|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
74-311 |
3.66e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 262.31 E-value: 3.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVpGKRV 153
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLtDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLSIYkcisLEEVFLKL 311
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL----LEDVFLEL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
74-286 |
4.48e-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: 204.94 E-value: 4.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRV 153
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYfgwifgmetkeilerlqfllnfldlpsekrlvknlSGGQQRRVSFAVALMHDPELLILD 233
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL-----------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHL 286
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
81-311 |
1.07e-54 |
|
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: 192.38 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQEI 160
Cdd:COG4555 9 KKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 239
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFlDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 240 DPLLRQSIWNHLVHITKAGqKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVFLKL 311
Cdd:COG4555 164 DVMARRLLREILRALKKEG-KTVLFSSHIMQEvEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
74-295 |
5.50e-52 |
|
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: 183.86 E-value: 5.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNAnqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRV 153
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI-NGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLtDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 295
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
81-289 |
1.59e-45 |
|
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: 165.06 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKnanqVLNNLNMTVPKGtIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQEI 160
Cdd:cd03264 8 KRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 239
Cdd:cd03264 82 GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLgDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 194201171 240 DPLLRQSIWNHLVHItkAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAE 289
Cdd:cd03264 162 DPEERIRFRNLLSEL--GEDRIVILSTHIVEDvESLCNQVAVLNKGKLVFE 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
73-289 |
7.06e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 166.05 E-value: 7.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGsgvPGKR 152
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDrANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 232 LDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHLLAE 289
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVeELCDRIVIINKGRKVLS 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
85-295 |
1.25e-44 |
|
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: 162.54 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 85 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQEIALYG 164
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 243
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAAdRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 244 RQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVL 295
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
81-288 |
1.13e-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: 156.91 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKR-VGYMPQE 159
Cdd:cd03259 8 KTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTGVP--PERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 160 IALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGlLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 194201171 239 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLA 288
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQ 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
74-284 |
3.54e-42 |
|
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: 155.13 E-value: 3.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTrgsgVPGKRV 153
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELsEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSG 284
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVeELCDRVLLLNKG 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
72-296 |
4.50e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 158.43 E-value: 4.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGK 151
Cdd:PRK13537 6 APIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-SLCGEPVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEKRL-VKNLSGGQQRRVSFAVALMHDPELL 230
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAkVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 231 ILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARG-KTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
74-289 |
4.93e-42 |
|
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: 155.32 E-value: 4.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGKRV 153
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LVDGEPVTG----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMyFGW-IFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVA-LGLeLQGVPKAEARERAEELLELVGLSgFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 232 LDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLM--RSGHLLAE 289
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAvFLADRVVVLsaRPGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
70-272 |
7.54e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.02 E-value: 7.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRymDAGEIFVlGGKPGTRgsg 147
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKP--TSGEVLV-DGKPVTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 vPGKRVGYMPQEIALygefsiqetmmyFGW-------IFGME-----TKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQ 214
Cdd:COG1116 78 -PGPDRGVVFQEPAL------------LPWltvldnvALGLElrgvpKAERRERARELLELVGLaGFEDAYPHQLSGGMR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 215 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 272
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEA 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
73-296 |
3.04e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 157.30 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGSGVPGKR 152
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-VPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEKRL-VKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADArVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 232 LDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
74-286 |
3.38e-41 |
|
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: 152.64 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG----GKPGTRGSGVP 149
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 GKRVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPE 228
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGdRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
74-289 |
7.52e-40 |
|
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: 148.52 E-value: 7.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVpgKRV 153
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILErlqfLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKdSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194201171 233 DEPTVGVDPL----LRQSIWNHlvhitKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:cd03268 151 DEPTNGLDPDgikeLRELILSL-----RDQGITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
70-296 |
1.44e-39 |
|
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: 148.97 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG---GKPGTRGS 146
Cdd:COG1127 2 SEPMIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 GVPGKRVGYMPQEIALYGEFSIQETMMY----FGwifGMETKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQR 215
Cdd:COG1127 78 YELRRRIGMLFQGGALFDSLTVFENVAFplreHT---DLSEAEIRELVLEKLELVGLpgaadkmPSE------LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 216 RVSFAVALMHDPELLILDEPTVGVDPLLRQSIwNHLVH-ITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPS 293
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVI-DELIReLRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
...
gi 194201171 294 VLL 296
Cdd:COG1127 228 ELL 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
86-285 |
4.27e-39 |
|
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: 146.46 E-value: 4.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 86 KKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQ------- 158
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQnpddqff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 ------EIAlygeFSIQetmmyfgwIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:cd03225 90 gptveeEVA----FGLE--------NLGLPEEEIEERVEEALELVGLEGlRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 232 LDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGH 285
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
74-298 |
2.91e-38 |
|
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: 144.95 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGSGVP---- 149
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG-EDISGLSEAElyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 GKRVGYMPQEIALYGEFSIQETMMYfgWI---FGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMH 225
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAF--PLrehTRLSEEEIREIVLEKLEAVGLRgAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIwNHLVH-ITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLSI 298
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVI-DDLIRsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
69-297 |
5.40e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.46 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGsgv 148
Cdd:COG1121 2 MMMPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 pgKRVGYMPQEIALYGEF--SIQETMM-----YFGWiFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFA 220
Cdd:COG1121 75 --RRIGYVPQRAEVDWDFpiTVRDVVLmgrygRRGL-FRRPSRADREAVDEALERVGLEDlADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQA--HTIGLMRsgHLLAEESPSVLLS 297
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYfdRVLLLNR--GLVAHGPPEEVLT 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
73-297 |
9.50e-38 |
|
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: 144.03 E-value: 9.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP-GTRGSGVPGK 151
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL-LDGRDlASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEFSIQETMM-----YFGWiFGMETKE-------ILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSF 219
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVAlgrypHLGL-FGRPSAEdreaveeALERTG-LEHLAD-----RPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 220 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
93-237 |
1.21e-37 |
|
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: 140.09 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQETM 172
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLV----KNLSGGQQRRVSFAVALMHDPELLILDEPTV 237
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDlADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
609-787 |
2.41e-37 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 141.11 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 609 FTDFVAPGVILTIVFFLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVVFGVT-N 687
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPlR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 688 NGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVIWPIEGMPVVLRYISLCLPLTLATSSLR 767
Cdd:COG0842 81 GLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALR 160
|
170 180
....*....|....*....|
gi 194201171 768 SILTRGWAILESDVYIGYIL 787
Cdd:COG0842 161 ALFLGGAGLADVWPSLLVLL 180
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
72-311 |
8.75e-37 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 152.97 E-value: 8.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRhafkaYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG---KPGTRGSGV 148
Cdd:NF033858 5 EGVSHR-----YGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmaDARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PgkRVGYMPQEIA--LYGEFSIQETMMYFGWIFGMETKEILERLQFLLN------FLDLPSEKrlvknLSGGQQRRVSFA 220
Cdd:NF033858 76 P--RIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRatglapFADRPAGK-----LSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKA-GQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLSIY 299
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLART 228
|
250
....*....|..
gi 194201171 300 KCISLEEVFLKL 311
Cdd:NF033858 229 GADTLEAAFIAL 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
74-296 |
1.85e-36 |
|
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: 140.13 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNAnqvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYM--DAGEIFVlGGKPGTRGSGVPGK 151
Cdd:cd03295 1 IEFENVTKRYGGGKKA---VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLIepTSGEIFI-DGEDIREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 R-VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEK---RLVKNLSGGQQRRVSFAVALMHDP 227
Cdd:cd03295 75 RkIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfadRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 228 ELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
74-297 |
5.58e-36 |
|
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: 138.23 E-value: 5.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPgTRGSGVPG--K 151
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKD-ITKKNLRElrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQ-------------EIAlygefsiqetmmyFGWI-FGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRR 216
Cdd:COG1122 76 KVGLVFQnpddqlfaptveeDVA-------------FGPEnLGLPREEIRERVEEALELVGLEHlADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 217 VSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVL 295
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
..
gi 194201171 296 LS 297
Cdd:COG1122 222 FS 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
74-289 |
1.30e-35 |
|
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: 136.73 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRV 153
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMeELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHItKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAE 289
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYE 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
71-291 |
2.50e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.33 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 71 QAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSG--- 147
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI-DGQDISSLSErel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 --VPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALM 224
Cdd:COG1136 81 arLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDrLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 225 HDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEES 291
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
76-285 |
4.58e-35 |
|
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: 133.47 E-value: 4.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 76 VRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSGVPGK---R 152
Cdd:cd03229 3 LKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-IDGEDLTDLEDELPPlrrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEFSIQETMMYfgwifgmetkeilerlqfllnfldlpsekrlvkNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIAL---------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGH 285
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
74-286 |
5.93e-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: 134.94 E-value: 5.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG---KPGTRGSGVPG 150
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 KRVGYMPQEIALY-------GEfSIQETMmyfgWIFGMETKEILERLQFLLNFLDLPSEKRLVKN----LSGGQQRRVSF 219
Cdd:cd03257 82 KEIQMVFQDPMSSlnprmtiGE-QIAEPL----RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRypheLSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 220 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
70-295 |
1.83e-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: 137.54 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTrgsGV- 148
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-LDGRDVT---GLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PGKR-VGYMPQEIALYGEFSIQE------TMMyfgwifGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFA 220
Cdd:COG3842 74 PEKRnVGMVFQDYALFPHLTVAEnvafglRMR------GVPKAEIRARVAELLELVGLEGlADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 295
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAlALADRIAVMNDGRIEQVGTPEEI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
73-297 |
5.05e-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: 133.00 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR 152
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEI--ALYGEFSIQETMMYFGWIFGMetKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPE 228
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSflDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
85-285 |
5.74e-34 |
|
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: 129.67 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 85 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQeialyg 164
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 efsiqetmmyfgwifgmetkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 194201171 245 QSIWNHLVHITKAGqKTVIITTHYIEEARQA-HTIGLMRSGH 285
Cdd:cd00267 117 ERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
75-289 |
1.99e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.09 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVG 154
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMPQeialygefsiqetmmyfgwifgmetkeILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:cd03214 77 YVPQ---------------------------ALELLG-LAHLAD-----RPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 235 PTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAE 289
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQ 179
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
429-779 |
3.35e-33 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 133.67 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 429 GVMLFIFALPVMQVILFCLAIG---RDPQGLNLAIVNGEMNDTVREncywedgchFKnlgcRYLSHLNTSVVKTYYEDLD 505
Cdd:pfam12698 2 SFLIITLLLPILLILLLGLIFSnavNDPEELPVAVVDEDNSSLSRQ---------LV----RALEASPTVNLVQYVDSEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 506 DAKEAVRKGTAWGAVYISENFTDafiaranlgrdsDEETIDSSEVKVWLDMSNQQIGVMLNRDIQlAFRDFAMGLLGQCG 585
Cdd:pfam12698 69 EAKEALKNGKIDGLLVIPKGFSK------------DLLKGESATVTVYINSSNLLVSKLILNALQ-SLLQQLNASALVLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 586 SNPKLGDVPIQFRDPIYGTMNPSFTDFVAPgVILTIVFFLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQF 665
Cdd:pfam12698 136 LEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 666 VVMCgqtTLVLIFMLVVFGVT-NNGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVIWPIE 744
Cdd:pfam12698 215 LVGL---LQLLIILLLLFGIGiPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLE 291
|
330 340 350
....*....|....*....|....*....|....*..
gi 194201171 745 GMPVVLRYISLCLPLTLATSSLRSILTR--GWAILES 779
Cdd:pfam12698 292 DPPSFLQWIFSIIPFFSPIDGLLRLIYGdsLWEIAPS 328
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
82-267 |
2.80e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.88 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGSgvpgKRVGYMPQEIA 161
Cdd:cd03235 8 SYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-KPLEKER----KRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 162 LYGEF--SIQETMM-----YFGWIFGMETK------EILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPE 228
Cdd:cd03235 79 IDRDFpiSVRDVVLmglygHKGLFRRLSKAdkakvdEALERVG-LSELAD-----RQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTH 267
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTH 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
72-280 |
4.54e-32 |
|
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: 126.05 E-value: 4.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgK 151
Cdd:COG4133 1 MMLEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEFSIQETMMYFGWIFGMET-----KEILERLQfLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHD 226
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLRAdreaiDEALEAVG-LAGLADLP-----VRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 227 PELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQAHTIGL 280
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARG-GAVLLTTHQPLELAAARVLDL 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
94-308 |
6.72e-32 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 137.56 E-value: 6.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 94 NNLNMTVPKGTIYGLLGASGCGKTT-------LLSCIVGR-----RYMDAGEIfvlggkpGTRgsgvpgKRVGYMPQEIA 161
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASEGEawlfgQPVDAGDI-------ATR------RRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 162 LYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 241 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVF 308
Cdd:NF033858 430 PVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARGAATLEEAF 497
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-297 |
7.04e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.88 E-value: 7.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 32 DPSAIISTDSAMAATnndggtqPNAVAAWGAPANGPRNTQAAVSVRHAFKAYG-KKKNANQVLNNLNMTVPKGTIYGLLG 110
Cdd:COG1123 226 PPEEILAAPQALAAV-------PRLGAARGRAAPAAAAAEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 111 ASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSGVP----GKRVGYMPQ--EIALYGEFSIQETMMYFGWIFGMETK 184
Cdd:COG1123 299 ESGSGKSTLARLLLGLLRPTSGSIL-FDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSR 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 185 -EILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKT 261
Cdd:COG1123 378 aERRERVAELLERVGLPPDlaDRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLT 457
|
250 260 270
....*....|....*....|....*....|....*..
gi 194201171 262 VIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG1123 458 YLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
74-295 |
2.32e-31 |
|
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: 125.04 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTrgsGVP-GKR 152
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL-LDGKDIT---NLPpHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 -VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELL 230
Cdd:cd03300 73 pVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 231 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 295
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
80-286 |
3.77e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 80 FKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgVPG--KRVGYMP 157
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-LDGKPLSAMP-PPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 QEIALYGEfSIQE----TMMYFGWIFGMET-KEILERLQFLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:COG4619 81 QEPALWGG-TVRDnlpfPFQLRERKFDRERaLELLERLGLPPDILDKP-----VERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
74-292 |
3.78e-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: 124.19 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRgsgVPGKR- 152
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL-LDGQDITK---LPMHKr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 ----VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDP 227
Cdd:cd03218 73 arlgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHItHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 228 ELLILDEPTVGVDPLLRQSIwNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESP 292
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTP 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
82-297 |
6.18e-31 |
|
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: 123.31 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRYmdAGEIfVLGGKPGTRGSgvPGKRV----GY 155
Cdd:cd03224 9 GYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPR--SGSI-RFDGRDITGLP--PHERAragiGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 156 MPQEIALYGEFSIQETMMYFGWIFGME-TKEILERLqfLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILD 233
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAkRKARLERV--YELFPRLKErRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGV-TILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
72-299 |
1.92e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.86 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGT-RGSGVPG 150
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 --KRVGYMPQEIALYGEFSIQETMM-----YFGW---IFGMETKE-------ILERLQfLLNFLDlpseKRlVKNLSGGQ 213
Cdd:COG3638 78 lrRRIGMIFQQFNLVPRLSVLTNVLagrlgRTSTwrsLLGLFPPEdreraleALERVG-LADKAY----QR-ADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 214 QRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ--AHTIGLmRSGHLL---- 287
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyaDRIIGL-RDGRVVfdgp 230
|
250
....*....|...
gi 194201171 288 -AEESPSVLLSIY 299
Cdd:COG3638 231 pAELTDAVLREIY 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
74-294 |
4.99e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.93 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgrrYMD----AGEIFVLGGKPGT-RGSGV 148
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLL----YGEerptSGQVLVNGQDLSRlKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PG--KRVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMH 225
Cdd:COG2884 75 PYlrRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDkAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIE--EARQAHTIGLmRSGHLLAEESPSV 294
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLElvDRMPKRVLEL-EDGRLVRDEARGV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
74-292 |
9.29e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 9.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK-------PGTRgs 146
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGRdlftnlpPRER-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 gvpgkRVGYMPQEIALYGEFSIQETmmyfgwI-FGMETK-----EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSF 219
Cdd:COG1118 76 -----RVGFVFQHYALFPHMTVAEN------IaFGLRVRppskaEIRARVEELLELVQLEGlADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 220 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESP 292
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQVGTP 218
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
71-272 |
1.11e-29 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 123.61 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 71 QAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPG 150
Cdd:TIGR03265 2 SPYLSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIY-QGGRDITRLP--PQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 KR-VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPE 228
Cdd:TIGR03265 75 KRdYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPgSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194201171 229 LLILDEPTVGVDPLLRQsiwnHLVHITKAGQK----TVIITTHYIEEA 272
Cdd:TIGR03265 155 LLLLDEPLSALDARVRE----HLRTEIRQLQRrlgvTTIMVTHDQEEA 198
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
83-297 |
1.47e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 121.02 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKK-KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG---KRVGYMPQ 158
Cdd:TIGR04521 10 YQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdlrKKVGLVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 --EIALYGEfSIQETMMyFGWI-FGMETKEILERLQFLLNFLDLPsEKRLVKN---LSGGQQRRVSFAVALMHDPELLIL 232
Cdd:TIGR04521 90 fpEHQLFEE-TVYKDIA-FGPKnLGLSEEEAEERVKEALELVGLD-EEYLERSpfeLSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDvAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
74-289 |
1.49e-29 |
|
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: 119.61 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpGTRGSGVPGK-- 151
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD----GTDLTLLSGKel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 -----RVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLpSEKR--LVKNLSGGQQRRVSFAVALM 224
Cdd:cd03258 78 rkarrRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKAdaYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 225 HDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
74-284 |
3.23e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 118.13 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKR- 152
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI-GGRDVTDLP--PKDRd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLlDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 232 LDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH-YIEEARQAHTIGLMRSG 284
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDG 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
75-293 |
6.92e-29 |
|
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: 117.92 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTrgsgvpgkrvG 154
Cdd:cd03219 2 EVRGLTKRFGGLV----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGEDIT----------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMPQEIA------------LYGEFSIQETMM----------YFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSG 211
Cdd:cd03219 67 LPPHEIArlgigrtfqiprLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLaDLADRPAGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 212 GQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEE 290
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
...
gi 194201171 291 SPS 293
Cdd:cd03219 226 TPD 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
95-288 |
9.30e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 116.63 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 95 NLNMTVPKGTIyGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP---GTRGSGVP--GKRVGYMPQEIALYGEFSIQ 169
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTI-VLNGTVlfdSRKKINLPpqQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 170 ETMmyfgwIFGMETKEILERLQF---LLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 245
Cdd:cd03297 94 ENL-----AFGLKRKRNREDRISvdeLLDLLGLdHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 194201171 246 SIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLA 288
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQY 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
72-287 |
1.08e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.56 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGK 151
Cdd:COG3839 2 ASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-IGGRDVTDLP--PKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 R-VGYMPQEIALYGEFSIQETMMyfgwiFGME------------TKEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVS 218
Cdd:COG3839 75 RnIAMVFQSYALYPHMTVYENIA-----FPLKlrkvpkaeidrrVREAAELLG-LEDLLD-----RKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 219 FAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLL 287
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQ 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
88-285 |
1.35e-28 |
|
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: 114.79 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGS-GVPGKRVGYMPQEIALYGEf 166
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-IDGVDLRDLDlESLRKNIAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQEtmmyfgwifgmetkeilerlqfllnfldlpsekrlvkN-LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 245
Cdd:cd03228 91 TIRE-------------------------------------NiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 194201171 246 SIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGH 285
Cdd:cd03228 134 LILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
84-267 |
3.91e-28 |
|
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: 115.45 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 84 GKKKNAN---QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR---RYMDAGEIFVlGGKPGTRGSgVPgKRVGYMP 157
Cdd:cd03234 11 LKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILF-NGQPRKPDQ-FQ-KCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 QEIALYGEFSIQETMmYFGWIFGM---ETKEILERL--QFLLNFL-DLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:cd03234 88 QDDILLPGLTVRETL-TYTAILRLprkSSDAIRKKRveDVLLRDLaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 194201171 232 LDEPTVGVDPLLRqsiwNHLVHITK---AGQKTVIITTH 267
Cdd:cd03234 167 LDEPTSGLDSFTA----LNLVSTLSqlaRRNRIVILTIH 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
91-267 |
5.60e-28 |
|
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: 113.80 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR--YMDAGEIFVlGGKPgtRGSGVPGKRVGYMPQEIALYGEFSI 168
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLI-NGRP--LDKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMMYfgwifgmeTKEIlerlqfllnfldlpsekrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIW 248
Cdd:cd03213 100 RETLMF--------AAKL--------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*....
gi 194201171 249 NHLVHITKAGqKTVIITTH 267
Cdd:cd03213 152 SLLRRLADTG-RTIICSIH 169
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
74-288 |
6.39e-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: 115.57 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRhafkaYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRY-MDAGEIFVLGGKPGT------Rgs 146
Cdd:COG1119 9 VTVR-----RGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGedvwelR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 gvpgKRVGYMPQEIALY--GEFSIQETMM--YFGWI--FGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSF 219
Cdd:COG1119 78 ----KRIGLVSPALQLRfpRDETVLDVVLsgFFDSIglYREPTDEQRERARELLELLGLAHlADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 220 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQA--HTIgLMRSGHLLA 288
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGitHVL-LLKDGRVVA 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
75-289 |
8.75e-28 |
|
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: 114.74 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKaygKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVG 154
Cdd:cd03267 22 SLKSLFK---RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-RRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 Y-MPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03267 98 VvFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAE 289
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYD 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
76-295 |
2.40e-27 |
|
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: 113.43 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 76 VRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgTRGSGVPGK---- 151
Cdd:cd03256 3 VENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG----TDINKLKGKalrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 ---RVGYMPQEIALYGEFSIQE--------TMMYFGWIFGMETKEILERLQFLLNFLDLpSEK--RLVKNLSGGQQRRVS 218
Cdd:cd03256 76 lrrQIGMIFQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGL-LDKayQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 219 FAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ--AHTIGLmRSGHLLAEESPSVL 295
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyaDRIVGL-KDGRIVFDGPPAEL 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
74-293 |
4.04e-27 |
|
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: 112.66 E-value: 4.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC-------IVGRRymDAGEIFVLGGKPGTRGS 146
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrlndlIPGAP--DEGEVLLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 GVPG--KRVGYMPQEIALYgEFSIQETMMYFGWIFGMETKEIL-ERLQFLLNFLDLPSEkrlVKN------LSGGQQRRV 217
Cdd:cd03260 75 DVLElrRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDE---VKDrlhalgLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 218 SFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHItkAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLaEESPS 293
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAaRVADRTAFLLNGRLV-EFGPT 224
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
73-271 |
5.01e-27 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 114.49 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKR 152
Cdd:TIGR03522 2 SIRVSSLTKLYGTQN----ALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQ-RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:TIGR03522 77 IGYLPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLrPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 194201171 232 LDEPTVGVDPllrqsiwNHLVHITK-----AGQKTVIITTHYIEE 271
Cdd:TIGR03522 157 LDEPTTGLDP-------NQLVEIRNvikniGKDKTIILSTHIMQE 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
89-297 |
6.48e-27 |
|
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: 118.47 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 89 ANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---RRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQE-----I 160
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGRRIGMVFQDpmtqlN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMyfgwIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 239
Cdd:COG1123 98 PVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERrLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 240 DPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG1123 174 DVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
601-769 |
1.26e-26 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 110.44 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 601 IYGTMNPSFTDFVAPGVILTIVFFLAV-ALTSSALIIERTEGLLDRSWVAGV-SPFEILFSHVITQFVVMCGQTTLVLIF 678
Cdd:pfam01061 33 LFGNLGNQQGGLNRPGLLFFSILFNAFsALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 679 MLVVFGVT-NNGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVIWPIEGMPVVLRYISLCL 757
Cdd:pfam01061 113 VYFMVGLPpSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLN 192
|
170
....*....|..
gi 194201171 758 PLTLATSSLRSI 769
Cdd:pfam01061 193 PLTYAIEALRAN 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
72-272 |
1.54e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.88 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGK 151
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-TLDGVPVTG----PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEFSIQETMMyFGWIF-GMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPEL 229
Cdd:COG4525 77 DRGVVFQKDALLPWLNVLDNVA-FGLRLrGVPKAERRARAEELLALVGLADfARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 194201171 230 LILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 272
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
76-287 |
1.68e-26 |
|
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: 111.97 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 76 VRHAFKAYGKKKNANQVL---------NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGS 146
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILkktgqtvgvNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-DGQDIAAMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 -----GVPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFA 220
Cdd:cd03294 93 rkelrELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLeGWEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLL 287
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRLV 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
75-297 |
1.78e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.89 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRgsgVP-GKR- 152
Cdd:COG1137 5 EAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF-LDGEDITH---LPmHKRa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 ---VGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLpseKRLVKN----LSGGQQRRVSFAVALMH 225
Cdd:COG1137 77 rlgIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI---THLRKSkaysLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEarqahTIG------LMRSGHLLAEESPSVLLS 297
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGI-GVLITDHNVRE-----TLGicdrayIISEGKVLAEGTPEEILN 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
81-299 |
1.95e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 111.24 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPG-TRGSGVPG--KRVGYMP 157
Cdd:TIGR02315 9 KVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITkLRGKKLRKlrRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 QEIALYGEFSIQETM------------MYFGWIFGMETKEILERLQfLLNFLDLPSEKrlVKNLSGGQQRRVSFAVALMH 225
Cdd:TIGR02315 86 QHYNLIERLTVLENVlhgrlgykptwrSLLGRFSEEDKERALSALE-RVGLADKAYQR--ADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ--AHTIGLmRSGHLLAEESPS-----VLLSI 298
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyaDRIVGL-KAGEIVFDGAPSelddeVLRHI 241
|
.
gi 194201171 299 Y 299
Cdd:TIGR02315 242 Y 242
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
70-267 |
4.34e-26 |
|
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: 110.51 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP--GTRGSG 147
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDGRDitGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 VPGKRVGYMPQEIALYGEFSIQETMM----------YFGWIFGM-----ETKEILERLQFLLNFLDLpSEKR--LVKNLS 210
Cdd:COG0411 76 IARLGIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLprarrEEREARERAEELLERVGL-ADRAdePAGNLS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 211 GGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH 267
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
85-286 |
1.58e-25 |
|
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: 108.19 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 85 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR-VGYMPQEIALY 163
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL-LNGKDITNLP--PEKRdISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 164 GEFSIQETMMYfgwifGM------------ETKEILERLQF--LLNfldlpsekRLVKNLSGGQQRRVSFAVALMHDPEL 229
Cdd:cd03299 84 PHMTVYKNIAY-----GLkkrkvdkkeierKVLEIAEMLGIdhLLN--------RKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 230 LILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKL 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
73-286 |
2.10e-25 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 107.81 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRgSGVPGKR 152
Cdd:cd03296 2 SIEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL-FGGEDATD-VPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEFSIQETMMyfgwiFGMETK---------EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVA 222
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVA-----FGLRVKprserppeaEIRAKVHELLKLVQLDWlADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 223 LMHDPELLILDEPTVGVDPLLRQSI--W----NHLVHITkagqkTVIItTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELrrWlrrlHDELHVT-----TVFV-THDQEEALEvADRVVVMNKGRI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
83-284 |
1.06e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 104.65 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKKKNanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRYMdaGEIFvLGGKPgtRGSGVPGKRVGYMPQEI 160
Cdd:cd03226 9 YKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKESS--GSIL-LNGKP--IKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 --ALYGEFSIQEtmMYFGwifGMETKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTV 237
Cdd:cd03226 81 dyQLFTDSVREE--LLLG---LKELDAGNEQAETVLKDLDLYALKeRHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194201171 238 GVDPLLRQSIWNHLVHITKAGqKTVIITTHYIE-EARQAHTIGLMRSG 284
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQG-KAVIVITHDYEfLAKVCDRVLLLANG 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
74-295 |
1.08e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.04 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgVPGKRV 153
Cdd:PRK11432 7 VVLKNITKRFGS----NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDVTHRS-IQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGfEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 295
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
81-251 |
1.87e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtrgsgvPGKRVGYMPQEI 160
Cdd:COG0488 6 KSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----------KGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMM---------------------------------------YFGWIFGMETKEILERLQFLLNFLDlps 201
Cdd:COG0488 71 PLDDDLTVLDTVLdgdaelraleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARAEEILSGLGFPEEDLD--- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 194201171 202 ekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTvgvdpllrqsiwNHL 251
Cdd:COG0488 148 --RPVSELSGGWRRRVALARALLSEPDLLLLDEPT------------NHL 183
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
74-286 |
2.08e-24 |
|
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: 104.15 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--K 151
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEFSIQETMMyFG--WIFGM-------ETKEILERLQfLLNFLD-LPSEkrlvknLSGGQQRRVSFAV 221
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENIT-LApiKVKGMskaeaeeRALELLEKVG-LADKADaYPAQ------LSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 222 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGM-TMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
53-297 |
2.50e-24 |
|
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: 111.39 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 53 QPNAVAAWGAPANgPRNTQAAVSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAG 132
Cdd:COG4988 317 APEPAAPAGTAPL-PAAGPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 133 EIFVlGGKPGTRGSGVP-GKRVGYMPQE-----------IALYGEFSIQETMMyfgwifgmetkEILERLQfLLNFLD-L 199
Cdd:COG4988 393 SILI-NGVDLSDLDPASwRRQIAWVPQNpylfagtirenLRLGRPDASDEELE-----------AALEAAG-LDEFVAaL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 200 PS--EKRL---VKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQ 274
Cdd:COG4988 460 PDglDTPLgegGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ 537
|
250 260
....*....|....*....|...
gi 194201171 275 AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLA 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
53-296 |
3.50e-24 |
|
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: 110.63 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 53 QPNAVAAWGAPANGPrnTQAAVSVRHAFKAYGKkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAG 132
Cdd:COG4987 315 APPAVTEPAEPAPAP--GGPSLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 133 EIfVLGGKPGTRGSGV-PGKRVGYMPQEIalygefsiqetmmyfgWIFGM----------------ETKEILERLQfLLN 195
Cdd:COG4987 391 SI-TLGGVDLRDLDEDdLRRRIAVVPQRP----------------HLFDTtlrenlrlarpdatdeELWAALERVG-LGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 196 FLD-LPS--EKRLV---KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYI 269
Cdd:COG4987 453 WLAaLPDglDTWLGeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL 530
|
250 260
....*....|....*....|....*..
gi 194201171 270 EEARQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
82-297 |
3.95e-24 |
|
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: 104.29 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRYmdAGEIfVLGGKPGTRGSgvPGKRV----GY 155
Cdd:COG0410 12 GYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGllPPR--SGSI-RFDGEDITGLP--PHRIArlgiGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 156 MPQEIALYGEFSIQETMMyFGWIFGMETKEILERLQFLLN-FLDLpSEKR--LVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:COG0410 83 VPEGRRIFPSLTVEENLL-LGAYARRDRAEVRADLERVYElFPRL-KERRrqRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGV-TILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
82-291 |
4.20e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 103.76 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKRV----GYMP 157
Cdd:TIGR03410 9 YYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI-RLDGEDITKLP--PHERAragiAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 QEIALYGEFSIQETMMyfgwiFGMET---------KEILERLQFLLNFLdlpseKRLVKNLSGGQQRRVSFAVALMHDPE 228
Cdd:TIGR03410 82 QGREIFPRLTVEENLL-----TGLAAlprrsrkipDEIYELFPVLKEML-----GRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEES 291
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
74-251 |
5.29e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgTRGSGVpgkRV 153
Cdd:COG0488 316 LELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV---KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQE-IALYGEFSIQETMMYfgwifGMETKEILERLQFLLNFLdLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELL 230
Cdd:COG0488 381 GYFDQHqEELDPDKTVLDELRD-----GAPGGTEQEVRGYLGRFL-FSGDDafKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180
....*....|....*....|.
gi 194201171 231 ILDEPTvgvdpllrqsiwNHL 251
Cdd:COG0488 455 LLDEPT------------NHL 463
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
80-319 |
2.96e-23 |
|
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: 110.10 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 80 FKAYGKKknanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRVGYMPQE 159
Cdd:TIGR01257 938 FEPSGRP-----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV-GGKDIETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 160 IALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 239 VDPLLRQSIWNHLVHItKAGqKTVIITTHYIEEAR-QAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVFLKLSRIQSQ 317
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKY-RSG-RTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQ 1169
|
..
gi 194201171 318 KG 319
Cdd:TIGR01257 1170 RG 1171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-293 |
3.10e-23 |
|
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: 103.98 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---RRYMDAGEIFVLG----GKPGTRGS 146
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGedllKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 GVPGKRVGYMPQE----------IalyGEfSIQETMMYFGwifGMETKEILERLQFLLNFLDLPSEKRLVKN----LSGG 212
Cdd:COG0444 82 KIRGREIQMIFQDpmtslnpvmtV---GD-QIAEPLRIHG---GLSKAEARERAIELLERVGLPDPERRLDRypheLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 213 QQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHlLAEES 291
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVMYAGR-IVEEG 233
|
..
gi 194201171 292 PS 293
Cdd:COG0444 234 PV 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
92-286 |
3.54e-23 |
|
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: 99.43 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR----VGYMP---QEIALYG 164
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT-LDGKPVTRRS--PRDAiragIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EFSIQETMmyfgwifgmetkeILERLqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:cd03215 92 DLSVAENI-------------ALSSL------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 194201171 245 QSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:cd03215 141 AEIYRLIRELADAG-KAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
80-297 |
4.12e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 101.32 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 80 FKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR--VGYMP 157
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 QEIALYGEFSIQETMMyFGWIF--GMETKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSFAVALMHDPE 228
Cdd:PRK09493 84 QQFYLFPHLTALENVM-FGPLRvrGASKEEAEKQARELLAKVGLaerahhyPSE------LSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHT-IGLMRSGHLLAEESPSVLLS 297
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGM-TMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIK 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
75-292 |
4.14e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 101.20 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGT---------RG 145
Cdd:TIGR04406 3 VAENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL-IDGQDIThlpmherarLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 146 sgvpgkrVGYMPQEIALYGEFSIQETMMYFgwifgMETKEIL---ERLQFLLNFLDLPSEKRLVKN----LSGGQQRRVS 218
Cdd:TIGR04406 78 -------IGYLPQEASIFRKLTVEENIMAV-----LEIRKDLdraEREERLEALLEEFQISHLRDNkamsLSGGERRRVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 219 FAVALMHDPELLILDEPTVGVDPLLRQSIWNhLVHITKAGQKTVIITTHYIEEarqahTIG------LMRSGHLLAEESP 292
Cdd:TIGR04406 146 IARALATNPKFILLDEPFAGVDPIAVGDIKK-IIKHLKERGIGVLITDHNVRE-----TLDicdrayIISDGKVLAEGTP 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
74-284 |
4.66e-23 |
|
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: 99.85 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHA-FKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgsgvpGKR 152
Cdd:cd03250 1 ISVEDAsFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQEIALYGEfSIQETMmyfgwIFGME-----TKEILERLQFLLNFLDLPS-------EKRLvkNLSGGQQRRVSFA 220
Cdd:cd03250 68 IAYVSQEPWIQNG-TIRENI-----LFGKPfdeerYEKVIKACALEPDLEILPDgdlteigEKGI--NLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSG 284
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
93-267 |
7.21e-23 |
|
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: 99.79 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGKRVGYMPQEIAL-YGEF----- 166
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV----NGQDVSDLRGRAIPYLRRKIGVvFQDFrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 -SIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEKR-LVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:cd03292 93 rNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|...
gi 194201171 245 QSIWNHLVHITKAGqKTVIITTH 267
Cdd:cd03292 173 WEIMNLLKKINKAG-TTVVVATH 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
73-284 |
1.96e-22 |
|
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: 97.29 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAfkaygkkKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP-GTRGSGVPGK 151
Cdd:cd03246 5 NVSFRYP-------GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-RLDGADiSQWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEfSIQETMmyfgwifgmetkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLI 231
Cdd:cd03246 77 HVGYLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 232 LDEPTVGVDPLLRQSIwNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSG 284
Cdd:cd03246 120 LDEPNSHLDVEGERAL-NQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
108-292 |
3.50e-22 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 101.03 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 108 LLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgVPGKR--VGYMPQEIALYGEFSIQETMMYFGWIFGMETKE 185
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI-MLDGEDVTN---VPPHLrhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 186 ILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVII 264
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEfADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180
....*....|....*....|....*....
gi 194201171 265 TTHYIEEA-RQAHTIGLMRSGHLLAEESP 292
Cdd:TIGR01187 157 VTHDQEEAmTMSDRIAIMRKGKIAQIGTP 185
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
96-297 |
4.57e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 101.34 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 96 LNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGV---PGKR-VGYMPQEIALYGEFSIQET 171
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflpPEKRrIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 MMYFGW-IFGMETKEILERLQFLLNfLDlPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNH 250
Cdd:TIGR02142 96 LRYGMKrARPSERRISFERVIELLG-IG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194201171 251 LVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
74-297 |
5.55e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.14 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--K 151
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 RVGYMPQEIALYGEFSIQETMMYfG--WIFGMETKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSFAVA 222
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLadkadayPAQ------LSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 223 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGM-TMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
83-289 |
8.58e-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: 95.46 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYMPQEIAL 162
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDGVPVSDLEKALSSLISVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YGEfSIQETmmyfgwifgmetkeilerlqfllnfldlpsekrLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 242
Cdd:cd03247 87 FDT-TLRNN---------------------------------LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 194201171 243 LRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 289
Cdd:cd03247 133 TERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
70-289 |
8.93e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.40 E-value: 8.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvP 149
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-LDGEPVRFRS--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 G----KRVGYMPQEIALYGEFSIQETMMY------FGWI--FGM--ETKEILERLQfllnfLDLPSEkRLVKNLSGGQQR 215
Cdd:COG1129 74 RdaqaAGIAIIHQELNLVPNLSVAENIFLgreprrGGLIdwRAMrrRARELLARLG-----LDIDPD-TPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 216 RVSFAVALMHDPELLILDEPT-----VGVDPLLRqsiwnhLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTaslteREVERLFR------IIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGT 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
75-271 |
9.01e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.39 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKAYGKKKNAnqvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRgsgvpgkRVG 154
Cdd:COG4586 23 ALKGLFRREYREVEA---VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-------RKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMpQEIA--------LYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMH 225
Cdd:COG4586 93 FA-RRIGvvfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLgELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHY---IEE 271
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddIEA 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
74-292 |
9.11e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTrgsGVPG-KR 152
Cdd:PRK09452 15 VELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-LDGQDIT---HVPAeNR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 -VGYMPQEIALYGEFSIQETMMyfgwiFGMETK-----EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMH 225
Cdd:PRK09452 87 hVNTVFQSYALFPHMTVFENVA-----FGLRMQktpaaEITPRVMEALRMVQLEEfAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLvhitKAGQKTVIIT----THYIEEA-----RqahtIGLMRSGHLLAEESP 292
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNEL----KALQRKLGITfvfvTHDQEEAltmsdR----IVVMRDGRIEQDGTP 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
67-297 |
1.19e-21 |
|
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: 103.76 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYGKkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGT--- 143
Cdd:COG2274 467 LPRLKGDIELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGIDLRqid 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 144 ----RgsgvpgKRVGYMPQEIAL-YGefSIQETMMYFGWIFGMEtkEILERLQF--LLNFLD-LP-------SEKrlVKN 208
Cdd:COG2274 544 paslR------RQIGVVLQDVFLfSG--TIRENITLGDPDATDE--EIIEAARLagLHDFIEaLPmgydtvvGEG--GSN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 209 LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLA 288
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
....*....
gi 194201171 289 EESPSVLLS 297
Cdd:COG2274 690 DGTHEELLA 698
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
74-289 |
1.57e-21 |
|
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: 94.42 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvpgkrv 153
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEVSFAS------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 gymPQE-IALygefsiqetmmyfgwifGMETkeilerlqfllnfldlpsekrlVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:cd03216 69 ---PRDaRRA-----------------GIAM----------------------VYQLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
73-287 |
3.08e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.85 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLscivgrRYMD------------AGEIFVLGGK 140
Cdd:PRK11124 2 SIQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLL------RVLNllemprsgtlniAGNHFDFSKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 141 PGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMYFGW-IFGM-------ETKEILERLQfLLNFLDlpsekRLVKNLSGG 212
Cdd:PRK11124 72 PSDKAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLskdqalaRAEKLLERLR-LKPYAD-----RFPLHLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 213 QQRRVSFAVALMHDPELLILDEPTVGVDPllrqSIWNHLVHITKAGQKTVI---ITTHYIEEARQAHT-IGLMRSGHLL 287
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDP----EITAQIVSIIRELAETGItqvIVTHEVEVARKTASrVVYMENGHIV 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
93-314 |
3.14e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--KRVGYMPQeialYGEFSIQE 170
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirKKVGLVFQ----YPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 171 TMMY----FGWI-FGMETKEILERLQFLLNFLDLPSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 242
Cdd:PRK13637 99 ETIEkdiaFGPInLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 243 LRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSvllSIYKCIS-LEEVFLKLSRI 314
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPR---EVFKEVEtLESIGLAVPQV 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
92-272 |
3.57e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.31 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGKRVGYMPQEIALYGEFSIQET 171
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-TLDGKPVEG----PGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 MMYFGWIFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNH 250
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKVGLEgAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170 180
....*....|....*....|..
gi 194201171 251 LVHITKAGQKTVIITTHYIEEA 272
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDIEEA 192
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
74-295 |
1.01e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFV-------LGGKP--GTR 144
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltaLSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 145 gsgvpgKRVGYMPQ------------------EIAlygefsiqetmmyfgwifGMETKEILERLQFLLNFLDL------- 199
Cdd:COG1135 82 ------RKIGMIFQhfnllssrtvaenvalplEIA------------------GVPKAEIRKRVAELLELVGLsdkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 200 PSEkrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTI 278
Cdd:COG1135 138 PSQ------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRV 211
|
250
....*....|....*..
gi 194201171 279 GLMRSGHLLaeESPSVL 295
Cdd:COG1135 212 AVLENGRIV--EQGPVL 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
73-287 |
1.01e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLscivgrRYMD------------AGEIFVLGGK 140
Cdd:COG4161 2 SIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLL------RVLNlletpdsgqlniAGHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 141 PGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMYFG-WIFGMETKEILERLQFLLNFLDLpSEK--RLVKNLSGGQQRRV 217
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRL-TDKadRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 218 SFAVALMHDPELLILDEPTVGVDPllrqSIWNHLVHITKAGQKTVI---ITTHYIEEARQ-AHTIGLMRSGHLL 287
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDP----EITAQVVEIIRELSQTGItqvIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
88-275 |
1.07e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgTRGsgvPGKRVGYMPQEIALYGEF- 166
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRA---GGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 -SIQETMMYFGW----IFGMETKE-------ILERLQFLlnflDLpsEKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:NF040873 72 lTVRDLVAMGRWarrgLWRRLTRDdraavddALERVGLA----DL--AGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 194201171 235 PTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQA 275
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRRA 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
81-297 |
2.10e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.42 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR-VGYMPQE 159
Cdd:PRK10895 11 KAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 160 IALYGEFSIQETMMYFgwifgMETKEILERLQFLLNFLDLPSE-------KRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:PRK10895 87 ASIFRRLSVYDNLMAV-----LQIRDDLSAEQREDRANELMEEfhiehlrDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKtVIITTHYIEEA----RQAHTIGlmrSGHLLAEESPSVLLS 297
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLG-VLITDHNVRETlavcERAYIVS---QGHLIAHGTPTEILQ 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
74-267 |
2.10e-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: 90.20 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgTRGSGVpgkRV 153
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTV---KI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQeialygefsiqetmmyfgwifgmetkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILD 233
Cdd:cd03221 66 GYFEQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|....
gi 194201171 234 EPTVGVDPLLRQSIWNHLvhitKAGQKTVIITTH 267
Cdd:cd03221 96 EPTNHLDLESIEALEEAL----KEYPGTVILVSH 125
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
82-297 |
3.09e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.54 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP-GTRGSGVPGKRVGYMPQEI 160
Cdd:PRK11231 11 GYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-LGDKPiSMLSSRQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMY--------FGWIFGMETKEI---LERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPEL 229
Cdd:PRK11231 86 LTPEGITVRELVAYgrspwlslWGRLSAEDNARVnqaMEQTR-INHLAD-----RRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 230 LILDEPTVGVDpLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK11231 160 VLLDEPTTYLD-INHQVELMRLMRELNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
92-289 |
3.48e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPG----KRVGYMP---QEIALYG 164
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR-LDGKPVRIRS--PRdairAGIAYVPedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EFSIQETMMY--------FGWIFGMETKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:COG1129 344 DLSIRENITLasldrlsrGGLLDRRRERALAEEYIKRLR-IKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 237 VGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGlSDRILVMREGRIVGE 475
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
76-284 |
5.41e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 76 VRHAFKAYgkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKR-VG 154
Cdd:PRK11607 22 IRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHVP--PYQRpIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMPQEIALYGEFSIQETMMyfgwiFGMETK-----EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPE 228
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIA-----FGLKQDklpkaEIASRVNEMLGLVHMQEfAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSG 284
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRG 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
74-297 |
7.90e-20 |
|
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: 91.52 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKNAnqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgRRY-MDAGEIFVLGGKpgTRGSGVPGKR 152
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYdVDSGRILIDGHD--VRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 --VGYMPQEIALYGEfSIQETMMYfgWIFGMETKEILERLQ------FLLNF---LDLPSEKRLVKnLSGGQQRRVSFAV 221
Cdd:cd03251 76 rqIGLVSQDVFLFND-TVAENIAY--GRPGATREEVEEAARaanaheFIMELpegYDTVIGERGVK-LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 222 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
93-271 |
1.08e-19 |
|
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: 98.16 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVpGKRVGYMPQEIALYGEFSIQETM 172
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-HQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHL 251
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSlYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|
gi 194201171 252 VHITKAGqKTVIITTHYIEE 271
Cdd:TIGR01257 2114 VSIIREG-RAVVLTSHSMEE 2132
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
69-293 |
2.61e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGKKKnANqvlNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgv 148
Cdd:COG3845 1 MMPPALELRGITKRFGGVV-AN---DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DGKPVRIRS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PGK----RVGYMPQEIALYGEFSIQETMMY-----FGWIFGM-----ETKEILERLQFllnFLDLpseKRLVKNLSGGQQ 214
Cdd:COG3845 74 PRDaialGIGMVHQHFMLVPNLTVAENIVLgleptKGGRLDRkaaraRIRELSERYGL---DVDP---DAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 215 RRVSFAVALMHDPELLILDEPTVGVDP--------LLRQsiwnhlvhITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGH 285
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPqeadelfeILRR--------LAAEG-KSIIFITHKLREVMAiADRVTVLRRGK 218
|
....*...
gi 194201171 286 LLAEESPS 293
Cdd:COG3845 219 VVGTVDTA 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
69-316 |
2.64e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.21 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGKKKNanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGV 148
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PGKRVGYMPQE-----IALYGEFSIQetmmyfgwiFGMETK--------EILERLQF---LLNFLDLPSEkrlvkNLSGG 212
Cdd:PRK13632 81 IRKKIGIIFQNpdnqfIGATVEDDIA---------FGLENKkvppkkmkDIIDDLAKkvgMEDYLDKEPQ-----NLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 213 QQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESP 292
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
250 260
....*....|....*....|....
gi 194201171 293 SVLLSiykcislEEVFLKLSRIQS 316
Cdd:PRK13632 227 KEILN-------NKEILEKAKIDS 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
41-278 |
3.75e-19 |
|
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: 94.66 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 41 SAMAATNNDGGTQPNAVAAWGAPANGPRNTQAAVSVRHAfkaygkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLL 120
Cdd:TIGR02857 294 AEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYP--------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 121 SCIVGRRYMDAGEIfVLGGKPGTRGS-GVPGKRVGYMPQEIALYgEFSIQETM-MYFGWIFGMETKEILER--LQFLLNF 196
Cdd:TIGR02857 366 NLLLGFVDPTEGSI-AVNGVPLADADaDSWRDQIAWVPQHPFLF-AGTIAENIrLARPDASDAEIREALERagLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 197 LDLPSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHItkAGQKTVIITTHYIEEAR 273
Cdd:TIGR02857 444 LPQGLDTPIGEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAA 521
|
....*
gi 194201171 274 QAHTI 278
Cdd:TIGR02857 522 LADRI 526
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
47-267 |
4.31e-19 |
|
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: 94.35 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 47 NNDGGTQPNAVAAWGAPANGPRNTQAAVSVRHAfkaygkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR 126
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP--------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 127 RYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEfSIQETMMYF-GWIFGMETKEILERLQfLLNFLD-LPS--E 202
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT-TVRENLRLArPDATDEELWAALERVG-LADWLRaLPDglD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 203 KRLV---KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIwnhLVHITKAGQ-KTVIITTH 267
Cdd:TIGR02868 463 TVLGeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITH 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
91-267 |
9.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEI----------------------FVLGGKPGTRGSGV 148
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvlekLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PG--KRVGYMPQ--EIALYgEFSIQETMMyFGWI-FGMETKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAV 221
Cdd:PRK13651 101 KEirRRVGVVFQfaEYQLF-EQTIEKDII-FGPVsMGVSKEEAKKRAAKYIELVGLDESylQRSPFELSGGQKRRVALAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 194201171 222 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTH 267
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTH 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
67-267 |
9.38e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 9.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRY--MDAGEIFVLGGKPgtR 144
Cdd:TIGR00955 15 AQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgVKGSGSVLLNGMP--I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 145 GSGVPGKRVGYMPQEIALYGEFSIQETMMyFGWIFGME----TKEILERLQFLLNFLDLPS-------EKRLVKNLSGGQ 213
Cdd:TIGR00955 93 DAKEMRAISAYVQQDDLFIPTLTVREHLM-FQAHLRMPrrvtKKEKRERVDEVLQALGLRKcantrigVPGRVKGLSGGE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 214 QRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTH 267
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIH 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
72-272 |
1.02e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKpgtRGSGV-PG 150
Cdd:PRK11000 2 ASVTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEK---RMNDVpPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 KR-VGYMPQEIALYGEFSIQETMMyFGW-IFGMETKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDP 227
Cdd:PRK11000 74 ERgVGMVFQSYALYPHLSVAENMS-FGLkLAGAKKEEINQRVNQVAEVLQLAHLlDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 194201171 228 ELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 272
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEA 197
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
91-315 |
1.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.68 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlgGKPGTRGSGVPGKRVGYMPQEIALYGEFS--- 167
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDYAIPANLKKIKEVKRLRKEIGLVFQFPeyq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 168 -IQETM---MYFGWI-FGMETKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:PRK13645 103 lFQETIekdIAFGPVnLGENKQEAYKKVPELLKLVQLPEDyvKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 241 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPsvlLSIYKCISLeevflkLSRIQ 315
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP---FEIFSNQEL------LTKIE 249
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
93-310 |
1.48e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK---PGTRGSGVPG--KRVGYMPQ--EIALYge 165
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGERvitAGKKNKKLKPlrKKVGIVFQfpEHQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 fsiQETM---MYFGWI-FGMETKEILERLQFLLNFLDLPsEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:PRK13634 100 ---EETVekdICFGPMnFGVSEEDAKQKAREMIELVGLP-EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 239 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPsvllsiykcislEEVFLK 310
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDaARYADQIVVMHKGTVFLQGTP------------REIFAD 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
91-290 |
1.98e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.20 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtRGSGVPGKRVGYMPqeialygEFSIQE 170
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGLGGGFNP-------ELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 171 TMMYFGWIFGMETKEILERLQF------LLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEiiefseLGDFIDLP-----VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 194201171 245 QSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEE 290
Cdd:cd03220 179 EKCQRRLRELLKQG-KTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
95-298 |
2.54e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.12 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 95 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIQETMm 173
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL-WNGQDLTALP--PAERpVSMLFQENNLFPHLTVAQNI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 174 YFGWIFGM--------ETKEILERLQfLLNFLD-LPSEkrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:COG3840 93 GLGLRPGLkltaeqraQVEQALERVG-LAGLLDrLPGQ------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 245 QSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLSI 298
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
74-297 |
3.62e-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: 87.55 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAY------GKKKNAnQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSG 147
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfGAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS-FRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 VPGKRVGYMPQEI--ALYGEFSIQETMmyfGWIFG--------METKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQR 215
Cdd:TIGR02769 81 KQRRAFRRDVQLVfqDSPSAVNPRMTV---RQIIGeplrhltsLDESEQKARIAELLDMVGLRSEdaDKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 216 RVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSV 294
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQ 237
|
...
gi 194201171 295 LLS 297
Cdd:TIGR02769 238 LLS 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
93-297 |
5.00e-18 |
|
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: 91.02 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG-------KPGTRGSGVPGKRVGYMPQEIALYGE 165
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmtKPGPDGRGRAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 FSIQETM-----MYFGWIFGM---------------ETKEILERlqfllnfldLPSEkrlvknLSGGQQRRVSFAVALMH 225
Cdd:TIGR03269 380 RTVLDNLteaigLELPDELARmkavitlkmvgfdeeKAEEILDK---------YPDE------LSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
61-296 |
1.29e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.22 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 61 GAPANGPRNTQAAVSVRH-AFkAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMD--AGEIFVl 137
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENvSF-SYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL--RFYDptSGRILI- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 138 GGKPGT-------RgsgvpgKRVGYMPQEIALYgEFSIQETMMYfgwifGMET---KEILE--RLQFLLNFLD-LPS--- 201
Cdd:COG1132 400 DGVDIRdltleslR------RQIGVVPQDTFLF-SGTIRENIRY-----GRPDatdEEVEEaaKAAQAHEFIEaLPDgyd 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 202 ---EKRLVkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTI 278
Cdd:COG1132 468 tvvGERGV-NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRI 544
|
250
....*....|....*...
gi 194201171 279 GLMRSGHLLAEESPSVLL 296
Cdd:COG1132 545 LVLDDGRIVEQGTHEELL 562
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
64-289 |
1.42e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 87.87 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 64 ANGPRNtqaAVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCG--KTTLLSCIVGRrymDAGEifvlggKP 141
Cdd:NF000106 7 SNGARN---AVEVRGLVKHFGEVK----AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP---DAGR------RP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 142 GTRGSGVPGKRV------GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQ 214
Cdd:NF000106 71 WRF*TWCANRRAlrrtig*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTeAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 215 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG-ATVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
83-296 |
1.64e-17 |
|
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: 84.58 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGK----RVGYMPQ 158
Cdd:cd03254 12 YDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI----DGIDIRDISRKslrsMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 EIALYGEfSIQETMMYFGWIFGMETKEILERLQFLLNFLD-LP-------SEKRlvKNLSGGQQRRVSFAVALMHDPELL 230
Cdd:cd03254 85 DTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMkLPngydtvlGENG--GNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 231 ILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
85-315 |
1.79e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 85 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEI----FVLGGKPGTRGSGVPG---------- 150
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPyskkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 --KRVGYMPQ--EIALYGEfSIQETMMyFGWI-FGMETKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVAL 223
Cdd:PRK13631 114 lrRRVSMVFQfpEYQLFKD-TIEKDIM-FGPVaLGVKKSEAKKLAKFYLNKMGLDDSylERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 224 MHDPELLILDEPTVGVDPLLRQSIWNhLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPsvllsiYKcI 302
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP------YE-I 263
|
250
....*....|...
gi 194201171 303 SLEEVFLKLSRIQ 315
Cdd:PRK13631 264 FTDQHIINSTSIQ 276
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
91-286 |
1.97e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGvPGKRVGYMPQEIALYgefsiqE 170
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-RFHGTDVSRLHA-RDRKVGFVFQHYALF------R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 171 TMMYFGWI-FGM---------ETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 239
Cdd:PRK10851 88 HMTVFDNIaFGLtvlprrerpNAAAIKAKVTQLLEMVQLAHlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194201171 240 DPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
67-300 |
3.19e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.36 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYGKKK-NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtRG 145
Cdd:COG1134 15 RLYHEPSRSLKELLLRRRRTRrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 146 SGVPGKRVGYMPqeialygEFSIQETMMYFGWIFGMETKEILERLQF------LLNFLDLPsekrlVKNLSGGQQRRVSF 219
Cdd:COG1134 90 SALLELGAGFHP-------ELTGRENIYLNGRLLGLSRKEIDEKFDEivefaeLGDFIDQP-----VKTYSSGMRARLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 220 AVALMHDPELLILDEPT-VGvDPLLRQsiwnhlvhitKAGQK---------TVIITTHYIEEARQ-AHTIGLMRSGHLLA 288
Cdd:COG1134 158 AVATAVDPDILLVDEVLaVG-DAAFQK----------KCLARirelresgrTVIFVSHSMGAVRRlCDRAIWLEKGRLVM 226
|
250
....*....|..
gi 194201171 289 EESPSVLLSIYK 300
Cdd:COG1134 227 DGDPEEVIAAYE 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
83-297 |
4.27e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGT--RGSGVPGKRVGYMPQEI 160
Cdd:PRK11614 15 YGKI----QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI-VFDGKDITdwQTAKIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYFGwiFGMETKEILERLQFLLNFLDLPSEKRLVK--NLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:PRK11614 90 RVFSRMTVEENLAMGG--FFAERDQFQERIKWVYELFPRLHERRIQRagTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 239 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
74-297 |
5.53e-17 |
|
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: 83.30 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYgkKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRV 153
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEfSIQETMMYFGWifGMETKEILE--RLQFLLNF-LDLPSEKRLV-----KNLSGGQQRRVSFAVALMH 225
Cdd:cd03252 79 GVVLQENVLFNR-SIRDNIALADP--GMSMERVIEaaKLAGAHDFiSELPEGYDTIvgeqgAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAgqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
96-273 |
7.52e-17 |
|
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: 82.16 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 96 LNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIqETMMY 174
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LINGVDVTAAP--PADRpVSMLFQENNLFAHLTV-EQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 175 FGWIFGME-TKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLV 252
Cdd:cd03298 93 LGLSPGLKlTAEDRQAIEVALARVGLAGlEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180
....*....|....*....|.
gi 194201171 253 HITKAGQKTVIITTHYIEEAR 273
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAK 193
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
92-288 |
9.89e-17 |
|
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: 87.02 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYgEFSIQET 171
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELF-PGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 MMYFGWIFgmETKEILE--RL----QFLLNFldlPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:TIGR01842 412 IARFGENA--DPEKIIEaaKLagvhELILRL---PDGYDTVigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194201171 241 PLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQAHTIGLMRSGHLLA 288
Cdd:TIGR01842 487 EEGEQALANAIKALKARG-ITVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
89-293 |
1.39e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 89 ANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG-----RRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQ--EIA 161
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVR-KKVGVVFQfpESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 162 LYGEFSIQETMmyFG-WIFGMETKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:PRK13643 97 LFEETVLKDVA--FGpQNFGIPKEKAEKIAAEKLEMVGLADEfwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 239 VDPLLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPS 293
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDvADYADYVYLLEKGHIISCGTPS 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
62-297 |
1.42e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.80 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 62 APANGPRNTQAAVSVRHAFKAYgkKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMDA--GEIfVLGG 139
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT--RAWDPqqGEI-LLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 140 KPGTRGS--------GVPGKRV----GYMPQEIALYGEFSIQETMMyfgwifgmetkEILER--LQFLLNfldlpSEKRL 205
Cdd:PRK11160 402 QPIADYSeaalrqaiSVVSQRVhlfsATLRDNLLLAAPNASDEALI-----------EVLQQvgLEKLLE-----DDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 206 V-------KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTI 278
Cdd:PRK11160 466 NawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRI 543
|
250
....*....|....*....
gi 194201171 279 GLMRSGHLLAEESPSVLLS 297
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLA 562
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
99-297 |
1.48e-16 |
|
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: 84.77 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 99 TVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP---GTRGSGVP-GKR-VGYMPQEIALYGEFSIQETMM 173
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI-RLGGEVlqdSARGIFLPpHRRrIGYVFQEARLFPHLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 174 YfGWIFGMETK------EILERLQF--LLNfldlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 245
Cdd:COG4148 100 Y-GRKRAPRAErrisfdEVVELLGIghLLD--------RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 246 SIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEvARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
88-314 |
1.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP---GTRGSGVPGKRVGYMPQ--EIAL 162
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-FDGKPidySRKGLMKLRESVGMVFQdpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YGEfSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:PRK13636 96 FSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIeHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 242 LLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLSiyKCISLEEVFLKLSRI 314
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFA--EKEMLRKVNLRLPRI 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
87-267 |
2.16e-16 |
|
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: 80.48 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 87 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYMPQEIALYGEF 166
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETMMYFGWIFGMETKEILERLQfLLNFLDLpsEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPlLRQS 246
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALA-AVGLTGF--EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVA 164
|
170 180
....*....|....*....|...
gi 194201171 247 IWNHLV--HITKAGqkTVIITTH 267
Cdd:TIGR01189 165 LLAGLLraHLARGG--IVLLTTH 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
92-324 |
2.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.83 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTT-------LLSCIVGRRYM------DAGEIFVLGGKPGTrgsgvpgkrVGYMP- 157
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTiakhmnaLLIPSEGKVYVdgldtsDEENLWDIRNKAGM---------VFQNPd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 -QEIAlygefSIQETMMYFG-WIFGMETKEILERLQFLLNFLDLPSEKRLVKN-LSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:PRK13633 96 nQIVA-----TIVEEDVAFGpENLGIPPEEIRERVDESLKKVGMYEYRRHAPHlLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 235 PTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPsvllsiykcislEEVFLKLSRI 314
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP------------KEIFKEVEMM 238
|
250
....*....|
gi 194201171 315 QSQKGDVTHV 324
Cdd:PRK13633 239 KKIGLDVPQV 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
67-273 |
2.44e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.01 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC-------IVGRRYmdAGEIFvLGG 139
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EGEIL-LDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 140 K----PGT-----RgsgvpgKRVGyM--------PqeialygeFSIQETMMYFGWIFGMETKEIL-ERLQFLLNFLDLPS 201
Cdd:COG1117 78 EdiydPDVdvvelR------RRVG-MvfqkpnpfP--------KSIYDNVAYGLRLHGIKSKSELdEIVEESLRKAALWD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 202 EkrlVKN--------LSGGQQRRVSFAVALMHDPELLILDEPTVGVDP--------LLRQsiwnhLvhitkAGQKTVIIT 265
Cdd:COG1117 143 E---VKDrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieeLILE-----L-----KKDYTIVIV 209
|
....*...
gi 194201171 266 THYIEEAR 273
Cdd:COG1117 210 THNMQQAA 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
69-310 |
2.61e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCI-------VGRRYMDAGEIFVLGGKP 141
Cdd:PRK10619 1 MSENKLNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 142 GTRGsgVPGK--------RVGYMPQEIALYGEFSIQETMMYFG-WIFGMETKEILERLQFLLNF--LDLPSEKRLVKNLS 210
Cdd:PRK10619 77 GQLK--VADKnqlrllrtRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKvgIDERAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 211 GGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ--AHTIgLMRSGHLLA 288
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHEMGFARHvsSHVI-FLHQGKIEE 232
|
250 260
....*....|....*....|..
gi 194201171 289 EESPSVLLSIYKCISLEEvFLK 310
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQ-FLK 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
85-273 |
2.66e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 85 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCI-------VGRryMDAGEIFVLGGKPGTRGSGVPGK---RVG 154
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGT--IRVGDITIDTARSLSQQKGLIRQlrqHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMPQEIALYGEFSIQETMMYFGWIFGMETKE-ILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEGPVIVKGEPKEeATARARELLAKVGLAgKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAgQKTVIITTHYIEEAR 273
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFAR 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
93-272 |
2.70e-16 |
|
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: 81.36 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGKRVGYMPQEIALYGEFSIQETM 172
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-ILEGKQITE----PGPDRMVVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 myfgwifGMETKEIL------ERLQFLLNFLDL-----PSEKRlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:TIGR01184 76 -------ALAVDRVLpdlsksERRAIVEEHIALvglteAADKR-PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190
....*....|....*....|....*....|.
gi 194201171 242 LLRQSIWNHLVHITKAGQKTVIITTHYIEEA 272
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
91-292 |
2.81e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.57 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG----GKPGTRGSGVPGKRVGYMPQ--EIALYg 164
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQfpEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLpSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL-SEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 194201171 242 LLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESP 292
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDvAEYADDVLVLEHGKLIKHASP 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
73-325 |
2.98e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKKNAnqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGE---IFVLGGKPGTRGSGVP 149
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 GKRVGYMPQEIAlyGEF---SIQETMMyfgwiFGMETKEIlERLQFL------------LNFLDlpSEKrlvKNLSGGQQ 214
Cdd:PRK13640 83 REKVGIVFQNPD--NQFvgaTVGDDVA-----FGLENRAV-PRPEMIkivrdvladvgmLDYID--SEP---ANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 215 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPsv 294
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP-- 227
|
250 260 270
....*....|....*....|....*....|.
gi 194201171 295 llsiykcislEEVFLKLSRIQSQKGDVTHVN 325
Cdd:PRK13640 228 ----------VEIFSKVEMLKEIGLDIPFVY 248
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
91-297 |
3.32e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFV----LGGKPGTRGSGVPGKRVGYMPQ--EIALYg 164
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYIRPVRKRIGMVFQfpESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EFSIQETMMYFGWIFGMETKEILERLQFLLnfLDLPSEKRLVK----NLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 241 PLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
93-297 |
4.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRgSGVPGKR--VGYMPQ--EIALYGEfSI 168
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRklVGIVFQnpETQFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMMYFGWIFGMETKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSI 247
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 194201171 248 WNHLVHITKAGqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK13644 176 LERIKKLHEKG-KTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
74-293 |
5.18e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYgkKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGT-------Rgs 146
Cdd:PRK13635 6 IRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSeetvwdvR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 gvpgKRVGYMPQ-------------EIAlygeFSIQETmmyfgwifGMETKEILERLQFLLN------FLDlpsekRLVK 207
Cdd:PRK13635 81 ----RQVGMVFQnpdnqfvgatvqdDVA----FGLENI--------GVPREEMVERVDQALRqvgmedFLN-----REPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 208 NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLL 287
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
....*.
gi 194201171 288 AEESPS 293
Cdd:PRK13635 220 EEGTPE 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
91-314 |
6.19e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--KRVGYMPQ--EIALYGEf 166
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTVGIVFQnpDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETMMYFGWIFGMETKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 245
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEgFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 246 SIWNHLVHITKAGQkTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLSIYKCIslEEVFLKLSRI 314
Cdd:PRK13639 175 QIMKLLYDLNKEGI-TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI--RKANLRLPRV 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
70-287 |
6.34e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.59 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDAGEIFVLGGKPGTRGSGVP 149
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI--NRMNDLNPEVTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 GKRVGY--MPQEIALYGE------FSIQETMMYFGWIFGMETKEILerlqfllnflDLPSEKRL--------VKN----- 208
Cdd:PRK14239 76 SPRTDTvdLRKEIGMVFQqpnpfpMSIYENVVYGLRLKGIKDKQVL----------DEAVEKSLkgasiwdeVKDrlhds 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 209 ---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEA-RQAHTIGLMRSG 284
Cdd:PRK14239 146 algLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQAsRISDRTGFFLDG 223
|
...
gi 194201171 285 HLL 287
Cdd:PRK14239 224 DLI 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
97-273 |
8.49e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 79.13 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 97 NMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIQETM--- 172
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV-NDQSHTGLA--PYQRpVSMLFQENNLFAHLTVRQNIglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGMETKEILERLQFLLNFLDLPSekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLV 252
Cdd:TIGR01277 95 LHPGLKLNAEQQEKVVDAAQQVGIADYLD--RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180
....*....|....*....|.
gi 194201171 253 HITKAGQKTVIITTHYIEEAR 273
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDAR 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
90-315 |
8.92e-16 |
|
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: 79.89 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMD--AGEIFvLGGKPgTRGSGVPGKR--VGYMPQEIALYgE 165
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERFYDptSGEIL-LDGVD-IRDLNLRWLRsqIGLVSQEPVLF-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 FSIQETMMYfGwIFGMETKEILE--RLQFLLNFL-DLPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELLILDEPTV 237
Cdd:cd03249 91 GTIAENIRY-G-KPDATDEEVEEaaKKANIHDFImSLPDGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 238 GVDPLLRQSIWNHLVHITKAgqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLlsiykcISLEEVFLKLSRIQ 315
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL------MAQKGVYAKLVKAQ 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
74-286 |
9.75e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRV 153
Cdd:PRK15439 12 LCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI-GGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 G-YM-PQEIALYGEFSIQETMMyFGWIFGMETKEILERLQFLLNF-LDLPSEKRLvknLSGGQQRRVSFAVALMHDPELL 230
Cdd:PRK15439 87 GiYLvPQEPLLFPNLSVKENIL-FGLPKRQASMQKMKQLLAALGCqLDLDSSAGS---LEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 231 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIItTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFI-SHKLPEIRQlADRISVMRDGTI 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
88-272 |
1.82e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKG---TIyglLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtrgsgvpgKRVGYMPQE-IALY 163
Cdd:COG1101 17 NEKRALDGLNLTIEEGdfvTV---IGSNGAGKSTLLNAIAGSLPPDSGSILIDG------------KDVTKLPEYkRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 164 -------------GEFSIQETMMY-------FGWIFGMETKEIlERLQFLLNFLDLPSEKRL---VKNLSGGQQRRVSFA 220
Cdd:COG1101 82 igrvfqdpmmgtaPSMTIEENLALayrrgkrRGLRRGLTKKRR-ELFRELLATLGLGLENRLdtkVGLLSGGQRQALSLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 272
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQA 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
87-296 |
1.96e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 87 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEF 166
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETMMYFGWI-FGMETKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:PRK13647 95 STVWDDVAFGPVnMGLDKDEVERRVEEALKAVRMWDFRdKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 245 QSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLL 296
Cdd:PRK13647 175 ETLMEILDRLHNQG-KTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
86-267 |
2.21e-15 |
|
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: 77.67 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 86 KKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMD--AGEIFvLGGKPGTRGSgvpGKRVGYMPQEIALY 163
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEIL-INGRPLDKNF---QRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 164 GEFSIQETMMYFGWIFGmetkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 243
Cdd:cd03232 92 PNLTVREALRFSALLRG----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|....
gi 194201171 244 RQSIWNHLVHITKAGQkTVIITTH 267
Cdd:cd03232 144 AYNIVRFLKKLADSGQ-AILCTIH 166
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
74-299 |
2.73e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRV 153
Cdd:COG4604 2 IEIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMyfgwiFG----------METKEILERLqflLNFLDL-PSEKRLVKNLSGGQQRRVSFAVA 222
Cdd:COG4604 78 AILRQENHINSRLTVRELVA-----FGrfpyskgrltAEDREIIDEA---IAYLDLeDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 223 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESP------SVL 295
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAsCYADHIVAMKDGRVVAQGTPeeiitpEVL 229
|
....
gi 194201171 296 LSIY 299
Cdd:COG4604 230 SDIY 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
69-243 |
2.81e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.07 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG----KPGTR 144
Cdd:COG4598 4 TAPPALEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 145 GSGVPGK---------RVGYMPQEIALYGEFSIQETMMyFGWI--FGMETKEILERLQFLLNFLDLpSEKRLV--KNLSG 211
Cdd:COG4598 80 GELVPADrrqlqrirtRLGMVFQSFNLWSHMTVLENVI-EAPVhvLGRPKAEAIERAEALLAKVGL-ADKRDAypAHLSG 157
|
170 180 190
....*....|....*....|....*....|..
gi 194201171 212 GQQRRVSFAVALMHDPELLILDEPTVGVDPLL 243
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPEL 189
|
|
| TagG |
COG1682 |
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport ... |
607-773 |
3.15e-15 |
|
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport and metabolism];
Pssm-ID: 441288 [Multi-domain] Cd Length: 258 Bit Score: 78.69 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 607 PSFTDFVAPGviLTIVFFLAVALTSSALIIERTEGLLdRSwvAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVvFGVT 686
Cdd:COG1682 61 VPYALFLLAG--LLPWNFFSEALNRGSGSIVANAGLI-KK--VYFPREILPLARVLSALVNFLISLVVLLVVLLL-FGVP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 687 NNGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLaLGSF-YPTLLLSGVIWPIEGMPVVLRYISLCLPLTLATSS 765
Cdd:COG1682 135 PSWTLLLLPLALLLLLLFGLGLGLLLAALNVFFRDVQQI-VGLLlQLLFFLSPVFYPLSTLPEPLRWLLLLNPLTHIIEL 213
|
....*...
gi 194201171 766 LRSILTRG 773
Cdd:COG1682 214 FRAALLGG 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
93-286 |
3.70e-15 |
|
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: 83.07 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRryMDAGEifvlgGKPGTRGSgvpgkrVGYMPQEiALYGEFSIQETM 172
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE--MDKVE-----GHVHMKGS------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGMETKEILERLQFLLNFLDLPS-------EKRLvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 245
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPDLEILPSgdrteigEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 194201171 246 SIWNHLVHITKA-GQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:TIGR00957 798 HIFEHVIGPEGVlKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
81-286 |
4.11e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.23 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtrgsgvpgkrvgympQEI 160
Cdd:PRK11153 9 KVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG-------------------QDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYFGWIF----------------------GMETKEILERLQFLLNFLDLpSEKRLV--KNLSGGQQRR 216
Cdd:PRK11153 70 TALSEKELRKARRQIGMIFqhfnllssrtvfdnvalplelaGTPKAEIKARVTELLELVGL-SDKADRypAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 217 VSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 286
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
90-267 |
4.76e-15 |
|
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: 77.24 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL-YGefSI 168
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLfYG--TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMMYFGWIfgMETKEILERLQF--LLNF-------LDLPSEKRlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 239
Cdd:cd03245 95 RDNITLGAPL--ADDERILRAAELagVTDFvnkhpngLDLQIGER-GRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190
....*....|....*....|....*....|
gi 194201171 240 DpllrQSIWNHLVHITKA--GQKTVIITTH 267
Cdd:cd03245 172 D----MNSEERLKERLRQllGDKTLIIITH 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
85-287 |
1.15e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 85 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDA---GEIFVLGG---KPGTRGSGVPGKR--VGYM 156
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRtvqREGRLARDIRKSRanTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 157 PQEIALYGEFSIQETMMY------------FGWIFGMETKEILERLQF--LLNFldlpSEKRlVKNLSGGQQRRVSFAVA 222
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIgalgstpfwrtcFSWFTREQKQRALQALTRvgMVHF----AHQR-VSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 223 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLL 287
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVF 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
83-297 |
1.73e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.06 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKKKNANQvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQ--EI 160
Cdd:PRK13642 14 YEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEfSIQETMMyfgwiFGMETK-----EILERLQ---FLLNFLDLPSekRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:PRK13642 93 QFVGA-TVEDDVA-----FGMENQgipreEMIKRVDealLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
95-247 |
1.92e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.21 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 95 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrrymDAGEIFVLGGK---PGTRGSGVPG--KRVGYMPQEIALYGEFSIQ 169
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAG----TLSPAFSASGEvllNGRRLTALPAeqRRIGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 170 ETMMyfgwiFGMETK----EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:COG4136 95 ENLA-----FALPPTigraQRRARVEQALEEAGLAGfADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
...
gi 194201171 245 QSI 247
Cdd:COG4136 170 AQF 172
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
91-293 |
2.56e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC------------IVGRRYMDAGEIFVLGGKPGTRgsgvpgkRVGYMPQ 158
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFKMDVIELRR-------RVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 EIALYGEFSIQETMMyfgwiFGME-------TKEILERLQFLL----------NFLDLPSEKrlvknLSGGQQRRVSFAV 221
Cdd:PRK14247 90 IPNPIPNLSIFENVA-----LGLKlnrlvksKKELQERVRWALekaqlwdevkDRLDAPAGK-----LSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 222 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEE-ARQAHTIGLMRSGHLLaEESPS 293
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQaARISDYVAFLYKGQIV-EWGPT 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
92-296 |
3.42e-14 |
|
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: 79.40 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGS-GVPGKRVGYMPQEIALYGEfSIQE 170
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI-LLNGFSLKDIDrHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 171 TMMyFGWIFGMETKEILERLQFL-----LNFLDLPSEKRLVK---NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 242
Cdd:TIGR01193 567 NLL-LGAKENVSQDEIWAACEIAeikddIENMPLGYQTELSEegsSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 194201171 243 LRQSIWNHLVHITkagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:TIGR01193 646 TEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
92-297 |
3.89e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQET 171
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 M-M--------YFGWIFGMET--KEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:PRK09536 98 VeMgrtphrsrFDTWTETDRAavERAMERTG-VAQFAD-----RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 241 PllrqsiwNHLVHITKAGQ------KTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK09536 172 I-------NHQVRTLELVRrlvddgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
91-306 |
4.54e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.81 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP---GTRGSGVPGKRVGYM---PQEIALYG 164
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPldySKRGLLALRQQVATVfqdPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EfsIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 243
Cdd:PRK13638 94 D--IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 244 RQSIWNHLVHITKAGQKtVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSvllSIYKCISLEE 306
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNH-VIISSHDIDLIYEiSDAVYVLRQGQILTHGAPG---EVFACTEAME 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
91-242 |
4.60e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtRGSGVPG----------KRVGYMPQEI 160
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-------DGENIPAmsrsrlytvrKRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMmyfGWIFGMETK--EILERLQFLLNFLD---------LPSEkrlvknLSGGQQRRVSFAVALMHDPEL 229
Cdd:PRK11831 94 ALFTDMNVFDNV---AYPLREHTQlpAPLLHSTVMMKLEAvglrgaaklMPSE------LSGGMARRAALARAIALEPDL 164
|
170
....*....|...
gi 194201171 230 LILDEPTVGVDPL 242
Cdd:PRK11831 165 IMFDEPFVGQDPI 177
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
67-294 |
6.74e-14 |
|
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: 74.39 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGS 146
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-QDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 -----GVPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGM-----ETKEILER--LQFLLNFLdlPSEkrlvknLSGGQQ 214
Cdd:COG4181 81 edaraRLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRrdaraRARALLERvgLGHRLDHY--PAQ------LSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 215 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSV 294
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
91-310 |
6.86e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtRGSGVPGKRVGYMPQEIALYGE----- 165
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-------RGEPITKENIREVRKFVGLVFQnpddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 -FSIQ-ETMMYFGWI-FGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:PRK13652 91 iFSPTvEQDIAFGPInLGLDEETVAHRVSSALHMLGLEElRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 242 LLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPsvllsiykcislEEVFLK 310
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTV------------EEIFLQ 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
92-296 |
7.29e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGRRYMDAGEIFVLGGKP-GTRGSGVPGKRVGYMPQEIALYGEFSIQE 170
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILLDAQPlESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 171 --TMMYFGW-----IFGMETKEILERLQFLLNFLdlPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDpLL 243
Cdd:PRK10575 105 lvAIGRYPWhgalgRFGAADREKVEEAISLVGLK--PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 244 RQSIWNHLVH-ITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPSVLL 296
Cdd:PRK10575 182 HQVDVLALVHrLSQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
70-288 |
7.64e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYgkkKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLgGKPGTRgsGVP 149
Cdd:PRK15056 3 QQAGIVVNDVTVTW---RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIL-GQPTRQ--ALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 GKRVGYMPQEIALYGEFSI---QETMM----YFGW--IFGMETKEILERLQFLLNFLDLpsEKRLVKNLSGGQQRRVSFA 220
Cdd:PRK15056 77 KNLVAYVPQSEEVDWSFPVlveDVVMMgrygHMGWlrRAKKRDRQIVTAALARVDMVEF--RHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQAHTIGLMRSGHLLA 288
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSVTEFCDYTVMVKGTVLA 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
82-297 |
1.05e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDA--GEIFVLGGKPGTRGSGVPGKRVGYMPQE 159
Cdd:PRK10253 16 GYGKYT----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL--SRLMTPahGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 160 IALYGEFSIQETM---------MYFGWifGMETKEILERLQFLLNFLDLPSEKrlVKNLSGGQQRRVSFAVALMHDPELL 230
Cdd:PRK10253 90 ATTPGDITVQELVargryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQS--VDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 231 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQA-HTIGLmRSGHLLAEESPSVLLS 297
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYAsHLIAL-REGKIVAQGAPKEIVT 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
73-236 |
1.19e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtrgsgvpgK- 151
Cdd:PRK15064 319 ALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------------Kw 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 ----RVGYMPQEIAlyGEFSIQETMmyFGWIfGMETKE---------ILERLQFLLNflDLpseKRLVKNLSGGQQRRVS 218
Cdd:PRK15064 379 senaNIGYYAQDHA--YDFENDLTL--FDWM-SQWRQEgddeqavrgTLGRLLFSQD--DI---KKSVKVLSGGEKGRML 448
|
170
....*....|....*...
gi 194201171 219 FAVALMHDPELLILDEPT 236
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPT 466
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
90-287 |
1.25e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.11 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDAGEIFVLGGKPGTRGSGVPG---------KRVGYMPQEI 160
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF--NRLLELNEEARVEGEVRLFGRNIYSpdvdpievrREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYFGWIFGM--ETKEILERLQFLLNFLDLPSE--KRL---VKNLSGGQQRRVSFAVALMHDPELLILD 233
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEvkDRLndyPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHY-IEEARQAHTIGLMRSGHLL 287
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
92-289 |
1.27e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR----VGYMPQE---IALYG 164
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR-LDGEDITGLS--PRERrrlgVAYIPEDrlgRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 EFSIQETMM--------YFGWIFgMETKEILERLQFLLNFLDL--PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:COG3845 350 DMSVAENLIlgryrrppFSRGGF-LDRKAIRAFAEELIEEFDVrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 235 PTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 289
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAG-AAVLLISEDLDEILAlSDRIAVMYEGRIVGE 483
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
74-240 |
1.58e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtrgSGVPGKRV 153
Cdd:PRK09544 5 VSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGE--FSIQETMMYFGwifGMETKEI---LERLQfLLNFLDLPSEKrlvknLSGGQQRRVSFAVALMHDPE 228
Cdd:PRK09544 70 GYVPQKLYLDTTlpLTVNRFLRLRP---GTKKEDIlpaLKRVQ-AGHLIDAPMQK-----LSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 194201171 229 LLILDEPTVGVD 240
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
72-297 |
2.19e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPG- 150
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR-LNGRPLADWS--PAe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 --KRVGYMPQEIALYGEFSIQEtmmyfgwIFGM----------ETKEILERLQFLLNFLDLpsEKRLVKNLSGGQQRRVS 218
Cdd:PRK13548 74 laRRRAVLPQHSSLSFPFTVEE-------VVAMgraphglsraEDDALVAAALAQVDLAHL--AGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 219 FAVALM------HDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEES 291
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
....*.
gi 194201171 292 PSVLLS 297
Cdd:PRK13548 225 PAEVLT 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
75-247 |
2.40e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 SVRHAFKAYG-----KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgTRGSGVP 149
Cdd:PRK10419 5 NVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG----EPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 150 GKRVGYMPQEIAL-----YGEFSIQETMmyfGWIFG--------METKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQ 214
Cdd:PRK10419 81 RAQRKAFRRDIQMvfqdsISAVNPRKTV---REIIReplrhllsLDKAERLARASEMLRAVDLDDSvlDKRPPQLSGGQL 157
|
170 180 190
....*....|....*....|....*....|...
gi 194201171 215 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSI 247
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
81-289 |
2.55e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSG----VPGKRVGYM 156
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 157 PQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSFAVALMHDPEL 229
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLehranhrPSE------LSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 230 LILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 289
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
97-272 |
2.73e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 97 NMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIQETM--- 172
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-LNGQDHTTTP--PSRRpVSMLFQENNLFSHLTVAQNIglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGMETKEILERLQ---FLLNFLD-LPSEkrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIW 248
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIArqmGIEDLLArLPGQ------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180
....*....|....*....|....
gi 194201171 249 NHLVHITKAGQKTVIITTHYIEEA 272
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDA 193
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
94-241 |
2.75e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 94 NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTrgsGVPGKRVGYMP-----QEIALYGEFSI 168
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-LLRGQHIE---GLPGHQIARMGvvrtfQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMM----------YFGWIFGMET-----KEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:PRK11300 98 IENLLvaqhqqlktgLFSGLLKTPAfrraeSEALDRAATWLERVGLlEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
....*....
gi 194201171 233 DEPTVGVDP 241
Cdd:PRK11300 178 DEPAAGLNP 186
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
91-292 |
2.93e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGrrYMDageifvlggKPGTRGSGVPGKRVGYMPQE--IALYGEfsi 168
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILG--CLD---------KPTSGTYRVAGQDVATLDADalAQLRRE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 qetmmYFGWIF----------------------GMETKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSF 219
Cdd:PRK10535 87 -----HFGFIFqryhllshltaaqnvevpavyaGLERKQRLLRAQELLQRLGLedrveyqPSQ------LSGGQQQRVSI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 220 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHTIGLMRSGHLLAEESP 292
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
92-267 |
3.69e-13 |
|
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: 75.55 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrrymdageifVLggkPGTRGS----GVP---------GKRVGYMPQ 158
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG----------VW---PPTAGSvrldGADlsqwdreelGRHIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 EIALYgEFSIQEtmmyfgwifgmetkeilerlqfllN---FLDLPSEK-----RLV---------------------KNL 209
Cdd:COG4618 414 DVELF-DGTIAE------------------------NiarFGDADPEKvvaaaKLAgvhemilrlpdgydtrigeggARL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194201171 210 SGGQQRRVSFAVALMHDPELLILDEPTVGVDPL----LRQSIWNHlvhitKAGQKTVIITTH 267
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEgeaaLAAAIRAL-----KARGATVVVITH 525
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
90-300 |
4.68e-13 |
|
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: 71.02 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR-RY-MDAGEIFvLGGKPGTRGSgvpgkrvgymPQEIALYGefs 167
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYeVTEGEIL-FKGEDITDLP----------PEERARLG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 168 iqetmMYFGWIFGMETKEIleRLQFLLNFLDlpsekrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD----PLL 243
Cdd:cd03217 79 -----IFLAFQYPPEIPGV--KNADFLRYVN--------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 244 RQSIwNHLvhitKAGQKTVIITTHY--IEEARQAHTIGLMRSGHLLAEESPSVLLSIYK 300
Cdd:cd03217 144 AEVI-NKL----REEGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKSGDKELALEIEK 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
81-267 |
4.94e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKNANQ--VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRY--MDAGEIFVLGGKPGTRGSGVpgkrvgym 156
Cdd:COG2401 32 EAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLI-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 157 pQEIALYGEFSiqetmmyfgwifgmETKEILERLQflLNflDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:COG2401 104 -DAIGRKGDFK--------------DAVELLNAVG--LS--DAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|.
gi 194201171 237 VGVDPLLRQSIWNHLVHITKAGQKTVIITTH 267
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
92-267 |
5.63e-13 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 75.29 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL-YGefSIQE 170
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLfYG--TLRD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 171 TMMyfgwiFGM---ETKEILERLQF--LLNF-------LDLP-SEKRLvkNLSGGQQRRVSFAVALMHDPELLILDEPTV 237
Cdd:TIGR03375 558 NIA-----LGApyaDDEEILRAAELagVTEFvrrhpdgLDMQiGERGR--SLSGGQRQAVALARALLRDPPILLLDEPTS 630
|
170 180 190
....*....|....*....|....*....|..
gi 194201171 238 GVDpllrQSIWNHLVHITKA--GQKTVIITTH 267
Cdd:TIGR03375 631 AMD----NRSEERFKDRLKRwlAGKTLVLVTH 658
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
65-236 |
1.43e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 65 NGPRNTQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtr 144
Cdd:TIGR03719 314 PGPRLGDKVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 145 GSGVpgkRVGYMPQE-IALYGEFSIQET------MMYFGwifgmeTKEILERL---QFllNFLDLPSEKRlVKNLSGGQQ 214
Cdd:TIGR03719 382 GETV---KLAYVDQSrDALDPNKTVWEEisggldIIKLG------KREIPSRAyvgRF--NFKGSDQQKK-VGQLSGGER 449
|
170 180
....*....|....*....|..
gi 194201171 215 RRVSFAVALMHDPELLILDEPT 236
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPT 471
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
92-308 |
1.69e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMD--AGEIFVLGGKPGTRGSgvpgKRVGYMPQEIALYGEFSIQ 169
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL----KRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 170 ETMMYFGWIF---GMETKEILERLQFLLNFLDLPS-EKRLVKN-----LSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:PLN03211 159 ETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKcENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 241 PLLRQSIWNHLVHITKAGqKTVIITTHYIEEA--RQAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVF 308
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKG-KTIVTSMHQPSSRvyQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSF 307
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
83-272 |
3.14e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 83 YGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDAGEIFVLGGKPGTRGSGVPGK---------RV 153
Cdd:PRK14243 20 YGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCF--NRLNDLIPGFRVEGKVTFHGKNLYAPdvdpvevrrRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEfSIQETMMYFGWIFGME--TKEILERLQFLLNFLDLPSEKrLVKN---LSGGQQRRVSFAVALMHDPE 228
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYGARINGYKgdMDELVERSLRQAALWDEVKDK-LKQSglsLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 194201171 229 LLILDEPTVGVDPLLRQSIwNHLVHITKAgQKTVIITTHYIEEA 272
Cdd:PRK14243 172 VILMDEPCSALDPISTLRI-EELMHELKE-QYTIIIVTHNMQQA 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
95-286 |
4.09e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 95 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGsgvPGKRVG----YMPQEIALYGEF---- 166
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TAQRLArglvYLPEDRQSSGLYldap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 ------SIQETMMYFgWIFGMETKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:PRK15439 358 lawnvcALTHNRRGF-WIKPARENAVLERYRRALN-IKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 194201171 241 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
92-267 |
4.15e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.29 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQET 171
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-LLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 MMYFGWIFGMET-KEILERLQfLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD----PLLRQS 246
Cdd:cd03231 94 LRFWHADHSDEQvEEALARVG-LNGFEDRP-----VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEA 167
|
170 180
....*....|....*....|.
gi 194201171 247 IWNHLvhitkAGQKTVIITTH 267
Cdd:cd03231 168 MAGHC-----ARGGMVVLTTH 183
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
74-297 |
4.56e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 68.80 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMD--AGEIFVLG------GKPGTRg 145
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDvsSGSILIDGqdirevTLDSLR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 146 sgvpgKRVGYMPQEIALYgefsiQETMMY---FGWIFGMEtKEILERLQ------FLLNFLDLPSEK---RLVKnLSGGQ 213
Cdd:cd03253 75 -----RAIGVVPQDTVLF-----NDTIGYnirYGRPDATD-EEVIEAAKaaqihdKIMRFPDGYDTIvgeRGLK-LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 214 QRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAgqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPS 293
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHE 220
|
....
gi 194201171 294 VLLS 297
Cdd:cd03253 221 ELLA 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-287 |
5.05e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC------IVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIA 161
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 162 LYGEFSIQETMMYFGWIFGM-ETKEILERLQFLLNFLDLPSE--KRL---VKNLSGGQQRRVSFAVALMHDPELLILDEP 235
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLWKEvyDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 236 TVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEE-ARQAHTIGLMRSGHLL 287
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQvARVADYVAFLYNGELV 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
70-267 |
5.46e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLgGKPGTR----- 144
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQmdeea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 145 GSGVPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLpsEKRLV---KNLSGGQQRRVSFAV 221
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGL--GKRLDhlpAQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 194201171 222 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH 267
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
74-236 |
6.52e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 70.15 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAY-------GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGS 146
Cdd:COG4608 8 LEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL-FDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 GV---------------------PGKRVGympqEIalygefsIQETMMyfgwIFGMETK-EILERLQFLLNFLDLPSE-- 202
Cdd:COG4608 87 GRelrplrrrmqmvfqdpyaslnPRMTVG----DI-------IAEPLR----IHGLASKaERRERVAELLELVGLRPEha 151
|
170 180 190
....*....|....*....|....*....|....
gi 194201171 203 KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:COG4608 152 DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
93-314 |
7.98e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKRVGYMPQEIALYGEFS----I 168
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV-DDTLITSTS--KNKDIKQIRKKVGLVFQFPesqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMM---YFG-WIFGMETKEILERLQFLLNFLDLpSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:PRK13649 100 EETVLkdvAFGpQNFGVSQEEAEALAREKLALVGI-SESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 242 LLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSvllSIYKCIS-LEEVFLKLSRI 314
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGM-TIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPK---DIFQDVDfLEEKQLGVPKI 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
79-272 |
8.16e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 79 AFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKP------GTR-----GSG 147
Cdd:PRK11247 14 LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTAPlaeareDTRlmfqdARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 VPGKR----VGympqeIALYGEFSIQETMmyfgwifGMETKEILERLQfllnflDLPSEkrlvknLSGGQQRRVSFAVAL 223
Cdd:PRK11247 93 LPWKKvidnVG-----LGLKGQWRDAALQ-------ALAAVGLADRAN------EWPAA------LSGGQKQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 224 MHDPELLILDEPTVGVDPLLR-------QSIWnhlvhitkagQK---TVIITTHYIEEA 272
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRiemqdliESLW----------QQhgfTVLLVTHDVSEA 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
93-240 |
8.16e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvpgkrvgymPQEIALYGEFSIQETM 172
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV-TLDGHEVVTRS----------PQDGLANGIVYISEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGMETKE--ILERLQFLLN----------------FLDL-----PSEKRLVKNLSGGQQRRVSFAVALMHDPEL 229
Cdd:PRK10762 337 KRDGLVLGMSVKEnmSLTALRYFSRaggslkhadeqqavsdFIRLfniktPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170
....*....|.
gi 194201171 230 LILDEPTVGVD 240
Cdd:PRK10762 417 LILDEPTRGVD 427
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
86-267 |
1.17e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 86 KKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR---YMDAGEIFVLGGKpgtRGSGVPgKRVGYMPQEIAL 162
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRP---LDSSFQ-RSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YGEFSIQETMMYFGWI---FGMETKEILERLQFLLNFLDLPSEKRLVKNLSGG-----QQRRVSFAVALMHDPELLI-LD 233
Cdd:TIGR00956 848 LPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEglnveQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTH 267
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIH 960
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
74-270 |
1.98e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrryMDAGE------IFVLG--------G 139
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG---MDQYEptsgriIYHVAlcekcgyvE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 140 KPGTRGSGVPG------------------------KRVGYMPQE-IALYGEFSIQETMMYFGWIFGMETKEILERLQFLL 194
Cdd:TIGR03269 74 RPSKVGEPCPVcggtlepeevdfwnlsdklrrrirKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 195 NFLDLpsEKR---LVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE 270
Cdd:TIGR03269 154 EMVQL--SHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-267 |
2.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.75 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvGRRYMDAGEIFVlGGKPGTRGSGVPGKRVGY--MPQEIALYGE 165
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRV-EGRVEFFNQNIYERRVNLnrLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 ------FSIQETMMY----FGWIFGMETKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELLILD 233
Cdd:PRK14258 96 kpnlfpMSVYDNVAYgvkiVGWRPKLEIDDIVESALKDADLWDEIKHKihKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....*
gi 194201171 234 EPTVGVDPLLRQSIwNHLVHITK-AGQKTVIITTH 267
Cdd:PRK14258 176 EPCFGLDPIASMKV-ESLIQSLRlRSELTMVIVSH 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
86-297 |
2.05e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.83 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 86 KKNANQ---VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKpgtrgsgVPGKRVGYMPQEIAL 162
Cdd:PRK13650 13 KYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-------LTEENVWDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 Y-----GEF--SIQETMMYFGWIF-GMETKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILD 233
Cdd:PRK13650 86 VfqnpdNQFvgATVEDDVAFGLENkGIPHEEMKERVNEALELVGMQDFKeREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
67-286 |
2.07e-11 |
|
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: 66.73 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYgKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGRRYMDAGEIFVLGGKPgtrgs 146
Cdd:cd03248 5 PDHLKGIVKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVA-LLENFYQPQGGQVLLDGKP----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 gVPGKRVGYMPQEIALYGE----F--SIQETMMYfgWIFGMETKEILERLQ------FLLNFLDLPSEKRLVKN--LSGG 212
Cdd:cd03248 78 -ISQYEHKYLHSKVSLVGQepvlFarSLQDNIAY--GLQSCSFECVKEAAQkahahsFISELASGYDTEVGEKGsqLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 213 QQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIwnHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQV--QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
78-286 |
2.32e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.44 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 78 HAFKAYgkkKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTR--GSGVP--GKRV 153
Cdd:PRK10908 6 HVSKAY---LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW-FSGHDITRlkNREVPflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 154 GYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLIL 232
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKaKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 233 DEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHL 286
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGV-TVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
93-311 |
3.20e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.08 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEialyGEFSIQETM 172
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQN----PDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 MYFGWIFGME-----TKEILERLQFLLNFLDL----PSEKrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 243
Cdd:PRK13648 101 VKYDVAFGLEnhavpYDEMHRRVSEALKQVDMleraDYEP---NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 244 RQSIWNhLVHITKAGQKTVIIT-THYIEEARQAHTIGLMRSGHLLAEESPSvllSIYKCI-SLEEVFLKL 311
Cdd:PRK13648 178 RQNLLD-LVRKVKSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGTPT---EIFDHAeELTRIGLDL 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
77-297 |
4.11e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.52 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 77 RHAFKAYGKKKNANQVLN---------NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSG 147
Cdd:PRK10070 19 QRAFKYIEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 ----VPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPSEKR-LVKNLSGGQQRRVSFAVA 222
Cdd:PRK10070 99 elreVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHsYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 223 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
89-284 |
4.74e-11 |
|
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: 66.80 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 89 ANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtRGSGvpgkRVGYMPQeIALYGEFSI 168
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------KHSG----RISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMmyfgwIFGMETKE-----ILERLQFLLNFLDLPSEKRLVK-----NLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:cd03291 115 KENI-----IFGVSYDEyryksVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 194201171 239 VDPLLRQSIWNHLVHITKAgQKTVIITTHYIEEARQAHTIGLMRSG 284
Cdd:cd03291 190 LDVFTEKEIFESCVCKLMA-NKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
93-284 |
8.48e-11 |
|
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: 64.66 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR----VGYMPQEIALYGEfSI 168
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMMyFGWIFGMET-KEILE--RLQFLLNFLDLPSEKRLVK---NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 242
Cdd:cd03290 96 EENIT-FGSPFNKQRyKAVTDacSLQPDIDLLPFGDQTEIGErgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 194201171 243 LRQSIWNH-LVHITKAGQKTVIITTHYIEEARQAHTIGLMRSG 284
Cdd:cd03290 175 LSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| DUF3652 |
pfam12372 |
Huntingtin protein region; This domain family is found in eukaryotes, and is approximately 40 ... |
3353-3395 |
9.52e-11 |
|
Huntingtin protein region; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam02985. This family is in the middle region of the Huntingtin protein associated with Huntington's disease. The protein is of unknown function, however it is known that a polyglutamine (CAG) repeat in the gene coding for it results in the development of Huntington's disease.
Pssm-ID: 463554 Cd Length: 41 Bit Score: 59.38 E-value: 9.52e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 194201171 3353 ALLQQPRVW---RELNASLNPSLRCELLDLldsvaRCILQDTIFYR 3395
Cdd:pfam12372 1 AIIGQPRIIqlcDGLMASGQPAVRHEIPAL-----RPILQDTFFYR 41
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
84-275 |
1.05e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 84 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALY 163
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 164 GEfsiqetMMYFGWIFGMETKEILERLQFLLNFLD---LPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:PRK10247 94 GD------TVYDNLIFPWQIRNQQPDPAIFLDDLErfaLPDTilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 194201171 239 VDPLLRQSIwNHLVH-ITKAGQKTVIITTHYIEEARQA 275
Cdd:PRK10247 168 LDESNKHNV-NEIIHrYVREQNIAVLWVTHDKDEINHA 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
72-244 |
1.22e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.41 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 72 AAVSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK------PGTRG 145
Cdd:PRK11650 2 AGLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRvvnelePADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 146 sgvpgkrVGYMPQEIALYGEFSIQETMMYFGWIFGMETKEILERLQF------LLNFLDlpsekRLVKNLSGGQQRRVSF 219
Cdd:PRK11650 78 -------IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarileLEPLLD-----RKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|....*
gi 194201171 220 AVALMHDPELLILDEPTVGVDPLLR 244
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLR 170
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
92-280 |
1.44e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKRVGYMPQEIALYGEFSIQET 171
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-KLDGGDIDDPD--VAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 MMYFGWIFGMETKEILERLQF--LLNFLDLPSekrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP----LLRQ 245
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAvgLAPLAHLPF-----GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaavaLFAE 168
|
170 180 190
....*....|....*....|....*....|....*
gi 194201171 246 SIWNHLvhitkAGQKTVIITTHYIEEARQAHTIGL 280
Cdd:PRK13539 169 LIRAHL-----AQGGIVIAATHIPLGLPGARELDL 198
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
67-286 |
2.09e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.05 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 67 PRNTQAAVSVRHAFKAYGKKKNaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgS 146
Cdd:TIGR00958 472 PLNLEGLIEFQDVSFSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---------D 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 GVP---------GKRVGYMPQEIALYGEfSIQETMMYFGWIFGMETKEILERLQFLLNFL-DLPS-------EKRlvKNL 209
Cdd:TIGR00958 542 GVPlvqydhhylHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNgydtevgEKG--SQL 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 210 SGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNhlvhITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
95-267 |
2.38e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 95 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMY 174
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL-WQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 175 FGWIFGMETKE----ILERLQfLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLILDEP-----TVGVDPLLRq 245
Cdd:PRK13538 98 YQRLHGPGDDEalweALAQVG-LAGFEDVP-----VRQLSAGQQRRVALARLWLTRAPLWILDEPftaidKQGVARLEA- 170
|
170 180
....*....|....*....|...
gi 194201171 246 siwnHLV-HITKAGqkTVIITTH 267
Cdd:PRK13538 171 ----LLAqHAEQGG--MVILTTH 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
91-236 |
2.40e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP----GTRGSGVPGKRVGYmpQEIALYGEF 166
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-LIDGQEmrfaSTTAALAAGVAIIY--QELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETMMY------FGWI----FGMETKEILERLQfllnfLDL-PSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEP 235
Cdd:PRK11288 95 TVAENLYLgqlphkGGIVnrrlLNYEAREQLEHLG-----VDIdPDTP--LKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
.
gi 194201171 236 T 236
Cdd:PRK11288 168 T 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
84-274 |
2.73e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 84 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG---GKPGTRGSGVPGkrVGYMPQEI 160
Cdd:PRK09700 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAQLG--IGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETmMYFGW-----IFG---METKEILERLQFLLNFLDL---PSEKrlVKNLSGGQQRRVSFAVALMHDPEL 229
Cdd:PRK09700 90 SVIDELTVLEN-LYIGRhltkkVCGvniIDWREMRVRAAMMLLRVGLkvdLDEK--VANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 194201171 230 LILDEPTVG-----VDPLLrqSIWNHLvhitKAGQKTVIITTHYIEEARQ 274
Cdd:PRK09700 167 IIMDEPTSSltnkeVDYLF--LIMNQL----RKEGTAIVYISHKLAEIRR 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
65-236 |
3.14e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 65 NGPRNTQAAVSVRHAFKAYGKKknanqVL-NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgt 143
Cdd:PRK11819 316 PGPRLGDKVIEAENLSKSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 144 rGSGVpgkRVGYMPQ-------EIALYGEFSIQETMMYFGwifgmeTKEILERL---QFllNFLDLPSEKRlVKNLSGGQ 213
Cdd:PRK11819 384 -GETV---KLAYVDQsrdaldpNKTVWEEISGGLDIIKVG------NREIPSRAyvgRF--NFKGGDQQKK-VGVLSGGE 450
|
170 180
....*....|....*....|...
gi 194201171 214 QRRVSFAVALMHDPELLILDEPT 236
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
92-267 |
3.52e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtrGSGVPGKRVGYMpQEIALYGE------ 165
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-------RQSIKKDLCTYQ-KQLCFVGHrsginp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 -FSIQETmMYFGWIFGMETKEILE--RLQFLLNFLDLPSEKrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 242
Cdd:PRK13540 88 yLTLREN-CLYDIHFSPGAVGITElcRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*.
gi 194201171 243 LRQSIWNHL-VHITKAGqkTVIITTH 267
Cdd:PRK13540 162 SLLTIITKIqEHRAKGG--AVLLTSH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
63-277 |
3.68e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 63 PANGPRntqaaVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKpg 142
Cdd:PRK10938 255 PANEPR-----IVLNNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGR-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 143 TRGSGVP----GKRVGYMPQEIALygEFSIQETMM------YFGWIfGMeTKEILERLQFL----LNFLDLPSE--KRLV 206
Cdd:PRK10938 324 RRGSGETiwdiKKHIGYVSSSLHL--DYRVSTSVRnvilsgFFDSI-GI-YQAVSDRQQKLaqqwLDILGIDKRtaDAPF 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 207 KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHT 277
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACIT 470
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
87-267 |
4.18e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 87 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKRVGYMPQEIALYGEF 166
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGD--RSRFMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETMMYFGWIFGMETKEILERLQFLLNFLDlpSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP----L 242
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQMPGSALAIVGLAG--YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLegitL 175
|
170 180
....*....|....*....|....*
gi 194201171 243 LRQSIWNHLvhitkAGQKTVIITTH 267
Cdd:PRK13543 176 VNRMISAHL-----RGGGAALVTTH 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
69-285 |
5.07e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.41 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGKKKNanqvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTR---G 145
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 146 SGVPGKRV------GYMPQEIA--LYGEFS----IQETMMYFGW----------IFGMETKEI-LERLQfllnflDLPSe 202
Cdd:PRK11701 78 LSEAERRRllrtewGFVHQHPRdgLRMQVSaggnIGERLMAVGArhygdirataGDWLERVEIdAARID------DLPT- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 203 krlvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD--------PLLRQsiwnhLVHITkagQKTVIITTHYIEEARQ 274
Cdd:PRK11701 151 -----TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarllDLLRG-----LVREL---GLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 194201171 275 -AHTIGLMRSGH 285
Cdd:PRK11701 218 lAHRLLVMKQGR 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
91-236 |
5.24e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLgGKP----GTRGSGVPGkrVGYMPQEIALYGEF 166
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL-GKEvtfnGPKSSQEAG--IGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETmmyfgwIF-GMETKEILERLQF---------LLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEP 235
Cdd:PRK10762 95 TIAEN------IFlGREFVNRFGRIDWkkmyaeadkLLARLNLRfSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
.
gi 194201171 236 T 236
Cdd:PRK10762 169 T 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
91-269 |
6.21e-10 |
|
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: 62.81 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIY-----GLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtrgsGVPGKRVGYMPQEIALYGE 165
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 166 FSIQETMMYFGWIFGMETK---EILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 242
Cdd:cd03237 76 GTVRDLLSSITKDFYTHPYfktEIAKPLQ-IEQILD-----REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190
....*....|....*....|....*....|....
gi 194201171 243 LRqsiwnhlVHITKA-------GQKTVIITTHYI 269
Cdd:cd03237 150 QR-------LMASKVirrfaenNEKTAFVVEHDI 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
81-267 |
8.63e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrryMDA---GEIFVLggkpgtrgsgvPGKRVGYMP 157
Cdd:PRK11819 14 KVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKefeGEARPA-----------PGIKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 QEIALYGEFSIQETMMYfgwifGM-ETKEILER------------------------LQFLLNFLD-------------- 198
Cdd:PRK11819 77 QEPQLDPEKTVRENVEE-----GVaEVKAALDRfneiyaayaepdadfdalaaeqgeLQEIIDAADawdldsqleiamda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 199 --LPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTvgvdpllrqsiwNHL----V-----HITK-AGqkTVIITT 266
Cdd:PRK11819 152 lrCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT------------NHLdaesVawleqFLHDyPG--TVVAVT 217
|
.
gi 194201171 267 H 267
Cdd:PRK11819 218 H 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
92-241 |
9.90e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTiyGLL--GASGCGKTTLLSCIV-------GR-RYMDAGEIFVLGGKPgtrgsgvpgkrvgYMPQ--- 158
Cdd:COG4178 378 LLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAglwpygsGRiARPAGARVLFLPQRP-------------YLPLgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 -EIALY----GEFSiQETMmyfgwifgmetKEILER--LQFLLNFLDLpsEKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:COG4178 443 rEALLYpataEAFS-DAEL-----------REALEAvgLGHLAERLDE--EADWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170
....*....|
gi 194201171 232 LDEPTVGVDP 241
Cdd:COG4178 509 LDEATSALDE 518
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
73-289 |
1.15e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 73 AVSVRHAFKAYgKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR-RYMDAGEIFVlggkpgtRGSgvpgk 151
Cdd:PLN03232 614 AISIKNGYFSW-DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVI-------RGS----- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 rVGYMPQEIALYGEfSIQETMMyFGWIFGMETKEILERLQFLLNFLDLPSEKRLVK------NLSGGQQRRVSFAVALMH 225
Cdd:PLN03232 681 -VAYVPQVSWIFNA-TVRENIL-FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEigergvNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 226 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITThyieearQAHTIGLMRSGHLLAE 289
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTN-------QLHFLPLMDRIILVSE 814
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
81-267 |
1.22e-09 |
|
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: 64.19 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgsgVPGKRVGYMPQEI 160
Cdd:TIGR03719 12 KVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYfgwifGM-ETKEILER------------------------LQFLL----------------NFLDL 199
Cdd:TIGR03719 78 QLDPTKTVRENVEE-----GVaEIKDALDRfneisakyaepdadfdklaaeqaeLQEIIdaadawdldsqleiamDALRC 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 200 PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPllrQSI-W--NHLvhitKAGQKTVIITTH 267
Cdd:TIGR03719 153 PPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVaWleRHL----QEYPGTVVAVTH 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
93-288 |
1.27e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR-VGYMPQEIALYGEFSIQET 171
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 M----------------MYfgwifgMETKEILERLQFLLNfldlPSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEP 235
Cdd:PRK10982 94 MwlgryptkgmfvdqdkMY------RDTKAIFDELDIDID----PRAK--VATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194201171 236 TVGvdplLRQSIWNHLVHITKAGQKT---VIITTHYIEEARQ-AHTIGLMRSGHLLA 288
Cdd:PRK10982 162 TSS----LTEKEVNHLFTIIRKLKERgcgIVYISHKMEEIFQlCDEITILRDGQWIA 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
91-241 |
1.47e-09 |
|
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: 61.30 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRrYM-DAGEIFVLggkpgTRGSGVPgkRVGYMPQEI-ALYgefsi 168
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGN-YLpDSGSILVR-----HDGGWVD--LAQASPREIlALR----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMmyfGWI--F--------------------GMETKEILERLQFLLNFLDLPseKRL----VKNLSGGQQRRVSFAVA 222
Cdd:COG4778 92 RRTI---GYVsqFlrviprvsaldvvaepllerGVDREEARARARELLARLNLP--ERLwdlpPATFSGGEQQRVNIARG 166
|
170
....*....|....*....
gi 194201171 223 LMHDPELLILDEPTVGVDP 241
Cdd:COG4778 167 FIADPPLLLLDEPTASLDA 185
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
82-236 |
2.22e-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: 63.55 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 82 AYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKT-TLLScIVG----RRYMDAGEIFVLG----GKPGTRGSGVPGKR 152
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRllpdPAAHPSGSILFDGqdllGLSERELRRIRGNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 153 VGYMPQE--IALYGEFSIQ----ETMMyfgWIFGMETKEILERLQFLLNFLDLPSEKRLVK----NLSGGQQRRVSFAVA 222
Cdd:COG4172 94 IAMIFQEpmTSLNPLHTIGkqiaEVLR---LHRGLSGAAARARALELLERVGIPDPERRLDayphQLSGGQRQRVMIAMA 170
|
170
....*....|....
gi 194201171 223 LMHDPELLILDEPT 236
Cdd:COG4172 171 LANEPDLLIADEPT 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
93-236 |
2.37e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIY-----GLLGASGCGKTTLLScivgrryMDAGEIfvlggKPgTRGSGVPGKRVGYMPQEIALYGEFS 167
Cdd:PRK13409 350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAK-------LLAGVL-----KP-DEGEVDPELKISYKPQYIKPDYDGT 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 168 IQETMMYFGWIFG--METKEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:PRK13409 417 VEDLLRSITDDLGssYYKSEIIKPLQ-LERLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
92-285 |
2.48e-09 |
|
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: 64.16 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtRGSGvpgkRVGYMPQeIALYGEFSIQET 171
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------KHSG----RISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 172 MmyfgwIFGMETKE-----ILERLQFLLNFLDLPSEKRLVK-----NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:TIGR01271 507 I-----IFGLSYDEyrytsVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 194201171 242 LLRQSIWNHLVHITKAgQKTVIITTHYIEEARQAHTIGLMRSGH 285
Cdd:TIGR01271 582 VTEKEIFESCLCKLMS-NKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
93-304 |
4.12e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG-RRYMD-AGEIFvLGGKP----GTRGSGVPGKRVGYmpQEIALYGEF 166
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEII-FEGEElqasNIRDTERAGIAIIH--QELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQETM------MYFGWI----FGMETKEILERLQFLLNfldlPSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:PRK13549 98 SVLENIflgneiTPGGIMdydaMYLRAQKLLAQLKLDIN----PATP--VGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194201171 237 VgvdPLLRQSIwNHLVHIT---KAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEEsPSVLLSIYKCISL 304
Cdd:PRK13549 172 A---SLTESET-AVLLDIIrdlKAHGIACIYISHKLNEvKAISDTICVIRDGRHIGTR-PAAGMTEDDIITM 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
94-240 |
4.24e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 94 NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSGVPG--KRVGYMPQ---EIALYGEFSI 168
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR-LNGKDISPRSPLDAvkKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETMMY--------FGWIFGM----ETKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:PRK09700 359 AQNMAIsrslkdggYKGAMGLfhevDEQRTAENQRELLA-LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
....
gi 194201171 237 VGVD 240
Cdd:PRK09700 438 RGID 441
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-293 |
4.61e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSC-------IVGRRYmdAGEIfVLGGKP--GTRGSGVPGKRVGYMPQEIAL 162
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDV-LLGGRSifNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YgEFSIQETMMYfgwifGMETKEILERLQFL------LNFLDL--PSEKRLVKN---LSGGQQRRVSFAVALMHDPELLI 231
Cdd:PRK14271 113 F-PMSIMDNVLA-----GVRAHKLVPRKEFRgvaqarLTEVGLwdAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 232 LDEPTVGVDPLLRQSIWNHLVHItkAGQKTVIITTHYI-EEARQAHTIGLMRSGHLLaEESPS 293
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLaQAARISDRAALFFDGRLV-EEGPT 246
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-267 |
5.64e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 4 KKEATLSQQQTQQPIMDLERIKRHFSWSDPSaiISTDSAMAATNNDGGTQPNAVAAWGApANGPRNTQAAV--------- 74
Cdd:PLN03140 793 KKQAIISEETAEEMEGEEDSIPRSLSSADGN--NTREVAIQRMSNPEGLSKNRDSSLEA-ANGVAPKRGMVlpftplams 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 75 --SVRH------AFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR---YMDaGEIfvlggkpgt 143
Cdd:PLN03140 870 fdDVNYfvdmpaEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtggYIE-GDI--------- 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 144 RGSGVPGKR------VGYMPQEIALYGEFSIQETMMYFGwiFGMETKEIL--ERLQFLLNFLDLPSEKRL---------V 206
Cdd:PLN03140 940 RISGFPKKQetfariSGYCEQNDIHSPQVTVRESLIYSA--FLRLPKEVSkeEKMMFVDEVMELVELDNLkdaivglpgV 1017
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194201171 207 KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPlLRQSIWNHLVHITKAGQKTVIITTH 267
Cdd:PLN03140 1018 TGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA-RAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
87-297 |
7.19e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 87 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--------RRYMDAGEIfVLGGKPGTRgsgVPGKRVG---- 154
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDV-TLNGEPLAA---IDAPRLArlra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMPQEIALYGEFSIQETMM-------YFGWIFGMETKEILERLQFLLNFLDLpsEKRLVKNLSGGQQRRVSFAVAL---- 223
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIVLlgryphaRRAGALTHRDGEIAWQALALAGATAL--VGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 224 -----MHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
76-240 |
7.20e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 76 VRHaFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR---RYmdAGEIFVLGGKPGTRGSG----- 147
Cdd:PRK13549 262 VRN-LTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAypgRW--EGEIFIDGKPVKIRNPQqaiaq 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 148 ----VPG--KRVGYMP-----QEIAL--YGEFS----IQEtmmyfgwifGMETKEILERLQFLLnfLDLPSEKRLVKNLS 210
Cdd:PRK13549 339 giamVPEdrKRDGIVPvmgvgKNITLaaLDRFTggsrIDD---------AAELKTILESIQRLK--VKTASPELAIARLS 407
|
170 180 190
....*....|....*....|....*....|
gi 194201171 211 GGQQRRVSFAVALMHDPELLILDEPTVGVD 240
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
79-286 |
7.91e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 79 AFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDA--GEIfvlggkpgtRGSGVPGKRVgym 156
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVseGDI---------RFHDIPLTKL--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 157 pQEIALYGEFSI--QETMMYFGWIFGM-------ETKEILERLQFLLN----FLDLPS-------EKRLVknLSGGQQRR 216
Cdd:PRK10789 383 -QLDSWRSRLAVvsQTPFLFSDTVANNialgrpdATQQEIEHVARLASvhddILRLPQgydtevgERGVM--LSGGQKQR 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 217 VSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
74-295 |
8.92e-09 |
|
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: 61.38 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDA--GEIFVLGGKPGTRG-SGVPG 150
Cdd:TIGR02633 2 LEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 KRVGYMPQEIALYGEFSIQETMMYFGWI----FGMETKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALM 224
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNvtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 225 HDPELLILDEPTVGvdpLLRQ--SIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVL 295
Cdd:TIGR02633 158 KQARLLILDEPSSS---LTEKetEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
70-285 |
1.24e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 70 TQAAVSVRHAFKAYGKKKNanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP-GTRGSGV 148
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR-LDGRPlSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PGKRVGYMPQE-IALYGEFSIQETMmyfgwifGMETKE-----ILERLQFLLNFLDLPS--EKRLVK---NLSGGQQRRV 217
Cdd:PRK10790 413 LRQGVAMVQQDpVVLADTFLANVTL-------GRDISEeqvwqALETVQLAELARSLPDglYTPLGEqgnNLSVGQKQLL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 218 SFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGH 285
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
93-234 |
1.74e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.67 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTR-GSGVPGKRVGYmpQEIALYGefsiqeT 171
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAiSSGLNGQLTGI--ENIELKG------L 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 172 MMyfgwifGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:PRK13545 112 MM------GLTKEKIKEIIPEIIEFADIGKfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
93-236 |
2.83e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIY-----GLLGASGCGKTTLLScivgrryMDAGEIfvlggKPgTRGSGVPGKRVGYMPQEIalygEFS 167
Cdd:COG1245 351 YGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAK-------ILAGVL-----KP-DEGEVDEDLKISYKPQYI----SPD 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 168 IQETMMYF-----GWIFG--METKEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:COG1245 414 YDGTVEEFlrsanTDDFGssYYKTEIIKPLG-LEKLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
92-297 |
3.47e-08 |
|
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: 59.73 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 92 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgSGVP---------GKRVGYMPQEIAL 162
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL---------DGHDladytlaslRRQVALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YGEfSIQETMMYfGWIFGMETKEILERLQ--FLLNFLD-LPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:TIGR02203 418 FND-TIANNIAY-GRTEQADRAEIERALAaaYAQDFVDkLPLGLDTPigengVLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194201171 235 PTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
91-240 |
4.41e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMD--AGEIFvLGGKPgTRGSGVP---GKRVGYMPQEIALYG- 164
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVF-KDGKE-VDVSTVSdaiDAGLAYVTEDRKGYGl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 165 --EFSIQETMMY--------FGWIFGMETKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 234
Cdd:NF040905 352 nlIDDIKRNITLanlgkvsrRGVIDENEEIKVAEEYRKKMN-IKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
....*.
gi 194201171 235 PTVGVD 240
Cdd:NF040905 431 PTRGID 436
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
88-235 |
4.75e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.35 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTV----PKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK---PGTRGSGVP--GKRVGYMPQ 158
Cdd:PRK11144 5 NFKQQLGDLCLTVnltlPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRvlfDAEKGICLPpeKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 EIALYGEFSIQETMMYfgwifGMETKEileRLQF--LLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEP 235
Cdd:PRK11144 84 DARLFPHYKVRGNLRY-----GMAKSM---VAQFdkIVALLGIePLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
209-286 |
8.31e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 8.31e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 209 LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHL 286
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-269 |
9.19e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 2 APKKEATLSQQQTQQPIMDLERIKRHFSwsDPSAII-STDSAMAATNNDGGTQPNAVAAWGAPANGPRNTQAAVSVRHAF 80
Cdd:PTZ00243 590 APKVKTSLLSRALRMLCCEQCRPTKRHP--SPSVVVeDTDYGSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDF 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 81 KAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgsgvpGKRVGYMPQEi 160
Cdd:PTZ00243 668 FELEPKV----LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQ- 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 161 ALYGEFSIQETMMYFgwifgmeTKEILERLQFLLNFLDLPSEKRLVK------------NLSGGQQRRVSFAVALMHDPE 228
Cdd:PTZ00243 730 AWIMNATVRGNILFF-------DEEDAARLADAVRVSQLEADLAQLGggleteigekgvNLSGGQKARVSLARAVYANRD 802
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 194201171 229 LLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYI 269
Cdd:PTZ00243 803 VYLLDDPLSALDAHVGERVVEECFLGALAG-KTRVLATHQV 842
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
90-270 |
1.15e-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: 58.38 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL------- 162
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIfsgtfrk 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 ----YGEFSIQETmmyfgWIFGMET--KEILERLQFLLNFLdlpsekrLVKN---LSGGQQRRVSFAVALMHDPELLILD 233
Cdd:TIGR01271 1311 nldpYEQWSDEEI-----WKVAEEVglKSVIEQFPDKLDFV-------LVDGgyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|....*..
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHitKAGQKTVIITTHYIE 270
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVE 1413
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
71-284 |
3.11e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 71 QAAVSVRHAFKAYgKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtRGSgvpg 150
Cdd:PLN03130 612 LPAISIKNGYFSW-DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI------RGT---- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 151 krVGYMPQeIALYGEFSIQETMMyFGWIFGMETKEILERLQFLLNFLDLPSEKRLVK------NLSGGQQRRVSFAVALM 224
Cdd:PLN03130 681 --VAYVPQ-VSWIFNATVRDNIL-FGSPFDPERYERAIDVTALQHDLDLLPGGDLTEigergvNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 225 HDPELLILDEPTVGVDPLLRQSIWNHLVHiTKAGQKTVIITTHYIEEARQAHTIGLMRSG 284
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
88-270 |
4.37e-07 |
|
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: 54.04 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgSGVPGKRVGymPQEiaLYGEFS 167
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI---------DGVDISKIG--LHD--LRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 168 I--QETMMYFGWI------FGMETKE----ILERLQFLLNFLDLPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELL 230
Cdd:cd03244 82 IipQDPVLFSGTIrsnldpFGEYSDEelwqALERVGLKEFVESLPGGLDTVveeggENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 194201171 231 ILDEPTVGVDP----LLRQSIWNHLVHitkagqKTVIITTHYIE 270
Cdd:cd03244 162 VLDEATASVDPetdaLIQKTIREAFKD------CTVLTIAHRLD 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
74-315 |
5.76e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.80 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 74 VSVRHAFKAY-GKKKNAnqvLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGRRY-MDAGEIFVLGgkPGTRGSGVPGK 151
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPA---LRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYdIDEGEILLDG--HDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 152 R--VGYMPQEIALYGEfSIQETMMY-FGWIFGMETKEILERLQFLLNFLD-LPSEKRLV--KN---LSGGQQRRVSFAVA 222
Cdd:PRK11176 416 RnqVALVSQNVHLFND-TIANNIAYaRTEQYSREQIEEAARMAYAMDFINkMDNGLDTVigENgvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 223 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLsiykci 302
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL------ 566
|
250
....*....|...
gi 194201171 303 SLEEVFLKLSRIQ 315
Cdd:PRK11176 567 AQNGVYAQLHKMQ 579
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
88-268 |
7.25e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDageifVLGGKPGTRGSGVPGKRvgymPQEIALYGEF- 166
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK-----ILEGDILFKGESILDLE----PEERAHLGIFl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 167 SIQetmmYFGWIFGMETKEILE-----RLQFL-------LNFLDLPSEK-RLVK------------NLSGGQQRRVSFAV 221
Cdd:CHL00131 89 AFQ----YPIEIPGVSNADFLRlaynsKRKFQglpeldpLEFLEIINEKlKLVGmdpsflsrnvneGFSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 194201171 222 ALMHDPELLILDEPTVGVDPLLRQSIwNHLVHITKAGQKTVIITTHY 268
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKII-AEGINKLMTSENSIILITHY 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
207-300 |
9.11e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 207 KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTI-------- 278
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIvvfnnpdr 1436
|
90 100
....*....|....*....|...
gi 194201171 279 -GLMRSGHLLAEESPSVLLSIYK 300
Cdd:PTZ00265 1437 tGSFVQAHGTHEELLSVQDGVYK 1459
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
93-236 |
1.19e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG----RRYmdAGEIfVLGGKP----GTRGSgvpgKRVGY--MPQEIAL 162
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphGSY--EGEI-LFDGEVcrfkDIRDS----EALGIviIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YGEFSIQETMMY------FGWI----FGMETKEILER--LQfllnflDLPSEkrLVKNLSGGQQRRVSFAVALMHDPELL 230
Cdd:NF040905 90 IPYLSIAENIFLgnerakRGVIdwneTNRRARELLAKvgLD------ESPDT--LVTDIGVGKQQLVEIAKALSKDVKLL 161
|
....*.
gi 194201171 231 ILDEPT 236
Cdd:NF040905 162 ILDEPT 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
209-411 |
1.30e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 209 LSGGQQRRVSFAVALMHDPELLILDEPTVGVD---PLLRQSIWNHLvhitKAGQ-KTVIITTHYIEEARQAHTIGLMRSg 284
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVQKTINNL----KGNEnRITIIIAHRLSTIRYANTIFVLSN- 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 285 hllAEESPSVLLSIykcisLEEVFLKLSRIQSQKGDVTHVNFSNNISlhamafGSKMDKPSSSqeggVVGLNFHQSkevL 364
Cdd:PTZ00265 655 ---RERGSTVDVDI-----IGEDPTKDNKENNNKNNKDDNNNNNNNN------NNKINNAGSY----IIEQGTHDA---L 713
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194201171 365 INDSNGSIYTL-NQEPYSPPPSrrNNNPNDEEScqDCYSNLCKITSKG 411
Cdd:PTZ00265 714 MKNKNGIYYTMiNNQKVSSKKS--SNNDNDKDS--DMKSSAYKDSERG 757
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
93-286 |
1.52e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTrgsgvPGKRVGYMPQEIALYGEFSIqetm 172
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVT-----AEQPEDYRKLFSAVFTDFHL---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 173 myFGWIFGMETKEI--------LERLQfLLNFLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 244
Cdd:PRK10522 409 --FDQLLGPEGKPAnpalvekwLERLK-MAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 194201171 245 QSIWNHLVHITKAGQKTVIITTH---YIEearQAHTIGLMRSGHL 286
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHddhYFI---HADRLLEMRNGQL 527
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
97-289 |
1.57e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 97 NMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYM--PQE------IALYgefSI 168
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-YLDGKPIDIRSPRDAIRAGIMlcPEDrkaegiIPVH---SV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 169 QETM--------MYFGWI--FGMETKEILERLQfLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 238
Cdd:PRK11288 349 ADNInisarrhhLRAGCLinNRWEAENADRFIR-SLN-IKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 194201171 239 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 289
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
69-297 |
2.02e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 69 NTQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKT-TLLSCIvgrRYMDAGEIFVLGGKPGTRGS- 146
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL---RLLPSPPVVYPSGDIRFHGEs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 147 ----------GVPGKRVGYMPQE--IALYGEFSIqETMMY--FGWIFGMETK----EI---LERL---QFLLNFLDLPSE 202
Cdd:PRK15134 78 llhaseqtlrGVRGNKIAMIFQEpmVSLNPLHTL-EKQLYevLSLHRGMRREaargEIlncLDRVgirQAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 203 krlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLM 281
Cdd:PRK15134 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVM 230
|
250
....*....|....*.
gi 194201171 282 RSGHLLAEESPSVLLS 297
Cdd:PRK15134 231 QNGRCVEQNRAATLFS 246
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
90-297 |
2.55e-06 |
|
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: 52.16 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDaGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL------- 162
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIfsgtfrk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 ----YGEFSIQETmmyfgWIFGMET--KEILERLQFLLNFLdlpsekrLVKN---LSGGQQRRVSFAVALMHDPELLILD 233
Cdd:cd03289 96 nldpYGKWSDEEI-----WKVAEEVglKSVIEQFPGQLDFV-------LVDGgcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194201171 234 EPTVGVDPLLRQSIWNHLVHitKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 297
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
84-286 |
2.66e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 84 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTlLSCIVGrrymdageifvlGGKPGTRGSGVPGKRVGYMPQEIALY 163
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKST-LSNIIG------------GSLSPTVGKVDRNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 164 GEFSIQETMMYFGWIFGMETKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEP-TVGVDP 241
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 194201171 242 LLRQSIwnHLVHITKAGQKTVIITTHYIEEARQAHT-IGLMRSGHL 286
Cdd:PRK13546 178 FAQKCL--DKIYEFKEQNKTIFFVSHNLGQVRQFCTkIAWIEGGKL 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
93-289 |
2.85e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR---RYmdAGEIFVLGGKPGTRGSG---------VPG--KRVGYMP- 157
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAypgKF--EGNVFINGKPVDIRNPAqairagiamVPEdrKRHGIVPi 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 158 ----QEIALygefSIQETMMYFGWI-FGMETKEILE---RLQFLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPEL 229
Cdd:TIGR02633 354 lgvgKNITL----SVLKSFCFKMRIdAAAELQIIGSaiqRLKVKTASPFLP-----IGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 230 LILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 289
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
88-241 |
2.92e-06 |
|
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: 50.23 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 88 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlgGKPgtrgsgvPGKRVGYMPQEialygefs 167
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMP-------EGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 168 iqeTMMYFGwifgmeT-KEILERlqfllnfldlPSEKRLvknlSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 241
Cdd:cd03223 73 ---PYLPLG------TlREQLIY----------PWDDVL----SGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
102-278 |
3.42e-06 |
|
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: 49.68 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 102 KGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGsgvpgkrvgympqeialygefsiqetmmyfgwifgm 181
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEE------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 182 etkeilerlqfLLNFLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP-----LLRQSIWNHLVHITK 256
Cdd:smart00382 45 -----------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLLLLKS 113
|
170 180
....*....|....*....|..
gi 194201171 257 AGQKTVIITTHYIEEARQAHTI 278
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLR 135
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
89-251 |
5.21e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 89 ANQVL-NNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgrrymdaGEIFVLGGkpGTRGSGVPGKrVGYMPQEiALYGEFS 167
Cdd:TIGR00954 463 NGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELWPVYG--GRLTKPAKGK-LFYVPQR-PYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 168 IQETMMYFGWIFGM--------ETKEILERLQfLLNFLDLPSEKRLVKN----LSGGQQRRVSFAVALMHDPELLILDEP 235
Cdd:TIGR00954 531 LRDQIIYPDSSEDMkrrglsdkDLEQILDNVQ-LTHILEREGGWSAVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170
....*....|....*.
gi 194201171 236 TVGVDPLLRQSIWNHL 251
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLC 625
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
96-292 |
5.65e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 96 LNMTVPKGTIYGLLGASGCGKTTLLSCIVGRrYMDAGEIFvLGGKPGTRGSGVP-GKRVGY----------MP--QEIAL 162
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQ-FAGQPLEAWSAAElARHRAYlsqqqtppfaMPvfQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 YGEFSIQETmmyfgwifgmETKEILERLQFLLNFLD-LPsekRLVKNLSGGQQRRVSFA-VALMHDPE------LLILDE 234
Cdd:PRK03695 93 HQPDKTRTE----------AVASALNEVAEALGLDDkLG---RSVNQLSGGEWQRVRLAaVVLQVWPDinpagqLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 235 PTVGVDpLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESP 292
Cdd:PRK03695 160 PMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRR 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
90-268 |
5.94e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRymdagEIFVLGGKPGTRGSGV----PGKRVG---YM----PQ 158
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-----DYEVTGGTVEFKGKDLlelsPEDRAGegiFMafqyPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 EI-ALYGEFSIQETMmyfGWIFGMETKEILERLQFL------LNFLDLPSE--KRLVK-NLSGGQQRRVSFAVALMHDPE 228
Cdd:PRK09580 89 EIpGVSNQFFLQTAL---NAVRSYRGQEPLDRFDFQdlmeekIALLKMPEDllTRSVNvGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 194201171 229 LLILDEPTVGVDpLLRQSIWNHLVHITKAGQKTVIITTHY 268
Cdd:PRK09580 166 LCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
84-236 |
9.34e-06 |
|
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: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 84 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMDA-GEIFVLGgkpgTRGSGVPGKRVGYMPQEIAL 162
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALL--RLIPSeGEIRFDG----QDLDGLSRRALRPLRRRMQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 -----YGEFS--------IQETMMYFGwiFGMETKEILERLQFLLNFLDLPSEKRlvkN-----LSGGQQRRVSFAVALM 224
Cdd:COG4172 367 vfqdpFGSLSprmtvgqiIAEGLRVHG--PGLSAAERRARVAEALEEVGLDPAAR---HrypheFSGGQRQRIAIARALI 441
|
170
....*....|..
gi 194201171 225 HDPELLILDEPT 236
Cdd:COG4172 442 LEPKLLVLDEPT 453
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
176-251 |
1.69e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194201171 176 GWIFGMETKEILERLqfllnflDLPSEKRLvKNLSGGQQRRVSFAVALMHDPELLILDEPTvgvdpllrqsiwNHL 251
Cdd:PRK11147 132 LWQLENRINEVLAQL-------GLDPDAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPT------------NHL 187
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
93-278 |
1.95e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTL-LSCIVG---RRYMD-----AGEIFVLGGKPGT---------------RGSGV 148
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAegqRRYVEslsayARQFLGQMDKPDVdsieglspaiaidqkTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PGKRVGympqeialygefSIQETMMYFGWIFGMETkeILERLQFLLNF-LDLPSEKRLVKNLSGGQQRRVSFAVALMHDP 227
Cdd:cd03270 91 PRSTVG------------TVTEIYDYLRLLFARVG--IRERLGFLVDVgLGYLTLSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194201171 228 E--LLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHTI 278
Cdd:cd03270 157 TgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHV 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
93-266 |
2.62e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 93 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYM-----PQEIALYGEFS 167
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI-TLHGKKINNHNANEAINHGFAlvteeRRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 168 IQETMM------YFGWIFGMETKEILERLQFLLNFLDL--PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 239
Cdd:PRK10982 343 IGFNSLisnirnYKNKVGLLDNSRMKSDTQWVIDSMRVktPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180
....*....|....*....|....*..
gi 194201171 240 DPLLRQSIWNHLVHITKAGQKTVIITT 266
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISS 449
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
61-284 |
3.47e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 61 GAPANGPRNTQAAVSVRHAFKAYGKKK-------NANQVLNNLNMTVPKGTIYGLLGASGCGKTT----LLSCIVGRrym 129
Cdd:PRK15134 263 GDPVPLPEPASPLLDVEQLQVAFPIRKgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ--- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 130 daGEIfVLGGKP---GTRGSGVPGKR---VGYMPQEIALYGEFSIQETMmyfgwifgmetKEILERLQFLLNF------- 196
Cdd:PRK15134 340 --GEI-WFDGQPlhnLNRRQLLPVRHriqVVFQDPNSSLNPRLNVLQII-----------EEGLRVHQPTLSAaqreqqv 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 197 --------LDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHY 268
Cdd:PRK15134 406 iavmeevgLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
250
....*....|....*..
gi 194201171 269 IEEARQ-AHTIGLMRSG 284
Cdd:PRK15134 486 LHVVRAlCHQVIVLRQG 502
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
209-289 |
4.17e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 209 LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLL 287
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVV 233
|
..
gi 194201171 288 AE 289
Cdd:PRK11022 234 ET 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
94-267 |
8.44e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 94 NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrrymdageifVLGGKPGTRGSGV-PGKRVGYMPQ---------EIAL- 162
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMG----------LLAANGRIGGSATfNGREILNLPEkelnklraeQISMi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 163 ----------YGEFSIQ--ETMMYFGwifGMETKEILERLQFLLNFLDLPSEKRLVK----NLSGGQQRRVSFAVALMHD 226
Cdd:PRK09473 103 fqdpmtslnpYMRVGEQlmEVLMLHK---GMSKAEAFEESVRMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 194201171 227 PELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH 267
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
91-284 |
8.56e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---RRYMDAGEIFVLGGKPGTRGSgvPGKRVGYMPQEIALYgefs 167
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkDNWHVTADRFRWNGIDLLKLS--PRERRKIIGREIAMI---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 168 IQETMMYF--------------------GWI---FGMETKEILErlqfLLNFLDLPSEKRLVKN----LSGGQQRRVSFA 220
Cdd:COG4170 95 FQEPSSCLdpsakigdqlieaipswtfkGKWwqrFKWRKKRAIE----LLHRVGIKDHKDIMNSypheLTEGECQKVMIA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 221 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSG 284
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESiSQWADTITVLYCG 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
204-286 |
1.31e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 204 RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRS 283
Cdd:PRK10938 131 RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
...
gi 194201171 284 GHL 286
Cdd:PRK10938 211 CTL 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
100-236 |
2.18e-04 |
|
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: 47.47 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 100 VPK-GTIYGLLGASGCGKTTLLScIVgrrymdAGEIFV-LG--GKPGT--------RGSG--------VPGK-RVGYMPQ 158
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALK-IL------SGELKPnLGdyDEEPSwdevlkrfRGTElqdyfkklANGEiKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 159 EIALYGEFsiqetmmyfgwiFGMETKEILER------LQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLI 231
Cdd:COG1245 168 YVDLIPKV------------FKGTVRELLEKvdergkLDELAEKLGLeNILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
....*
gi 194201171 232 LDEPT 236
Cdd:COG1245 236 FDEPS 240
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
90-280 |
2.25e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 90 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGKRVGYMPQEIALYGEFSIQ 169
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY----KNCNINNIAKPYCTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 170 ETMMYFGWIFgmETKEILERLQFLLNFLDLPSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWN 249
Cdd:PRK13541 89 ENLKFWSEIY--NSAETLYAAIHYFKLHDLLDEK--CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
170 180 190
....*....|....*....|....*....|.
gi 194201171 250 HLVHITKAGqKTVIITTHYIEEARQAHTIGL 280
Cdd:PRK13541 165 LIVMKANSG-GIVLLSSHLESSIKSAQILQL 194
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
100-267 |
2.43e-04 |
|
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: 44.87 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 100 VPKGTIYGLLGASGCGKTTLLSCIVGRRymdageifvlggKPGTRGSGVPGKRVGYMPQEIalygefsiqetmmyfgwif 179
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQL------------IPNGDNDEWDGITPVYKPQYI------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 180 gmetkeilerlqfllnfldlpsekrlvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQ 259
Cdd:cd03222 71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
....*...
gi 194201171 260 KTVIITTH 267
Cdd:cd03222 123 KTALVVEH 130
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
604-755 |
3.04e-04 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 45.19 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 604 TMNPSFTDFVApGVILTIVFFLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVVF 683
Cdd:COG1277 44 GLGLALLASLF-SLLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGKFLGALLVLLLALLITFLLALLLG 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 684 GVTN------NGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLsgVIWPIegMPVVLRYISL 755
Cdd:COG1277 123 LLLFgspppdLGAILGFYLGLLLLGLAFLAIGLFISALTRNQIVAAILAIALWLLLVIL--LAWIV--LFLALAYLRF 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
205-279 |
4.19e-04 |
|
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: 43.89 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 205 LVKNLSGGQQRRV--SFAVALMHDPE--LLILDEPTVGVDPLLRQSIWNHLVHITKaGQKTVIITTHY---IEEARQAHT 277
Cdd:cd03227 74 TRLQLSGGEKELSalALILALASLKPrpLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLpelAELADKLIH 152
|
..
gi 194201171 278 IG 279
Cdd:cd03227 153 IK 154
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
91-240 |
5.86e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTL---LSCI----VGRRYMDAGEifVLGGKPGTR---------------GSGV 148
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIetptGGELYYQGQD--LLKADPEAQkllrqkiqivfqnpyGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 149 PGKRVGYMPQE-IALYGEFSIQETMmyfgwifgmetkeilERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMH 225
Cdd:PRK11308 107 PRKKVGQILEEpLLINTSLSAAERR---------------EKALAMMAKVGLRPEhyDRYPHMFSGGQRQRIAIARALML 171
|
170
....*....|....*
gi 194201171 226 DPELLILDEPTVGVD 240
Cdd:PRK11308 172 DPDVVVADEPVSALD 186
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
184-267 |
6.68e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 184 KEILERLQFLLNF-LDLPSEKRLVKNLSGGQQRRVSFA-------VALMHdpellILDEPTVGVDPLLRQSIWNHLVHIT 255
Cdd:TIGR00630 463 KEIRERLGFLIDVgLDYLSLSRAAGTLSGGEAQRIRLAtqigsglTGVLY-----VLDEPSIGLHQRDNRRLINTLKRLR 537
|
90
....*....|..
gi 194201171 256 KAGQkTVIITTH 267
Cdd:TIGR00630 538 DLGN-TLIVVEH 548
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
91-267 |
1.04e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLscivgrRYMDAGEI-------FVLGGKPGTRGSGVPG---------KRVG 154
Cdd:PLN03073 191 DLIVDASVTLAFGRHYGLVGRNGTGKTTFL------RYMAMHAIdgipkncQILHVEQEVVGDDTTAlqcvlntdiERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 155 YMPQEIALYGEFSIQETMMYFGWIFGMET------------KEILERLQFL------------LNFLDLPSE--KRLVKN 208
Cdd:PLN03073 265 LLEEEAQLVAQQRELEFETETGKGKGANKdgvdkdavsqrlEEIYKRLELIdaytaearaasiLAGLSFTPEmqVKATKT 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 194201171 209 LSGGQQRRVSFAVALMHDPELLILDEPTVGVDplLRQSIWNHlVHITKaGQKTVIITTH 267
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLE-TYLLK-WPKTFIVVSH 399
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
608-743 |
1.12e-03 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family.
Pssm-ID: 403774 [Multi-domain] Cd Length: 281 Bit Score: 44.31 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 608 SFTDFVAPGVILTIVFFLAV-ALTSSALII--ERTEGLLDRSWVAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVVFG 684
Cdd:pfam12679 61 SALDEADDTDIDITAFLIPViAALLGADAIagERERGTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALA 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194201171 685 VT-------NNGDLFWVIVLTLLQG--MCGMCFGFLISSVCELERNAIQLALGSFyptlLLSGVIWPI 743
Cdd:pfam12679 141 ITlalgdplDLGDLLLLVAASVLLAlaLVFLSIGLLLSSVARSTRTAAAIALGLF----FVLAILWPI 204
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
91-297 |
3.26e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 91 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG-----------RRYMDagEIFVLGGKPGTRGSGVpGKRVGYMPQE 159
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadRMRFD--DIDLLRLSPRERRKLV-GHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 160 --IALYGEFSIQETMMYF--GWI--------FGMETKEILErlqfLLNFLDLPSEKRLVKN----LSGGQQRRVSFAVAL 223
Cdd:PRK15093 98 pqSCLDPSERVGRQLMQNipGWTykgrwwqrFGWRKRRAIE----LLHRVGIKDHKDAMRSfpyeLTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194201171 224 MHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 297
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
55-286 |
4.43e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.03 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 55 NAVAAWGAPANG--PRNTQAAVSVRHAFKAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMD-- 130
Cdd:PRK13657 314 DAVPDVRDPPGAidLGRVKGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDpq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 131 AGEIFVLGGKpgTRGSGVPGKR--VGYMPQEIALYGEfSIQETMMyfgwiFGM------ETKEILERLQfLLNFLdLPSE 202
Cdd:PRK13657 389 SGRILIDGTD--IRTVTRASLRrnIAVVFQDAGLFNR-SIEDNIR-----VGRpdatdeEMRAAAERAQ-AHDFI-ERKP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 203 KRLVKN-------LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKaGQKTVIItTHYIEEARQA 275
Cdd:PRK13657 459 DGYDTVvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFII-AHRLSTVRNA 536
|
250
....*....|.
gi 194201171 276 HTIGLMRSGHL 286
Cdd:PRK13657 537 DRILVFDNGRV 547
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
103-287 |
4.50e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 103 GTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGKRVGYMPQEIALYGE-------------FSIQ 169
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIF----NGQRIDTLSPGKLQALRRDIQFIFQdpyasldprqtvgDSIM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194201171 170 ETMMYFGWIFGmetKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSI 247
Cdd:PRK10261 426 EPLRVHGLLPG---KAAAARVAWLLERVGLLPEHawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 194201171 248 WNHLVHITKA-GQKTVIITTHYIEEARQAHTIGLMRSGHLL 287
Cdd:PRK10261 503 INLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
185-236 |
4.69e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 194201171 185 EILERLqFLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 236
Cdd:PRK13409 195 EVVERL-GLENILD-----RDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
|
| |
