESL--DMTFE--NLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-------KQRQDKI 74
Cdd:PRK11629 10 NLCKRYQEGSVQTDVlhNVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIRCFKALCKAPLSNvlIDEYARQL----NLNERTM-TISNLSGGTKRKVNVLIGLLSNPQIL 149
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAE--INSRALEMlaavGLEHRANhRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 150 ILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKV 198
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEM 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-196 |
9.50e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQL-----TKGEIRYFGEQLSK------KQR 70
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmdvielRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 QDKIGYVPQDI---ALFEHMTVNENI------------RCFKALCKAPLsnvlIDEYARQLNlnertMTISNLSGGTKRK 135
Cdd:PRK14247 84 VQMVFQIPNPIpnlSIFENVALGLKLnrlvkskkelqeRVRWALEKAQL----WDEVKDRLD-----APAGKLSGGQQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 136 VNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQI 196
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-153 |
1.01e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCiFE--SLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGY 76
Cdd:PRK10522 323 LELRNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrkLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNENircfkalckAPLSNVLIDEYARQLNLNERTM----TISN--LSGGTKRKVNVLIGLLSNPQILI 150
Cdd:PRK10522 402 VFTDFHLFDQLLGPEG---------KPANPALVEKWLERLKMAHKLEledgRISNlkLSKGQKKRLALLLALAEERDILL 472
|
...
gi 739682787 151 LDE 153
Cdd:PRK10522 473 LDE 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-176 |
1.03e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 8 SKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAG-LEQLTK---GEIRYFG---EQLSKKQRQDKIgYVPQD 80
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIgveGVITYDGitpEEIKKHYRGDVV-YNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIRcFKALCKAP---LSNVLIDEYARQlnLNERTMTISNL----------------SGGTKRKVNVLIG 141
Cdd:TIGR00956 147 DVHFPHLTVGETLD-FAARCKTPqnrPDGVSREEYAKH--IADVYMATYGLshtrntkvgndfvrgvSGGERKRVSIAEA 223
|
170 180 190
....*....|....*....|....*....|....*
gi 739682787 142 LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE 176
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANI 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-198 |
1.08e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLSKHYRKKCifesLDMTFENLQLTVL--LGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK----IGY 76
Cdd:PRK09700 267 EVRNVTSRDRKKV----RDISFSVCRGEILgfAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQ---DIALFEHMTVNENIRCFKALCKAPLSNV--LIDEYARQ---------LNLNERTM--TISNLSGGTKRKVNVLI 140
Cdd:PRK09700 343 ITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAmgLFHEVDEQrtaenqrelLALKCHSVnqNITELSGGNQQKVLISK 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 141 GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKV 198
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAV 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-200 |
1.09e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.90 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKcifeslDMTF--ENLQLTVLLGENGAGKSTLLRMIAGLEQLT---KGEIRYFGEQLS--KKQRQDKI 74
Cdd:cd03233 12 TTGKGRSKIPILK------DFSGvvKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKefAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIALFEHMTVNENIRcFKALCKAplsnvliDEYARqlnlnertmtisNLSGGTKRKVNVLIGLLSNPQILILDEP 154
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLD-FALRCKG-------NEFVR------------GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739682787 155 TVGIDLKSRFDIHNLLNTMKRER---LIILTTHHLDEVEALADQIKVIG 200
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLkttTFVSLYQASDEIYDLFDKVLVLY 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-195 |
1.17e-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: 69.06 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKkcIFESLDMTFENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRY-FGEQ---LSKKQ 69
Cdd:TIGR03269 279 IIKVRNVSKRYIS--VDRGVVKAVDNVSLEVkegeifgIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwvdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDK------IGYVPQDIALFEHMTVNENircfkaLCKApLSNVLIDEYARQLNL---------NERTMTI-----SNLS 129
Cdd:TIGR03269 357 PDGRgrakryIGILHQEYDLYPHRTVLDN------LTEA-IGLELPDELARMKAVitlkmvgfdEEKAEEIldkypDELS 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 130 GGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDI-HNLLNTMKR-ERLIILTTHHLDEVEALADQ 195
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEmEQTFIIVSHDMDFVLDVCDR 497
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-159 |
1.44e-13 |
|
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: 68.81 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRyFGEQLskkqrqdKIGYVPQDi 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETV-------KLAYVDQS- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 alFEHMTVNENIrcFKAlckaplsnvlIDEYARQLNLNERTMT------------------ISNLSGGTKRKVNVLIGLL 143
Cdd:TIGR03719 394 --RDALDPNKTV--WEE----------ISGGLDIIKLGKREIPsrayvgrfnfkgsdqqkkVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*.
gi 739682787 144 SNPQILILDEPTVGID 159
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD 475
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-195 |
1.46e-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: 69.06 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQL--TKGEIRY----------------FGE 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 64 Q-----------------LSKKQRQD---KIGYVPQ-DIALFEHMTVNENIrcFKALCKAPLSNV--------LIDeyar 114
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnLSDKLRRRirkRIAIMLQrTFALYGDDTVLDNV--LEALEEIGYEGKeavgravdLIE---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 115 QLNLNERTMTIS-NLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHN-LLNTMKRERLIILTTHHLDEV-EA 191
Cdd:TIGR03269 155 MVQLSHRITHIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEViED 234
|
....
gi 739682787 192 LADQ 195
Cdd:TIGR03269 235 LSDK 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-177 |
1.69e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL-SKKQRQD---KIGYV 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMaDARHRRAvcpRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIA--LFEHMTVNENI----RCF---KALCKAPlsnvlIDEYARQLNLN---ERTMtiSNLSGGTKRKVNVLIGLLSN 145
Cdd:NF033858 82 PQGLGknLYPTLSVFENLdffgRLFgqdAAERRRR-----IDELLRATGLApfaDRPA--GKLSGGMKQKLGLCCALIHD 154
|
170 180 190
....*....|....*....|....*....|..
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRER 177
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRIRAER 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-196 |
2.32e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.79 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQlTKGEIRYFGEQLSK-------KQRqdkiGYVPQDIALFEHMTVNENIRCFK-AL 99
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwsaaelaRHR----AYLSQQQSPPFAMPVFQYLALHQpAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 100 CKAPLSNVLIDEYARQLNLNER-TMTISNLSGGTKRKVNvLIGLL------SNP--QILILDEPTVGIDL--KSRFDihN 168
Cdd:COG4138 98 ASSEAVEQLLAQLAEALGLEDKlSRPLTQLSGGEWQRVR-LAAVLlqvwptINPegQLLLLDEPMNSLDVaqQAALD--R 174
|
170 180
....*....|....*....|....*....
gi 739682787 169 LLNTMKRE-RLIILTTHHLDEVEALADQI 196
Cdd:COG4138 175 LLRELCQQgITVVMSSHDLNHTLRHADRV 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-191 |
3.08e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 3 ELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLE--QLTKGEIRYFGE---QLSKKQRQDK-IGY 76
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEdilELSPDERARAgIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHMTVNE------NIRCFKALcKAPLSNVLIDEYARQLNLNERTMTIS---NLSGGTKRKVNVLIGLLSNPQ 147
Cdd:COG0396 82 AFQYPVEIPGVSVSNflrtalNARRGEEL-SAREFLKLLKEKMKELGLDEDFLDRYvneGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHH---LDEVEA 191
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPdRGILIITHYqriLDYIKP 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
3.20e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.18 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL--SKK---QRQDKI 74
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQ--DIALFEhMTVNENIRCFKALCKAPLSNVlideYARQLNLNERTmTISNL--------SGGTKRKVNVLIGLLS 144
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEV----RKRVDNALKRT-GIEHLkdkpthclSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVM 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-201 |
4.08e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL---SKKQRQDKIGY 76
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIRCFK----------ALCKAPLSNVLIDEYARQLNLNE--RTmtisnLSGGTKRKVNVLIGLLS 144
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLAApnasdealieVLQQVGLEKLLEDDKGLNAWLGEggRQ-----LSGGEQRRLGIARALLH 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALaDQIKVIGN 201
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDN 548
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-199 |
4.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR--KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGL---EQLTKGEIRYFGEQLSKK---QRQDK 73
Cdd:PRK13640 6 VEFKHVSFTYPdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKtvwDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 IGYVPQDI-ALFEHMTVNENIrCFKALCKAPLSNVLIDEYARQLN----LNERTMTISNLSGGTKRKVNVLIGLLSNPQI 148
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDV-AFGLENRAVPRPEMIKIVRDVLAdvgmLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 149 LILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEaLADQIKVI 199
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEAN-MADQVLVL 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-199 |
5.35e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYVPQDIALFEHmTVNEN 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 93 IrcfkALCKAPLSNVLIDEYARQLNLNERTMTISN------------LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDL 160
Cdd:PRK10789 409 I----ALGRPDATQQEIEHVARLASVHDDILRLPQgydtevgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739682787 161 KSRFDI-HNlLNTMKRERLIILTTHHLdevEAL--ADQIKVI 199
Cdd:PRK10789 485 RTEHQIlHN-LRQWGEGRTVIISAHRL---SALteASEILVM 522
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-199 |
5.50e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR-----QDKIG 75
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllalRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIalfEHMTVNENIRCFKALCKAPLSnVLIDEYARQ----LNLNE----RTMTISNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:PRK13638 81 TVFQDP---EQQIFYTDIDSDIAFSLRNLG-VPEAEITRRvdeaLTLVDaqhfRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEISDAVYVL 209
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-206 |
6.13e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.67 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGL---EQLTKGEIRYFGEQ---LSKKQ----RQDKIGYVPQD--IALFEHMTVNENI----RC 95
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREilnLPEKElnklRAEQISMIFQDpmTSLNPYMRVGEQLmevlML 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 FKALCKAP--------LSNVLIDEyARQlnlnERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIH 167
Cdd:PRK09473 127 HKGMSKAEafeesvrmLDAVKMPE-ARK----RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 168 NLLNTMKRE--RLIILTTHHLDEVEALADQIKVI----------GNDPFYR 206
Cdd:PRK09473 202 TLLNELKREfnTAIIMITHDLGVVAGICDKVLVMyagrtmeygnARDVFYQ 252
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-199 |
6.34e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK-KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYV 77
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQD---IA--LFEHMTVNENIRcfKALCKAPLSNVLIDEYARQLN------LNERTmtiSNLSGGTKRKVNVLIGLLSNP 146
Cdd:PRK10790 421 QQDpvvLAdtFLANVTLGRDIS--EEQVWQALETVQLAELARSLPdglytpLGEQG---NNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 147 QILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDE-VEalADQIKVI 199
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTiVE--ADTILVL 547
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-201 |
6.95e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYV 77
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 78 PQDIALFEHMTVNENIRCFKALCKAPLSNVLIDEYARQLNLNERTMT-------ISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVaqfadrpVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLAD 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-201 |
7.07e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIF---------ESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS---KK 68
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 69 QRQDKIGYVPQDIAlfehMTVNENIRCFKALcKAPLS-NVLIDEYARQLNLNERTMTIS-----------NLSGGTKRKV 136
Cdd:PRK15112 84 YRSQRIRMIFQDPS----TSLNPRQRISQIL-DFPLRlNTDLEPEQREKQIIETLRQVGllpdhasyyphMLAPGQKQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 137 NVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI--ILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-185 |
8.13e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.90 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRK-KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD------K 73
Cdd:PRK10908 1 MIRFEHVSKAYLGgRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrrQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 IGYVPQDIALFEHMTVNENIRC-----------FKALCKAPLSNVLIDEYARQLNLNertmtisnLSGGTKRKVNVLIGL 142
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIpliiagasgddIRRRVSAALDKVGLLDKAKNFPIQ--------LSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739682787 143 LSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHH 185
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-185 |
1.43e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLE--QLTKGEIRYFGEQLSKKQRQDKIG--- 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 ----YVPQDIA-----LFEHMTVNEnIRCFKAlcKAPLSNV----LIDEYARQLNLNERTMTIS---NLSGGTKRKVNVL 139
Cdd:PRK09580 81 fmafQYPVEIPgvsnqFFLQTALNA-VRSYRG--QEPLDRFdfqdLMEEKIALLKMPEDLLTRSvnvGFSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739682787 140 IGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHH 185
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHY 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-163 |
1.61e-12 |
|
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: 64.74 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 23 TFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGeqlskkqrqDKIGYVPQDIALFEHMTVNENIRC------- 95
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL---------DTVSYKPQYIKADYEGTVRDLLSSitkdfyt 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 96 ---FKALCKAPLSnvLIDEYARQLNlnertmtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSR 163
Cdd:cd03237 92 hpyFKTEIAKPLQ--IEQILDREVP---------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-199 |
1.62e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.02 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 20 LDMTFENLQLTVLLGENGAGKSTLLRMIAGLeqLT-KGEIRYFGE---QLSKKQRQDKIGYVPQDIALFeHMTVNENIrc 95
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIelrELDPESWRKHLSWVGQNPQLP-HGTLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 fkALCKAPLSNVLIDEYARQLNLNERTMTISN------------LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSR 163
Cdd:PRK11174 444 --LLGNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190
....*....|....*....|....*....|....*.
gi 739682787 164 FDIHNLLNTMKRERLIILTTHHLDEVEALaDQIKVI 199
Cdd:PRK11174 522 QLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVM 556
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-199 |
2.10e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLD---MTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQ---RQDKI 74
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDI-ALFEHMTVNENIRCFKALCKAPLSNVL--IDEYARQLN-LNERTMTISNLSGGTKRKVNVLIGLLSNPQILI 150
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIkrVDEALLAVNmLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 151 LDEPTVGIDLKSRFDIHNLLNTMK-RERLIILT-THHLDEVeALADQIKVI 199
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSiTHDLDEA-ASSDRILVM 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
2.16e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFEsLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQdKIGYVPQD 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP-YCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 IALFEHMTVNENIRCF-KALCKAPLSNVLIDEYARQLNLNERtmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:PRK13541 79 LGLKLEMTVFENLKFWsEIYNSAETLYAAIHYFKLHDLLDEK---CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170 180
....*....|....*....|....*...
gi 739682787 160 LKSRFDIHNLLNTMKRERLIILTTHHLD 187
Cdd:PRK13541 156 KENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-221 |
4.93e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 6 NLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS-------------KKQRQ- 71
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 --DKIGYVPQDIALFEHMTVNENIR----CFKALCKAP--------LSNVLIDEYARQlnlnertMTISNLSGGTKRKVN 137
Cdd:PRK10619 90 lrTRLTMVFQHFNLWSHMTVLENVMeapiQVLGLSKQEareravkyLAKVGIDERAQG-------KYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 138 VLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVIgndpfYRELLEDKHWPF 216
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFL-----HQGKIEEEGAPE 237
|
....*
gi 739682787 217 EVYNN 221
Cdd:PRK10619 238 QLFGN 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-199 |
5.27e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.43 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGL------EqltkGEIRYFGEQLSKKQRQD--KIGYV--PQDIALFEHMTVNENIrcFkaLCK 101
Cdd:NF040905 32 LCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRFKDIRDseALGIViiHQELALIPYLSIAENI--F--LGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 102 APLSNVLID---------EYARQLNLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKsrfDIHNLLN 171
Cdd:NF040905 104 ERAKRGVIDwnetnrrarELLAKVGLDESPDTlVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEE---DSAALLD 180
|
170 180 190
....*....|....*....|....*....|..
gi 739682787 172 TMK--RERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:NF040905 181 LLLelKAQGItsIIISHKLNEIRRVADSITVL 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-221 |
5.69e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 64.38 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKIGYVPQDIALFEHmTVNEN 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 93 ircfkaLCKAPLSNVLIDEYARQLNLNERTMTI---------------SNLSGGTKRKVNVLIGLLSNPQILILDEPTVG 157
Cdd:TIGR01193 568 ------LLLGAKENVSQDEIWAACEIAEIKDDIenmplgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 158 ID-LKSRFDIHNLLNTmkRERLIILTTHHLdEVEALADQIKV-----IGNDPFYRELLEDKHWPFEVYNN 221
Cdd:TIGR01193 642 LDtITEKKIVNNLLNL--QDKTIIFVAHRL-SVAKQSDKIIVldhgkIIEQGSHDELLDRNGFYASLIHN 708
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-59 |
6.30e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRK--------KCIFESLDMT-------FENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEI 58
Cdd:COG1134 4 MIEVENVSKSYRLyhepsrslKELLLRRRRTrreefwaLKDVSFEVergesvgIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
.
gi 739682787 59 R 59
Cdd:COG1134 84 E 84
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-163 |
9.00e-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: 63.65 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 17 FESLDMTFENLQLTV------------LLGENGAGKSTLLRMIAGLEQLTKGEIryfgeqlskkQRQDKIGYVPQDIALF 84
Cdd:COG1245 344 YPDLTKSYGGFSLEVeggeiregevlgIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 85 EHMTVNENIRcfKALCKAPLSNVLIDEYARQLNLnERTMT--ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKS 162
Cdd:COG1245 414 YDGTVEEFLR--SANTDDFGSSYYKTEIIKPLGL-EKLLDknVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
.
gi 739682787 163 R 163
Cdd:COG1245 491 R 491
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
1.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFE-----SLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIR----YFGEQ------- 64
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENElvalnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 65 ---LSKKQRQDK-----IGYVPQ--DIALFEHmTVNENIRCFKALCKAPLSNV--LIDEYARQLNLNERTMTIS--NLSG 130
Cdd:PRK13631 101 tnpYSKKIKNFKelrrrVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAkkLAKFYLNKMGLDDSYLERSpfGLSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 131 GTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVM 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-199 |
2.28e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLS----KKQRQDKIGYVPQDIALFEHMTVNENI---RCFKALCKAPL 104
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEAGIGIIHQELNLIPQLTIAENIflgREFVNRFGRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 105 SNVLIDEYAR---QLNLNERTMT-ISNLSGGTKRKVNVLIGLLSNPQILILDEPT---VGIDLKSRFdihNLLNTMKRE- 176
Cdd:PRK10762 115 WKKMYAEADKllaRLNLRFSSDKlVGELSIGEQQMVEIAKVLSFESKVIIMDEPTdalTDTETESLF---RVIRELKSQg 191
|
170 180
....*....|....*....|...
gi 739682787 177 RLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK10762 192 RGIVYISHRLKEIFEICDDVTVF 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
34-221 |
2.57e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 34 GENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL---SKKQRQDK---IGYVPQD--IALFEHMTVNENI----RCF----- 96
Cdd:PRK15079 54 GESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVrsdIQMIFQDplASLNPRMTIGEIIaeplRTYhpkls 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 97 ----KALCKAPLSNV-----LIDEYARQlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIH 167
Cdd:PRK15079 134 rqevKDRVKAMMLKVgllpnLINRYPHE------------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVV 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 168 NLLNTMKRER--LIILTTHHLDEVEALADQIKV--IGNDpfyRELLEDKhwpfEVYNN 221
Cdd:PRK15079 202 NLLQQLQREMglSLIFIAHDLAVVKHISDRVLVmyLGHA---VELGTYD----EVYHN 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-201 |
2.68e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 31 VLLGENGAGKSTLLRMIAGLEQLTKGE--------IRYFGEQLSKK-----QR---------QDKIGYVPQDIALFEHmt 88
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvsdewQRnntdmlspgEDDTGRTTAEIIQDEV-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 89 vNENIRCfkalckaplsnvliDEYARQLN----LNERTMtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRF 164
Cdd:PRK10938 111 -KDPARC--------------EQLAQQFGitalLDRRFK---YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 739682787 165 DIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK10938 173 QLAELLASLHQSGItLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-199 |
2.86e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKK--QRQDKIGYVP--QDIALFEHMTVNENI----------RCFK 97
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIARMGVVRtfQHVRLFREMTVIENLlvaqhqqlktGLFS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 98 ALCKAP----------------LSNVLIDEYA-RQlnlnertmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDL 160
Cdd:PRK11300 116 GLLKTPafrraesealdraatwLERVGLLEHAnRQ---------AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739682787 161 KSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK11300 187 KETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-155 |
2.91e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKcifesldMTFENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYfGEQLskkqrqdKI 74
Cdd:PRK11819 325 IEAENLSKSFGDR-------LLIDDLSFSLppggivgIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQ--DiALFEHMTVNENircfkalckaplsnvlIDEYARQLNLNERTMT------------------ISNLSGGTKR 134
Cdd:PRK11819 390 AYVDQsrD-ALDPNKTVWEE----------------ISGGLDIIKVGNREIPsrayvgrfnfkggdqqkkVGVLSGGERN 452
|
170 180
....*....|....*....|.
gi 739682787 135 KVNVLIGLLSNPQILILDEPT 155
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPT 473
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-196 |
3.43e-11 |
|
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: 60.62 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMT---------------FENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIR 59
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKlgilgrkgevgefwaLKDVSFEVprgerigLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 60 YFGeqlskkqrqdkigyvpQDIALFE-------HMTVNENIRcFKALCKApLSNVLIDE-YARQLNLNE----RTMTISN 127
Cdd:cd03220 81 VRG----------------RVSSLLGlgggfnpELTGRENIY-LNGRLLG-LSRKEIDEkIDEIIEFSElgdfIDLPVKT 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 128 LSGGTKRKVNVLIGLLSNPQILILDEPT-VGiDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEVEALADQI 196
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLaVG-DAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRA 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-189 |
3.96e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFE-----SLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIGY 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALfeHMTVNENIRCFKALCK------------------------APLSNVLIDEYARQL--------NLNERTMT 124
Cdd:PRK13651 83 VLEKLVI--QKTRFKKIKKIKEIRRrvgvvfqfaeyqlfeqtiekdiifGPVSMGVSKEEAKKRaakyielvGLDESYLQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 125 IS--NLSGGTKRKVnVLIGLLS-NPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLDEV 189
Cdd:PRK13651 161 RSpfELSGGQKRRV-ALAGILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNV 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
124-201 |
4.27e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 124 TISNLSGGTKRKVnvLIG--LLSNPQILILDEPTVGIDLKSRFDIHNLLNTM-KRERLIILTTHHLDEVEALADQIKVIG 200
Cdd:PRK10982 388 QIGSLSGGNQQKV--IIGrwLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMS 465
|
.
gi 739682787 201 N 201
Cdd:PRK10982 466 N 466
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-184 |
4.92e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAglEQLTKGEIRYfGEQLSKKQRQDK-----IGYVPQ-DIALfEHMTVNENIRcFKALCK 101
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLA--ERVTTGVITG-GDRLVNGRPLDSsfqrsIGYVQQqDLHL-PTSTVRESLR-FSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 102 APLS------NVLIDEYARQLNLNERTMTISNLSG---GTKRKVNVLIG--LLSNPQILI-LDEPTVGIDLKSRFDIHNL 169
Cdd:TIGR00956 865 QPKSvsksekMEYVEEVIKLLEMESYADAVVGVPGeglNVEQRKRLTIGveLVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
170
....*....|....*.
gi 739682787 170 L-NTMKRERLIILTTH 184
Cdd:TIGR00956 945 MrKLADHGQAILCTIH 960
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-186 |
6.88e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.05 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLR-------MIAGLEqlTKGEIRYFGEQLSKKQ----- 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYDPDvdvve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 -RQdKIGYVPQDIALFEhMTVNENI-----------------RCFKALCKAplsnVLIDEYARQLNLNErtmtiSNLSGG 131
Cdd:COG1117 90 lRR-RVGMVFQKPNPFP-KSIYDNVayglrlhgikskseldeIVEESLRKA----ALWDEVKDRLKKSA-----LGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 132 TK------RKVNVligllsNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHL 186
Cdd:COG1117 159 QQqrlciaRALAV------EPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-201 |
1.21e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRK----KCIFESLDMTFENLQLTVLLGENGAGKS-TLLRMIAGLEQ----LTKGEIRYFG-------EQ 64
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGesllhasEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 65 LSKKQRQDKIGYVPQD------------IALFEHMTVN----------ENIRCfkalckapLSNVLIDEYARQLNLNERt 122
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEpmvslnplhtleKQLYEVLSLHrgmrreaargEILNC--------LDRVGIRQAAKRLTDYPH- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 123 mtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE----RLIIltTHHLDEVEALADQIKV 198
Cdd:PRK15134 156 ----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnmgLLFI--THNLSIVRKLADRVAV 229
|
...
gi 739682787 199 IGN 201
Cdd:PRK15134 230 MQN 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-195 |
1.94e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.95 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 6 NLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGeIRYFGEQL----SKKQRQDKIGYVPQDI 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 ALFEH-----MTVNENI------------RCFKALCKAPLSNV-LIDEYARQLnlnerTMTISNLSGGTKRKVNVLIGLL 143
Cdd:PRK14271 105 MLFQRpnpfpMSIMDNVlagvrahklvprKEFRGVAQARLTEVgLWDAVKDRL-----SDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739682787 144 SNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALADQ 195
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDR 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-199 |
2.02e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.36 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 110 DEYARQLNLNERT-MTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTTHHLD 187
Cdd:NF000106 126 DELLERFSLTEAAgRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYME 205
|
90
....*....|..
gi 739682787 188 EVEALADQIKVI 199
Cdd:NF000106 206 EAEQLAHELTVI 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-198 |
2.22e-10 |
|
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: 59.45 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-KQ---RQDkIGY 76
Cdd:COG5265 358 VRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQaslRAA-IGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFeHMTVNENIR----------CFKAlckAPLSNvlIDEYARQL------NLNERTMtisNLSGGTKRKVNVLI 140
Cdd:COG5265 437 VPQDTVLF-NDTIAYNIAygrpdaseeeVEAA---ARAAQ--IHDFIESLpdgydtRVGERGL---KLSGGEKQRVAIAR 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 141 GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIIltTHHLDEVeALADQIKV 198
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGRttLVI--AHRLSTI-VDADEILV 564
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-184 |
2.38e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDKIGYVPQDIALFEHMTVNENIRC 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 FKAL--CKA------PLSNVLIDEYARQLnlnertmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLksrfDIH 167
Cdd:PRK13543 106 LCGLhgRRAkqmpgsALAIVGLAGYEDTL--------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGI 173
|
170 180
....*....|....*....|..
gi 739682787 168 NLLNTMKRERL-----IILTTH 184
Cdd:PRK13543 174 TLVNRMISAHLrgggaALVTTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-200 |
2.62e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRkkcifESLDMTFENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD-- 72
Cdd:TIGR00957 1285 VEFRNYCLRYR-----EDLDLVLRHINVTIhggekvgIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlr 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 -KIGYVPQDIALFEHmTVNENIRcfkalckaPLSNVLIDEYARQLNLNERTMTIS---------------NLSGGTKRKV 136
Cdd:TIGR00957 1360 fKITIIPQDPVLFSG-SLRMNLD--------PFSQYSDEEVWWALELAHLKTFVSalpdkldhecaeggeNLSVGQRQLV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 137 NVLIGLLSNPQILILDEPTVGIDL----------KSRFD------IHNLLNT-MKRERLIILTTHHLDEVEALADQIKVI 199
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLetdnliqstiRTQFEdctvltIAHRLNTiMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
|
.
gi 739682787 200 G 200
Cdd:TIGR00957 1511 G 1511
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-196 |
3.04e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHY----RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-------KQ 69
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalaQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIGYVPQDIALFEHMTVNENIR---CFKALCKAPLSNVLIDEYARqLNLNERT-MTISNLSGGTKRKVNVLIGLLSN 145
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEvpaVYAGLERKQRLLRAQELLQR-LGLEDRVeYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMkRER---LIILTthHLDEVEALADQI 196
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRghtVIIVT--HDPQVAAQAERV 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-194 |
6.89e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQL-----TKGEIRYFGEQLSKKQ-----RQ 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDvdpveVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 72 DKIGYV-----PQDIALFEHMTVNENIRCFKA----LCKAPLSN-VLIDEYARQLNlnertMTISNLSGGTKRKVNVLIG 141
Cdd:PRK14243 91 RRIGMVfqkpnPFPKSIYDNIAYGARINGYKGdmdeLVERSLRQaALWDEVKDKLK-----QSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 142 LLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEALAD 194
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-199 |
7.22e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHY--RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK---KQRQDKIGY 76
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytlASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIrcfKALCKAPLSNVLIDEYAR---------QLNLNERTMTISN---LSGGTKRKVNVLIGLLS 144
Cdd:PRK11176 422 VSQNVHLFND-TIANNI---AYARTEQYSREQIEEAARmayamdfinKMDNGLDTVIGENgvlLSGGQRQRIAIARALLR 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVI 199
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVV 551
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-198 |
8.20e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYR-KKCIF------ESLD-MTFEnLQ----LTVLlGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSK-- 67
Cdd:PRK11308 6 LQAIDLKKHYPvKRGLFkperlvKALDgVSFT-LErgktLAVV-GESGCGKSTLARLLTMIETPTGGELYYQGQDLLKad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 68 ----KQRQDKIGYVPQ-------------DIaLFEHMTVNENI----RCFKALckAPLSNV-LIDE-YARQLNLnertmt 124
Cdd:PRK11308 84 peaqKLLRQKIQIVFQnpygslnprkkvgQI-LEEPLLINTSLsaaeRREKAL--AMMAKVgLRPEhYDRYPHM------ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 125 isnLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE----RLIIltTHHLDEVEALADQIKV 198
Cdd:PRK11308 155 ---FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElglsYVFI--SHDLSVVEHIADEVMV 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-194 |
9.05e-10 |
|
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: 56.57 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRY-------FGEQLSKKQRQDKIGYVPQDIALFeHMTVNENI------- 93
Cdd:cd03290 28 QLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesePSFEATRSRNRYSVAYAAQKPWLL-NATVEENItfgspfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 -RCFKALCKAPLSNVLID--EYARQLNLNERTMtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID--LKSRFDIHN 168
Cdd:cd03290 107 kQRYKAVTDACSLQPDIDllPFGDQTEIGERGI---NLSGGQRQRICVARALYQNTNIVFLDDPFSALDihLSDHLMQEG 183
|
170 180 190
....*....|....*....|....*....|...
gi 739682787 169 LLNTMKRE-RLIILTTH------HLDEVEALAD 194
Cdd:cd03290 184 ILKFLQDDkRTLVLVTHklqylpHADWIIAMKD 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-199 |
1.16e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKC-IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFG---EQLSKKQRQDKI-G 75
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIAL-FEHMTVNENIrCF--KALCKAPLS-NVLIDEYARQLNLNE-RTMTISNLSGGTKRKVnVLIGLLS-NPQIL 149
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDL-AFgpENLCLPPIEiRKRVDRALAEIGLEKyRHRSPKTLSGGQGQCV-ALAGILTmEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 150 ILDEPTVGIDLKSRFDI-HNLLNTMKRERLIILTTHHLDEVEAlADQIKVI 199
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVlERIKKLHEKGKTIVYITHNLEELHD-ADRIIVM 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-191 |
1.67e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 29 LTVLLGENGAGKSTLLRMIAGLEQ--LTKGEIRYFGeqLSKKQRQ-DKI-GYVPQDIALFEHMTVNENIrCFKALCKAPL 104
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG--FPKKQETfARIsGYCEQNDIHSPQVTVRESL-IYSAFLRLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 105 S------NVLIDEYARQLNLNERTMTISNLSGGT------KRKVNVLIGLLSNPQILILDEPTVGIDLK-SRFDIHNLLN 171
Cdd:PLN03140 985 EvskeekMMFVDEVMELVELDNLKDAIVGLPGVTglsteqRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRTVRN 1064
|
170 180
....*....|....*....|..
gi 739682787 172 TMKRERLIILTTHH--LDEVEA 191
Cdd:PLN03140 1065 TVDTGRTVVCTIHQpsIDIFEA 1086
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-198 |
1.94e-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: 56.62 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKS----TLLRMIAGLEQLTKGEIRYFGEQL---SKKQ----RQDKIGYVPQD--IALFEHMTV----NENIR 94
Cdd:COG4172 41 LVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERElrriRGNRIAMIFQEpmTSLNPLHTIgkqiAEVLR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 95 CFKALCKAP--------LSNVLIDEYARQLNlnertmtiS---NLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSR 163
Cdd:COG4172 121 LHRGLSGAAararalelLERVGIPDPERRLD--------AyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQ 192
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 164 FDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKV 198
Cdd:COG4172 193 AQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAV 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-163 |
2.06e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 33 LGENGAGKSTLLRMIAGLEQLTKGEIryfgeqlskkQRQDKIGYVPQDIALFEHMTVNENIRcfkALCKAPLSNVLIDEY 112
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEV----------DPELKISYKPQYIKPDYDGTVEDLLR---SITDDLGSSYYKSEI 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 113 ARQLNLnERTMT--ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSR 163
Cdd:PRK13409 438 IKPLQL-ERLLDknVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-201 |
2.34e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 21 DMTFENL--QLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYVPQDIALFEHmTVNENIRC 95
Cdd:PRK13657 353 DVSFEAKpgQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrrNIAVVFQDAGLFNR-SIEDNIRV 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 FKA------LCKAPLSNVLIDEYARQL-----NLNERTmtiSNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRF 164
Cdd:PRK13657 432 GRPdatdeeMRAAAERAQAHDFIERKPdgydtVVGERG---RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 165 DIHNLLNTMKRERLIILTTHHLDEVEAlADQIKVIGN 201
Cdd:PRK13657 509 KVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDN 544
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
110-199 |
2.98e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 110 DEYARQLNLneRTMTIS----NLSGGTKRKVnVLI-GLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RLIILTT 183
Cdd:NF040905 385 EEYRKKMNI--KTPSVFqkvgNLSGGNQQKV-VLSkWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVIS 461
|
90
....*....|....*.
gi 739682787 184 HHLDEVEALADQIKVI 199
Cdd:NF040905 462 SELPELLGMCDRIYVM 477
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-199 |
3.45e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.48 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRK------KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQR---- 70
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 QDKIGYVPQ-------------DIALF-EHMTVN-ENIRcfkalckaplsnVLIDEYARQLNLNE-RTMTISNLSGGTKR 134
Cdd:PRK13633 84 RNKAGMVFQnpdnqivativeeDVAFGpENLGIPpEEIR------------ERVDESLKKVGMYEyRRHAPHLLSGGQKQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 135 KVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVeALADQIKVI 199
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA-VEADRIIVM 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-155 |
3.81e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQDK--------IGYVPQDIA-----------LFEHMTVNEN 92
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPprnvegtvYDFVAEGIEeqaeylkryhdISHLVETDPS 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 93 IRCFKALckAPLSNVL-----------IDEYARQLNLNERTMtISNLSGGTKRKVNVLIGLLSNPQILILDEPT 155
Cdd:PRK11147 114 EKNLNEL--AKLQEQLdhhnlwqlenrINEVLAQLGLDPDAA-LSSLSGGWLRKAALGRALVSNPDVLLLDEPT 184
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-190 |
4.15e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 33 LGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQ-----LSKKQRqdkIGYVPQDIALFEHMTVNENI----RCFKAlcKAP 103
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdagdIATRRR---VGYMSQAFSLYGELTVRQNLelhaRLFHL--PAA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 104 LSNVLIDEYARQLNLNE-RTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LII 180
Cdd:NF033858 373 EIAARVAEMLERFDLADvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDgvTIF 452
|
170
....*....|
gi 739682787 181 LTTHHLDEVE 190
Cdd:NF033858 453 ISTHFMNEAE 462
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-185 |
4.80e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLE--QLTKGEIRYFGEQLSKKQRQDK----- 73
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 74 -IGY-VPQDI-----ALFEHMTVNENIRC----------FKALCKAPLSNVLIDEYARQLNLNErtmtisNLSGGTKRKV 136
Cdd:CHL00131 87 fLAFqYPIEIpgvsnADFLRLAYNSKRKFqglpeldpleFLEIINEKLKLVGMDPSFLSRNVNE------GFSGGEKKRN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739682787 137 NVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNT-MKRERLIILTTHH 185
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHY 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-196 |
6.10e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLeqLT-KGEIRYFGEQLSK-------------KQRQDKIGYVP--QDIALFEHmtvnenirc 95
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL--LPgSGSIQFAGQPLEAwsaaelarhraylSQQQTPPFAMPvfQYLTLHQP--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 fkALCKAPLSNVLIDEYARQLNLNER-TMTISNLSGGTKRKVNVLIGLL-----SNP--QILILDEPTVGIDLKSRFDIH 167
Cdd:PRK03695 96 --DKTRTEAVASALNEVAEALGLDDKlGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190
....*....|....*....|....*....|
gi 739682787 168 NLLNTMKRE-RLIILTTHHLDEVEALADQI 196
Cdd:PRK03695 174 RLLSELCQQgIAVVMSSHDLNHTLRHADRV 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-203 |
6.65e-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: 54.29 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQLTKGE----------IRYF-GEQLS---KKQRQDKIGYV--PQDIALFEHmTVNE 91
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFrGSELQnyfTKLLEGDVKVIvkPQYVDLIPK-AVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 92 NIRcfkALCKAPLSNVLIDEYARQLNLN---ERTmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHN 168
Cdd:cd03236 106 KVG---ELLKKKDERGKLDELVDQLELRhvlDRN--IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 739682787 169 LLNTMKRE-RLIILTTHHLDEVEALADQIKVIGNDP 203
Cdd:cd03236 181 LIRELAEDdNYVLVVEHDLAVLDYLSDYIHCLYGEP 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-199 |
8.41e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 25 ENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL----SKKQRQDKIGYVPQDIALFEHMTVNENI 93
Cdd:PRK10982 15 DNVNLKVrphsihaLMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGISMVHQELNLVLQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 94 rcfkALCKAPLSNVLIDEYAR-----------QLNLNERTmTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKS 162
Cdd:PRK10982 95 ----WLGRYPTKGMFVDQDKMyrdtkaifdelDIDIDPRA-KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 739682787 163 RFDIHNLLNTMKRERL-IILTTHHLDEVEALADQIKVI 199
Cdd:PRK10982 170 VNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITIL 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-196 |
1.03e-08 |
|
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: 52.54 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIF-ESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIryfgeqlsKKQRQDKIGYVPQD 80
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 ialfEHMTVNeNIRCfkALCKaPLSNVlideyarqlnlnertmtisnLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDL 160
Cdd:cd03223 73 ----PYLPLG-TLRE--QLIY-PWDDV--------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 161 KSRFDIHNLLntmkRERLI-ILTTHHLDEVEALADQI 196
Cdd:cd03223 125 ESEDRLYQLL----KELGItVISVGHRPSLWKFHDRV 157
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-194 |
1.05e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 13 KKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLE--QLTKGEIRYFGEQLskkqrqdkigyvPQDIALFEHMTVN 90
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF------------GREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 91 ENIR-CFKALCKAPLSNVLIdeYARqlnlnertmTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID-LKSRFDIHN 168
Cdd:COG2401 110 GDFKdAVELLNAVGLSDAVL--WLR---------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrQTAKRVARN 178
|
170 180
....*....|....*....|....*..
gi 739682787 169 LLNTMKRERL-IILTTHHLDEVEALAD 194
Cdd:COG2401 179 LQKLARRAGItLVVATHHYDVIDDLQP 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-200 |
1.20e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.36 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 12 RKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLeqltkgeiryFGEQLSKKQRQDKIGyvpqdialfehmtvne 91
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLA----------LGGAQSATRRRSGVK---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 92 nIRCFKALCKAplsnvlideyarqlnlnERTMTISNLSGGTKRKV---NVLIGLLSNP-QILILDEPTVGIDLksrFDIH 167
Cdd:cd03227 60 -AGCIVAAVSA-----------------ELIFTRLQLSGGEKELSalaLILALASLKPrPLYILDEIDRGLDP---RDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 739682787 168 NLLNTMKR----ERLIILTThHLDEVEALADQIKVIG 200
Cdd:cd03227 119 ALAEAILEhlvkGAQVIVIT-HLPELAELADKLIHIK 154
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-199 |
2.82e-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: 52.03 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKkcifeSLDMTFENLQLTV-------LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD-- 72
Cdd:cd03369 7 IEVENLSVRYAP-----DLPPVLKNVSFKVkagekigIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 -KIGYVPQDIALFEHmTVNENIRCFkalckaplsnvliDEYARQ-----LNLNERTmtiSNLSGGTKRKVNVLIGLLSNP 146
Cdd:cd03369 82 sSLTIIPQDPTLFSG-TIRSNLDPF-------------DEYSDEeiygaLRVSEGG---LNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 147 QILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLDEVeALADQIKVI 199
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVM 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-159 |
3.51e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAG------LEQLTK-GEIRYFGEQLSKKQRqdKI 74
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTLfGRRRGSGETIWDIKK--HI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 75 GYVPQDIalfeHMT--VNENIR------------CFKALCKAplSNVLIDEYARQLNLNERT--MTISNLSGGTKRKVNV 138
Cdd:PRK10938 339 GYVSSSL----HLDyrVSTSVRnvilsgffdsigIYQAVSDR--QQKLAQQWLDILGIDKRTadAPFHSLSWGQQRLALI 412
|
170 180
....*....|....*....|.
gi 739682787 139 LIGLLSNPQILILDEPTVGID 159
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLD 433
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-199 |
4.16e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKST----LLRMIAgleqlTKGEIRYFG---EQLSKKQR---QDKIGYVPQD--IALFEHMTVNENIRCFKAL 99
Cdd:PRK15134 317 LVGESGSGKSTtglaLLRLIN-----SQGEIWFDGqplHNLNRRQLlpvRHRIQVVFQDpnSSLNPRLNVLQIIEEGLRV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 100 CKAPLSNVLIDEYARQ------LNLNERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTM 173
Cdd:PRK15134 392 HQPTLSAAQREQQVIAvmeevgLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
170 180
....*....|....*....|....*...
gi 739682787 174 KRERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:PRK15134 472 QQKHQLayLFISHDLHVVRALCHQVIVL 499
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-199 |
8.81e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGL---------EQLTKGE-IRYF-GEQLS---KKQRQDKIGYV--PQDIALFEhmtvneniRC 95
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEvLKRFrGTELQnyfKKLYNGEIKVVhkPQYVDLIP--------KV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 FKALCKAPLSNV----LIDEYARQLNLN---ERTmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHN 168
Cdd:PRK13409 176 FKGKVRELLKKVdergKLDEVVERLGLEnilDRD--ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVAR 253
|
170 180 190
....*....|....*....|....*....|.
gi 739682787 169 LLNTMKRERLIILTTHHLDEVEALADQIKVI 199
Cdd:PRK13409 254 LIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-198 |
9.93e-08 |
|
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: 51.61 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQlTKGEIRYFGEQLSKKQRQD------KIGYVPQD--IALFEHMTVNENIRCFKALCKAP 103
Cdd:COG4172 317 LVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrrRMQVVFQDpfGSLSPRMTVGQIIAEGLRVHGPG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 104 LSNVLIDEYARQL----NLNERTMT--ISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER 177
Cdd:COG4172 396 LSAAERRARVAEAleevGLDPAARHryPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREH 475
|
170 180
....*....|....*....|....*
gi 739682787 178 ----LIIltTHHLDEVEALADQIKV 198
Cdd:COG4172 476 glayLFI--SHDLAVVRALAHRVMV 498
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-194 |
1.02e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGleQLT----------KGEIRYFGEQLSK--- 67
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAida 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 68 -----------KQRQDKIGYVPQDIAL---FEHMT-VNENIRCFKALCKAPLsnvlidEYARQLNLNERTMTisNLSGGT 132
Cdd:PRK13547 79 prlarlravlpQAAQPAFAFSAREIVLlgrYPHARrAGALTHRDGEIAWQAL------ALAGATALVGRDVT--TLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 133 KRKVN---VLIGL------LSNPQILILDEPTVGIDLKSRfdiHNLLNTMK---RE-RLIILT--------THHLDEVEA 191
Cdd:PRK13547 151 LARVQfarVLAQLwpphdaAQPPRYLLLDEPTAALDLAHQ---HRLLDTVRrlaRDwNLGVLAivhdpnlaARHADRIAM 227
|
...
gi 739682787 192 LAD 194
Cdd:PRK13547 228 LAD 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-198 |
1.44e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 5 KNLSKHY--RKKCifesLDMTFENLQLTVL--LGENGAGKSTLLRMIAGLEQLTKGEIRYFGE--------QLSKKQR-- 70
Cdd:PRK11701 10 RGLTKLYgpRKGC----RDVSFDLYPGEVLgiVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 71 --QDKIGYVPQDIALFEHMTVN-----------------ENIRCfKALckAPLSNVLIDEyARqlnLNERTMTisnLSGG 131
Cdd:PRK11701 86 llRTEWGFVHQHPRDGLRMQVSaggnigerlmavgarhyGDIRA-TAG--DWLERVEIDA-AR---IDDLPTT---FSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 132 TKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRE-RL-IILTTHHLDEVEALADQIKV 198
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLaVVIVTHDLAVARLLAHRLLV 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-199 |
1.72e-07 |
|
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: 50.94 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGL---------EQLTKGEI--RYFGEQLS---KKQRQDKI--GYVPQDIalfehmtvnENI-R 94
Cdd:COG1245 104 ILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVlkRFRGTELQdyfKKLANGEIkvAHKPQYV---------DLIpK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 95 CFKALCKAPLSNV----LIDEYARQLNLN---ERTmtISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIH 167
Cdd:COG1245 175 VFKGTVRELLEKVdergKLDELAEKLGLEnilDRD--ISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVA 252
|
170 180 190
....*....|....*....|....*....|....*.
gi 739682787 168 NLLNTMKRERLIILTTHH----LDeveALADQIKVI 199
Cdd:COG1245 253 RLIRELAEEGKYVLVVEHdlaiLD---YLADYVHIL 285
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-159 |
3.26e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQLTKGEIryFGEQlskkqrqdKIGYVPQDiALFEHMTVNENIRCFKALCKAPLSNV 107
Cdd:PTZ00243 687 KLTVVLGATGSGKSTLLQSLLSQFEISEGRV--WAER--------SIAYVPQQ-AWIMNATVRGNILFFDEEDAARLADA 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739682787 108 L----IDEYARQL------NLNERTMtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:PTZ00243 756 VrvsqLEADLAQLgggletEIGEKGV---NLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-217 |
4.11e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLS-KHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYfgeqlskkQRQDKIGYVPQ 79
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGARVLFLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 80 ----------DIALF----EHMTvNENIRcfKALCKAPLSNvLIDEYARQLNLNERtmtisnLSGGTKRKVNVLIGLLSN 145
Cdd:COG4178 434 rpylplgtlrEALLYpataEAFS-DAELR--EALEAVGLGH-LAERLDEEADWDQV------LSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLntmkRERL----IILTTHHlDEVEALADQikVIgndpfyrELLEDKHWPFE 217
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLL----REELpgttVISVGHR-STLAAFHDR--VL-------ELTGDGSWQLL 565
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
14-203 |
4.46e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 14 KCIFESLDMTFENLqLTVLLGENGAGKSTLLRMIagleqltkgeiRY--FGEQ-LSKKQR---------QDKIGYVpqDI 81
Cdd:cd03240 10 RSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEAL-----------KYalTGELpPNSKGGahdpklireGEVRAQV--KL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 82 AlFEH-----MTVNENIRCFK--ALCKAPLSNVLIDEyarqlnlnertmTISNLSGGTKRKVNVLIGLL------SNPQI 148
Cdd:cd03240 76 A-FENangkkYTITRSLAILEnvIFCHQGESNWPLLD------------MRGRCSGGEKVLASLIIRLAlaetfgSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 149 LILDEPTVGIDLKSR-FDIHNLLNTMKRE--RLIILTTHHlDEVEALADQIKVIGNDP 203
Cdd:cd03240 143 LALDEPTTNLDEENIeESLAEIIEERKSQknFQLIVITHD-EELVDAADHIYRVEKDG 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-201 |
8.85e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKhYRKKCIFESLDMTFENLQLTVLLGENGAGKS----TLLRMI-AGLEQlTKGEIRYFGEQLSKKQ-RQDKIG 75
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCAlRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDI-ALFE--HMTVNENIRCFKALCKAPLSNVLI--------DEYARQLNLNERTMtisnlSGGTKRKVNVLIGLLS 144
Cdd:PRK10418 83 TIMQNPrSAFNplHTMHTHARETCLALGKPADDATLTaaleavglENAARVLKLYPFEM-----SGGMLQRMMIALALLC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739682787 145 NPQILILDEPTVGIDLKSRFDIHNLLNTMKRERL--IILTTHHLDEVEALADQIKVIGN 201
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-192 |
9.05e-07 |
|
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: 49.14 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK--KCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQlTKGEIRYFG---EQLSKKQRQDKIGY 76
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIRCFKALCKAPLSNV--------LIDEYARQLN--LNERTMTISNlsgGTKRKVNVLIGLLSNP 146
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQWSDEEIWKVaeevglksVIEQFPDKLDfvLVDGGYVLSN---GHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739682787 147 QILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHhldEVEAL 192
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH---RVEAL 1415
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-48 |
1.06e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 48.07 E-value: 1.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 739682787 2 IELKNLskhyrkKCiFESLDMTFENL-QLTVLLGENGAGKSTLLRMIA 48
Cdd:COG3950 6 LTIENF------RG-FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIA 46
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-199 |
1.17e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKS-TLLRMIAGLEQlTKGEIRYFGEQLSKKQRQdKIGYVPQ-----------DIALF--EHMT--------- 88
Cdd:PRK10261 47 IVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRSRQ-VIELSEQsaaqmrhvrgaDMAMIfqEPMTslnpvftvg 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 89 --VNENIRCFK------ALCKA---------PLSNVLIDEYARQLnlnertmtisnlSGGTKRKVNVLIGLLSNPQILIL 151
Cdd:PRK10261 125 eqIAESIRLHQgasreeAMVEAkrmldqvriPEAQTILSRYPHQL------------SGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739682787 152 DEPTVGIDLKSRFDIHNLLNTMKRERL--IILTTHHLDEVEALADQIKVI 199
Cdd:PRK10261 193 DEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVM 242
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-203 |
2.67e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 24 FENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEqlskkqrqdKIGYVPQDIalfehmtvnenircfkalckap 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI---------TPVYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 104 lsnvlideyarqlnlnertmtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLN--TMKRERLIIL 181
Cdd:cd03222 71 -----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlSEEGKKTALV 127
|
170 180
....*....|....*....|..
gi 739682787 182 TTHHLDEVEALADQIKVIGNDP 203
Cdd:cd03222 128 VEHDLAVLDYLSDRIHVFEGEP 149
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-199 |
3.75e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHY-RKKCIFESLD---MTFENLQLTVLLGENGAGKSTLLRMIAGL----EQLTKGEIRYFGEQL---SKKQ 69
Cdd:PRK11022 3 LLNVDKLSVHFgDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLqriSEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 70 RQDKIG----YVPQDI----------------ALFEHMTVNENIRCFKALckAPLSNVLIDEYARQLNLNERtmtisNLS 129
Cdd:PRK11022 83 RRNLVGaevaMIFQDPmtslnpcytvgfqimeAIKVHQGGNKKTRRQRAI--DLLNQVGIPDPASRLDVYPH-----QLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739682787 130 GGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAAHKIIVM 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-163 |
6.56e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 1 MIELKNLSKHYRKKCIFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIryfgeQLSKKQrqdKIGYVPQD 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGI---KLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 81 iaLFEHMTVNEnircfkalckAPL---SNVLIDEYARQL---------NLNERTMTISNLSGGTK-RKVNVLIgLLSNPQ 147
Cdd:PRK10636 384 --QLEFLRADE----------SPLqhlARLAPQELEQKLrdylggfgfQGDKVTEETRRFSGGEKaRLVLALI-VWQRPN 450
|
170
....*....|....*.
gi 739682787 148 ILILDEPTVGIDLKSR 163
Cdd:PRK10636 451 LLLLDEPTNHLDLDMR 466
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-210 |
6.94e-06 |
|
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: 46.48 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 19 SLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEqlskkqrqdkIGYVPQDiALFEHMTVNENIRCFKA 98
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------VAYVPQQ-AWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 99 L-----------CkAPLSNVLIDEYARQLNLNERTMtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDlkSRFDIH 167
Cdd:TIGR00957 725 LnekyyqqvleaC-ALLPDLEILPSGDRTEIGEKGV---NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD--AHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739682787 168 NLLNTMKRERLI-----ILTTH------HLDEVEALAD-QIKVIGNdpfYRELLE 210
Cdd:TIGR00957 799 IFEHVIGPEGVLknktrILVTHgisylpQVDVIIVMSGgKISEMGS---YQELLQ 850
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-187 |
1.97e-05 |
|
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: 44.46 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRK--KCIFESLDMTFENLQLTVLLGENGAGKSTLLRmiAGLEQL-TKGEIRYFG---EQLSKKQRQDKIG 75
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRLLnTEGDIQIDGvswNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 76 YVPQDIALFEHmTVNENIRCFKALCKAPLSNV--------LIDEYARQLNLnerTMTISN--LSGGTKRKVNVLIGLLSN 145
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLDPYGKWSDEEIWKVaeevglksVIEQFPGQLDF---VLVDGGcvLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739682787 146 PQILILDEPTVGIDLKSRFDIHNLLNTMKRERLIILTTHHLD 187
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-199 |
2.44e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQL-----SKKQ--RQDkIGYVPQD--IALFEHMTVNENIrcfkalcKA 102
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQalRRD-IQFIFQDpyASLDPRQTVGDSI-------ME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 103 PL--SNVLIDEYA--RQLNLNERTMTISN--------LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLL 170
Cdd:PRK10261 427 PLrvHGLLPGKAAaaRVAWLLERVGLLPEhawrypheFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180 190
....*....|....*....|....*....|.
gi 739682787 171 NTMKRERLI--ILTTHHLDEVEALADQIKVI 199
Cdd:PRK10261 507 LDLQRDFGIayLFISHDMAVVERISHRVAVM 537
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
77-201 |
2.47e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFeHMTVNENIRC---------FKALCKAPLSNVLIDEYARQLNLNERTMTISnLSGGTKRKVNVLIGLLSNPQ 147
Cdd:PTZ00265 1301 VSQEPMLF-NMSIYENIKFgkedatredVKRACKFAAIDEFIESLPNKYDTNVGPYGKS-LSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 739682787 148 ILILDEPTVGIDLKSRFDIHNLLNTM--KRERLIILTTHHLDEVEAlADQIKVIGN 201
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-189 |
2.49e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGYVPQDIALFEHmTVNENIRCF---------KAL 99
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrrVLSIIPQSPVLFSG-TVRFNIDPFsehndadlwEAL 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 100 CKAPLSNVlIDEYARQLNLnERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRERLI 179
Cdd:PLN03232 1346 ERAHIKDV-IDRNPFGLDA-EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM 1423
|
170
....*....|
gi 739682787 180 ILTTHHLDEV 189
Cdd:PLN03232 1424 LVIAHRLNTI 1433
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
2-184 |
4.67e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 43.03 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLskhyrkKCiFESLDMTFENLqlTVLLGENGAGKSTLLRMIAGLEQLT-------KGEIRYFGEQLSKKQRQ--D 72
Cdd:COG4938 4 ISIKNF------GP-FKEAELELKPL--TLLIGPNGSGKSTLIQALLLLLQSNfiylpaeRSGPARLYPSLVRELSDlgS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 73 KIGYVPQDIALFEHMTVNENIRCF---------KALCKAPLS-NVLIDEYARQL--NLNERTMTISNLSGGTKRKVNVLI 140
Cdd:COG4938 75 RGEYTADFLAELENLEILDDKSKElleqveewlEKIFPGKVEvDASSDLVRLVFrpSGNGKRIPLSNVGSGVSELLPILL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739682787 141 GLLS---NPQILILDEPTVGIDLKSRFDIHNLL-NTMKRERLIILTTH 184
Cdd:COG4938 155 ALLSaakPGSLLIIEEPEAHLHPKAQSALAELLaELANSGVQVIIETH 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-199 |
1.19e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 32 LLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEqlskkqrqdkIGYVPQDIALFEHMTVNENIRcFKALC---KAPLSNVL 108
Cdd:PRK13546 55 LVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------VSVIAISAGLSGQLTGIENIE-FKMLCmgfKRKEIKAM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 109 IDEYARQLNLNERT-MTISNLSGGTKRKVNVLIGLLSNPQILILDEP-TVGIDLKSRFDIHNLLNTMKRERLIILTTHHL 186
Cdd:PRK13546 124 TPKIIEFSELGEFIyQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNL 203
|
170
....*....|...
gi 739682787 187 DEVEALADQIKVI 199
Cdd:PRK13546 204 GQVRQFCTKIAWI 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-205 |
2.87e-04 |
|
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: 41.43 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGeqlskkqrqdKIGYVPQdIALFEHMTVNENIrc 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSPQ-TSWIMPGTIKDNI-- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 fkalckapLSNVLIDEY-------ARQLN-----LNERTMTI-----SNLSGGTKRKVNVLIGLLSNPQILILDEPTVGI 158
Cdd:TIGR01271 508 --------IFGLSYDEYrytsvikACQLEedialFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739682787 159 DLKSRFDIHN--LLNTMKRERLIILTT--HHLDEvealADQIKVIGNDPFY 205
Cdd:TIGR01271 580 DVVTEKEIFEscLCKLMSNKTRILVTSklEHLKK----ADKILLLHEGVCY 626
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-166 |
3.59e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAG-LEQLTK--GEIRYFGEQLSKKQRQDKIGYVPQDIALFEHMTVNENI----RC----- 95
Cdd:PLN03140 192 RMTLLLGPPSSGKTTLLLALAGkLDPSLKvsGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLdfsaRCqgvgt 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 --------------------------FKALCKAPLSNVLIDEYARQ---LNLNERTMT----ISNLSGGTKRKVNVLIGL 142
Cdd:PLN03140 272 rydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDYTLKilgLDICKDTIVgdemIRGISGGQKKRVTTGEMI 351
|
170 180
....*....|....*....|....
gi 739682787 143 LSNPQILILDEPTVGIDLKSRFDI 166
Cdd:PLN03140 352 VGPTKTLFMDEISTGLDSSTTYQI 375
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
128-199 |
3.68e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 3.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739682787 128 LSGGTKRKVNVLIGLLSNPQILILDEPTVGIDLKSRFDIHNLLNTMKRER--LIILTTHHLDEVEALADQIKVI 199
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWADKINVL 232
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
30-48 |
4.05e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.13 E-value: 4.05e-04
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-59 |
1.05e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|..
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQLTKGEIR 59
Cdd:cd01854 86 KTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-167 |
1.60e-03 |
|
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: 37.74 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 28 QLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYF--GEQLSKKQRQDKIGYVPQDIALFEHMTVNENIRcfkALCKAPLS 105
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIdgEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL---ALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739682787 106 NVLI-DEYAR----QLNLNERTMTISNLSGGTKRKVNVLIGLLSNPQILILDEPtvgidLKSRFDIH 167
Cdd:smart00382 80 DVLIlDEITSlldaEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL-----LRRRFDRR 141
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-159 |
1.74e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.19 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 29 LTVLLGENGAGKSTLLRMIAGleQLTKGEIryfgeqlSKKQRQDKIGYVPQDIALFeHMTVNENI---------RCFKAL 99
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLG--ELSHAET-------SSVVIRGSVAYVPQVSWIF-NATVRENIlfgsdfeseRYWRAI 714
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739682787 100 CKAPLSNVLIDEYARQLN-LNERTMtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:PLN03232 715 DVTALQHDLDLLPGRDLTeIGERGV---NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-45 |
1.83e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 739682787 2 IELKNLskhyrkKCiFESLDMTFENLqlTVLLGENGAGKSTLLR 45
Cdd:COG4637 5 IRIKNF------KS-LRDLELPLGPL--TVLIGANGSGKSNLLD 39
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
17-48 |
2.13e-03 |
|
ATP-binding cassette domain of MutS homologs; 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 also possess 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: 213210 [Multi-domain] Cd Length: 202 Bit Score: 38.00 E-value: 2.13e-03
10 20 30
....*....|....*....|....*....|..
gi 739682787 17 FESLDMTFENLQLTVLLGENGAGKSTLLRMIA 48
Cdd:cd03243 19 FVPNDINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-159 |
2.64e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.57 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 29 LTVLLGENGAGKSTLLR-MIAGLEQLTKGEIRYFGeqlskkqrqdKIGYVPQDIALFeHMTVNENIrCFKALCKAPLSNV 107
Cdd:PLN03130 645 LVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG----------TVAYVPQVSWIF-NATVRDNI-LFGSPFDPERYER 712
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739682787 108 LIDEYARQLNLN-----------ERTMtisNLSGGTKRKVNVLIGLLSNPQILILDEPTVGID 159
Cdd:PLN03130 713 AIDVTALQHDLDllpggdlteigERGV---NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-162 |
2.69e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.57 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 2 IELKNLSKHYRKKC--IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGEQLSKKQRQD---KIGY 76
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrkVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 77 VPQDIALFEHmTVNENIRCF---------KALCKAPLSNVlIDEYARQLNlNERTMTISNLSGGTKRKVNVLIGLLSNPQ 147
Cdd:PLN03130 1318 IPQAPVLFSG-TVRFNLDPFnehndadlwESLERAHLKDV-IRRNSLGLD-AEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170
....*....|....*
gi 739682787 148 ILILDEPTVGIDLKS 162
Cdd:PLN03130 1395 ILVLDEATAAVDVRT 1409
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-45 |
2.69e-03 |
|
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: 38.06 E-value: 2.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 739682787 2 IELKNlskhYRKkciFESLDMTFENlQLTVLLGENGAGKSTLLR 45
Cdd:COG3593 6 IKIKN----FRS---IKDLSIELSD-DLTVLVGENNSGKSSILE 41
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-205 |
3.29e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 37.53 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 16 IFESLDMTFENLQLTVLLGENGAGKSTLLRMIAGLEQLTKGEIRYFGeqlskkqrqdKIGYVPQdIALFEHMTVNENIrc 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQ-FSWIMPGTIKENI-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 96 fkalckapLSNVLIDEY-------ARQLN-----LNERTMTIS-----NLSGGTKRKVNVLIGLLSNPQILILDEPTVGI 158
Cdd:cd03291 119 --------IFGVSYDEYryksvvkACQLEeditkFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739682787 159 DLKSRFDIHN--LLNTMKRERLIILTThhldEVEAL--ADQIKVI--GNDPFY 205
Cdd:cd03291 191 DVFTEKEIFEscVCKLMANKTRILVTS----KMEHLkkADKILILheGSSYFY 239
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
4-44 |
3.43e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 37.83 E-value: 3.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 739682787 4 LKNLS-KHYRKkciFESLDMTFENlQLTVLLGENGAGKSTLL 44
Cdd:PRK00064 3 LTRLSlTDFRN---YEELDLELSP-GVNVLVGENGQGKTNLL 40
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
3-59 |
4.94e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 4.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739682787 3 ELKNLSKHYRK---KCIF------ESLDMTFENL--QLTVLLGENGAGKSTLLRMIAGLEQLTKGEIR 59
Cdd:pfam03193 71 ELEELLKIYRAigyPVLFvsaktgEGIEALKELLkgKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
12-48 |
6.32e-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: 6.32e-03
10 20 30
....*....|....*....|....*....|....*..
gi 739682787 12 RKKCIFESLDMtfENLQLTVLLGENGAGKSTLLRMIA 48
Cdd:cd03283 12 REKRVANDIDM--EKKNGILITGSNMSGKSTFLRTIG 46
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-45 |
8.48e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.14 E-value: 8.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 739682787 2 IELKNLSKHYRKKCIfesldmTFENlQLTVLLGENGAGKSTLLR 45
Cdd:COG0419 5 LRLENFRSYRDTETI------DFDD-GLNLIVGPNGAGKSTILE 41
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
4-47 |
9.01e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 36.51 E-value: 9.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 739682787 4 LKNLS-KHYRKkciFESLDMTFENlQLTVLLGENGAGKSTLLRMI 47
Cdd:cd03242 1 LKSLElRNFRN---YAELELEFEP-GVTVLVGENAQGKTNLLEAI 41
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-200 |
9.58e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 35.76 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 20 LDMTFENLQLTVLLGENGAGKSTLLrmiagLEQLTKGEIRYFGEQLSKKQRQDKIgYVPQdialfehmtvnenircfkal 99
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLYASGKARLISFLPKFSRNKLI-FIDQ-------------------- 67
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739682787 100 ckapLSNvLIDEYARQLNLNERTMTisnLSGGTKRKVNVLIGLLSNPQ--ILILDEPTVGIDLKsrfDIHNLLNTMKRER 177
Cdd:cd03238 68 ----LQF-LIDVGLGYLTLGQKLST---LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ---DINQLLEVIKGLI 136
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170 180
....*....|....*....|....*..
gi 739682787 178 ----LIILTTHHLDEVEaLADQIKVIG 200
Cdd:cd03238 137 dlgnTVILIEHNLDVLS-SADWIIDFG 162
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