|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
43-280 |
1.26e-82 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 262.69 E-value: 1.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVpGKRV 122
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLtDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLSIYkcisLEEVFLKL 280
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 ... |
43-255 |
5.10e-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: 200.32 E-value: 5.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRV 122
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYfgwifgmdtkeilerlqfllnfldlpsekrlvknlSGGQQRRVSFAVALMHDPELLILD 202
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL-----------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHL 255
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
50-280 |
1.80e-56 |
|
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: 193.15 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQEI 129
Cdd:COG4555 9 KKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFlDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 209 DPLLRQSIWNHLVHITKAGqKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVFLKL 280
Cdd:COG4555 164 DVMARRLLREILRALKKEG-KTVLFSSHIMQEvEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
43-264 |
5.24e-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: 180.01 E-value: 5.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNAnqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRV 122
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI-NGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLtDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 264
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
42-258 |
1.67e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 167.59 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGsgvPGKR 121
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDrANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 201 LDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHLLAE 258
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVeELCDRIVIINKGRKVLS 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
50-258 |
4.00e-46 |
|
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: 163.52 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKnanqVLNNLNMTVPKGtIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQEI 129
Cdd:cd03264 8 KRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:cd03264 82 GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLgDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 318068885 209 DPLLRQSIWNHLVHItkAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAE 258
Cdd:cd03264 162 DPEERIRFRNLLSEL--GEDRIVILSTHIVEDvESLCNQVAVLNKGKLVFE 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
54-264 |
1.48e-45 |
|
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: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 54 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQEIALYG 133
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 212
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAAdRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 213 RQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVL 264
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
50-257 |
5.42e-45 |
|
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: 160.38 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKR-VGYMPQE 128
Cdd:cd03259 8 KTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTGVP--PERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 IALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGlLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 318068885 208 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLA 257
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQ 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
41-265 |
8.94e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 160.36 E-value: 8.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGK 120
Cdd:PRK13537 6 APIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-SLCGEPVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEKRL-VKNLSGGQQRRVSFAVALMHDPELL 199
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAkVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 200 ILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLL 265
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 ... |
43-258 |
1.60e-43 |
|
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: 156.48 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGKRV 122
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LVDGEPVTG----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMyFGW-IFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVA-LGLeLQGVPKAEARERAEELLELVGLSgFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 201 LDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLM--RSGHLLAE 258
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAvFLADRVVVLsaRPGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
39-241 |
2.14e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.56 E-value: 2.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRymDAGEIFVlGGKPGTRgsg 116
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKP--TSGEVLV-DGKPVTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 117 vPGKRVGYMPQEIALygefsiqetmmyFGW------------IFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQ 183
Cdd:COG1116 78 -PGPDRGVVFQEPAL------------LPWltvldnvalgleLRGVPKAERRERARELLELVGLaGFEDAYPHQLSGGMR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 184 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 241
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEA 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
43-253 |
2.51e-43 |
|
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: 155.90 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTrgsgVPGKRV 122
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELsEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSG 253
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVeELCDRVLLLNKG 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
42-265 |
1.70e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 157.69 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGSGVPGKR 121
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-VPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEKRL-VKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADArVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 201 LDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLL 265
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
43-255 |
1.94e-42 |
|
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: 153.41 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG----GKPGTRGSGVP 118
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGdRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
39-265 |
1.61e-40 |
|
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: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG---GKPGTRGS 115
Cdd:COG1127 2 SEPMIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 GVPGKRVGYMPQEIALYGEFSIQETMMY----FGwifGMDTKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQR 184
Cdd:COG1127 78 YELRRRIGMLFQGGALFDSLTVFENVAFplreHT---DLSEAEIRELVLEKLELVGLpgaadkmPSE------LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 185 RVSFAVALMHDPELLILDEPTVGVDPLLRQSIwNHLVH-ITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPS 262
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVI-DELIReLRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
...
gi 318068885 263 VLL 265
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 ... |
55-254 |
2.00e-40 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 147.61 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 55 KKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQ------- 127
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQnpddqff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 ------EIAlygeFSIQetmmyfgwIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:cd03225 90 gptveeEVA----FGLE--------NLGLPEEEIEERVEEALELVGLEGlRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 201 LDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGH 254
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
43-258 |
1.31e-39 |
|
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: 145.05 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVpgKRV 122
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILErlqfLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKdSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318068885 202 DEPTVGVDPL----LRQSIWNHlvhitKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:cd03268 151 DEPTNGLDPDgikeLRELILSL-----RDQGITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
42-266 |
2.30e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.96 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP-GTRGSGVPGK 120
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL-LDGRDlASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEFSIQETMM-----YFGWiFGMDTKE-------ILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSF 188
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVAlgrypHLGL-FGRPSAEdreaveeALERTG-LEHLAD-----RPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
41-280 |
3.23e-39 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 156.05 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRhafkaYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG---KPGTRGSGV 117
Cdd:NF033858 5 EGVSHR-----YGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmaDARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PgkRVGYMPQEIA--LYGEFSIQETMMYFGWIFGMDTKEILERLQFLLN------FLDLPSEKrlvknLSGGQQRRVSFA 189
Cdd:NF033858 76 P--RIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRatglapFADRPAGK-----LSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKA-GQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLSIY 268
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLART 228
|
250
....*....|..
gi 318068885 269 KCISLEEVFLKL 280
Cdd:NF033858 229 GADTLEAAFIAL 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
38-266 |
3.23e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGsgv 117
Cdd:COG1121 2 MMMPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 pgKRVGYMPQEIALYGEF--SIQETMM-----YFGWIFGMDTK------EILERLQfLLNFLDlpsekRLVKNLSGGQQR 184
Cdd:COG1121 75 --RRIGYVPQRAEVDWDFpiTVRDVVLmgrygRRGLFRRPSRAdreavdEALERVG-LEDLAD-----RPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 185 RVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQA--HTIGLMRsgHLLAEESPS 262
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYfdRVLLLNR--GLVAHGPPE 223
|
....
gi 318068885 263 VLLS 266
Cdd:COG1121 224 EVLT 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
43-267 |
4.18e-39 |
|
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: 144.57 E-value: 4.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGSGVP---- 118
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG-EDISGLSEAElyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRVGYMPQEIALYGEFSIQETMMYfgWI---FGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMH 194
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAF--PLrehTRLSEEEIREIVLEKLEAVGLRgAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIwNHLVH-ITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLSI 267
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVI-DDLIRsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
62-206 |
5.54e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 141.25 E-value: 5.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQETM 141
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLV----KNLSGGQQRRVSFAVALMHDPELLILDEPTV 206
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDlADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
564-762 |
1.35e-37 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 139.18 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 564 FTDFVAPGVILTIVFFLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVVFGVT-N 642
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPlR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 643 NGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVIWPIEGMPVVLRYISLCLPLTLATSSLR 722
Cdd:COG0842 81 GLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 318068885 723 SILTRGWAIleSDVYIGYVSTLSWIVGFLVLTLLVLRAKR 762
Cdd:COG0842 161 ALFLGGAGL--ADVWPSLLVLLAFAVVLLALALRLFRRRL 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
43-266 |
2.70e-37 |
|
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: 139.39 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPgTRGSGVPG--K 120
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKD-ITKKNLRElrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQ-------------EIAlygefsiqetmmyFGWI-FGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRR 185
Cdd:COG1122 76 KVGLVFQnpddqlfaptveeDVA-------------FGPEnLGLPREEIRERVEEALELVGLEHlADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 186 VSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVL 264
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
..
gi 318068885 265 LS 266
Cdd:COG1122 222 FS 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
43-265 |
3.32e-37 |
|
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: 139.74 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNAnqvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYM--DAGEIFVlGGKPGTRGSGVPGK 120
Cdd:cd03295 1 IEFENVTKRYGGGKKA---VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLIepTSGEIFI-DGEDIREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 R-VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEK---RLVKNLSGGQQRRVSFAVALMHDP 196
Cdd:cd03295 75 RkIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfadRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 197 ELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLL 265
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
40-260 |
6.95e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.25 E-value: 6.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 40 QAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSG--- 116
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI-DGQDISSLSErel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 117 --VPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALM 193
Cdd:COG1136 81 arLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDrLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 194 HDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEES 260
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
42-266 |
1.53e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 138.01 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR 121
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEI--ALYGEFSIQETMMYFGWIFGMDtkEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSflDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
43-255 |
2.27e-36 |
|
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: 136.87 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG---KPGTRGSGVPG 119
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 KRVGYMPQEIALY-------GEfSIQETMMYFGwifGMDTKEILERLQFLLNF-LDLPSE--KRLVKNLSGGQQRRVSFA 189
Cdd:cd03257 82 KEIQMVFQDPMSSlnprmtiGE-QIAEPLRIHG---KLSKKEARKEAVLLLLVgVGLPEEvlNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
43-258 |
4.95e-36 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 135.57 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRV 122
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMeELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHItKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAE 258
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYE 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
39-264 |
5.65e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.46 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTrgsGV- 117
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-LDGRDVT---GLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PGKR-VGYMPQEIALYGEFSIQE------TMMyfgwifGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFA 189
Cdd:COG3842 74 PEKRnVGMVFQDYALFPHLTVAEnvafglRMR------GVPKAEIRARVAELLELVGLEGlADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 264
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAlALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
45-254 |
6.29e-36 |
|
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: 133.85 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 45 VRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSGVPGK---R 121
Cdd:cd03229 3 LKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-IDGEDLTDLEDELPPlrrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEFSIQETMMYfgwifgmdtkeilerlqfllnfldlpsekrlvkNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIAL---------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGH 254
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
44-258 |
4.07e-35 |
|
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: 131.40 E-value: 4.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVG 123
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMPQeialygefsiqetmmyfgwifgmdtkeILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:cd03214 77 YVPQ---------------------------ALELLG-LAHLAD-----RPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAE 258
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQ 179
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
54-254 |
7.49e-35 |
|
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: 130.06 E-value: 7.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 54 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQeialyg 133
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 efsiqetmmyfgwifgmdtkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 213
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 318068885 214 QSIWNHLVHITKAGqKTVIITTHYIEEARQA-HTIGLMRSGH 254
Cdd:cd00267 117 ERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
41-249 |
2.30e-34 |
|
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: 130.29 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgK 120
Cdd:COG4133 1 MMLEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEFSIQETMMYFGWIFGM-----DTKEILERLQfLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHD 195
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLradreAIDEALEAVG-LAGLADLP-----VRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 318068885 196 PELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQAHTIGL 249
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARG-GAVLLTTHQPLELAAARVLDL 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-266 |
5.72e-34 |
|
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: 136.96 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 23 PNAVAAWGAPANGPRNTQAAVSVRHAFKAYG-KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAG 101
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 102 EIFvLGGKPGTRGSGVP----GKRVGYMPQ--EIALYGEFSIQETMMYFGWIFG-MDTKEILERLQFLLNFLDLPSE--K 172
Cdd:COG1123 321 SIL-FDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDlaD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 173 RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMR 251
Cdd:COG1123 400 RYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMY 479
|
250
....*....|....*
gi 318068885 252 SGHLLAEESPSVLLS 266
Cdd:COG1123 480 DGRIVEDGPTEEVFA 494
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
57-236 |
3.54e-33 |
|
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: 127.26 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGSgvpgKRVGYMPQEIALYGEF- 135
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-KPLEKER----KRIGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 -SIQETMM--------YFGWIFGMDTKEILERLQF--LLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEP 204
Cdd:cd03235 85 iSVRDVVLmglyghkgLFRRLSKADKAKVDEALERvgLSELAD-----RQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190
....*....|....*....|....*....|..
gi 318068885 205 TVGVDPLLRQSIWNHLVHITKAGqKTVIITTH 236
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREG-MTILVVTH 190
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
49-255 |
3.88e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 49 FKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgVPG--KRVGYMP 126
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-LDGKPLSAMP-PPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 QEIALYGEfSIQE----TMMYFGWIFGMDT-KEILERLQFLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:COG4619 81 QEPALWGG-TVRDnlpfPFQLRERKFDRERaLELLERLGLPPDILDKP-----VERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
43-264 |
4.79e-33 |
|
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: 127.35 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTrgsGVP-GKR 121
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL-LDGKDIT---NLPpHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 -VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELL 199
Cdd:cd03300 73 pVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 200 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 264
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
63-277 |
5.15e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 136.79 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 63 NNLNMTVPKGTIYGLLGASGCGKTT-------LLSCIVGR-----RYMDAGEIfvlggkpGTRgsgvpgKRVGYMPQEIA 130
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASEGEawlfgQPVDAGDI-------ATR------RRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 131 LYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 210 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVF 277
Cdd:NF033858 430 PVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARGAATLEEAF 497
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
43-261 |
1.77e-32 |
|
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: 125.73 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRgsgVPGKR- 121
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL-LDGQDITK---LPMHKr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 ----VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDP 196
Cdd:cd03218 73 arlgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHItHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 197 ELLILDEPTVGVDPLLRQSIwNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESP 261
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTP 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
41-268 |
3.42e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 125.55 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGT-RGSGVPG 119
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 --KRVGYMPQEIALYGEFSIQETMM-----YFGW---IFGMDTKE-------ILERLQfLLNFLDlpseKRlVKNLSGGQ 182
Cdd:COG3638 78 lrRRIGMIFQQFNLVPRLSVLTNVLagrlgRTSTwrsLLGLFPPEdreraleALERVG-LADKAY----QR-ADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 183 QRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ--AHTIGLmRSGHLL---- 256
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyaDRIIGL-RDGRVVfdgp 230
|
250
....*....|...
gi 318068885 257 -AEESPSVLLSIY 268
Cdd:COG3638 231 pAELTDAVLREIY 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
51-266 |
1.16e-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: 122.93 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 51 AYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRYmdAGEIfVLGGKPGTRGSgvPGKRV----GY 124
Cdd:cd03224 9 GYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPR--SGSI-RFDGRDITGLP--PHERAragiGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 125 MPQEIALYGEFSIQETMMYFGWIFGMD-TKEILERLqfLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILD 202
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAkRKARLERV--YELFPRLKErRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 266
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGV-TILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
40-241 |
1.63e-31 |
|
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: 126.30 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 40 QAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPG 119
Cdd:TIGR03265 2 SPYLSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIY-QGGRDITRLP--PQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 KR-VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:TIGR03265 75 KRdYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPgSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 198 LLILDEPTVGVDPLLRQsiwnHLVHITKAGQK----TVIITTHYIEEA 241
Cdd:TIGR03265 155 LLLLDEPLSALDARVRE----HLRTEIRQLQRrlgvTTIMVTHDQEEA 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
43-261 |
1.84e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.03 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK-------PGTRgs 115
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGRdlftnlpPRER-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 gvpgkRVGYMPQEIALYGEFSIQETmmyfgwI-FGM-----DTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSF 188
Cdd:COG1118 76 -----RVGFVFQHYALFPHMTVAEN------IaFGLrvrppSKAEIRARVEELLELVQLEGlADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESP 261
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQVGTP 218
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
386-756 |
5.86e-31 |
|
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: 124.42 E-value: 5.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 386 GVMLFIFALPVMQVILFCLAIG---RDPQGLNLAIVNGEMNDTENCYWedgchfknlgcRYLSHLNTSVVKTYYEDLDDA 462
Cdd:pfam12698 2 SFLIITLLLPILLILLLGLIFSnavNDPEELPVAVVDEDNSSLSRQLV-----------RALEASPTVNLVQYVDSEEEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 463 KEAVRKGTAWGAVYISENFTDafiaranlgrdsDDETIDSSEVKVWLDMSNQQIGVMLNRDIQlAFRDFAMGLLGQCGSN 542
Cdd:pfam12698 71 KEALKNGKIDGLLVIPKGFSK------------DLLKGESATVTVYINSSNLLVSKLILNALQ-SLLQQLNASALVLLLE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 543 PKLGDVPIQFRDPIYGTMNPSFTDFVAPgVILTIVFFLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQFVV 622
Cdd:pfam12698 138 ALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 623 MCgqtTLVLIFMLVVFGVT-NNGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVIWPIEGM 701
Cdd:pfam12698 217 GL---LQLLIILLLLFGIGiPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDP 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 702 PVVLRYISLCLPLTLATSSLRSILTRgwaILESDVYIGYVSTLSWIVGFLVLTLL 756
Cdd:pfam12698 294 PSFLQWIFSIIPFFSPIDGLLRLIYG---DSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
43-263 |
7.32e-31 |
|
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: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgrrYMD----AGEIFVLGGKPGT-RGSGV 117
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLL----YGEerptSGQVLVNGQDLSRlKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PG--KRVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMH 194
Cdd:COG2884 75 PYlrRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDkAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIE--EARQAHTIGLmRSGHLLAEESPSV 263
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLElvDRMPKRVLEL-EDGRLVRDEARGV 223
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
52-266 |
9.16e-31 |
|
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: 122.17 E-value: 9.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKK-KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG---KRVGYMPQ 127
Cdd:TIGR04521 10 YQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdlrKKVGLVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 --EIALYGEfSIQETMMyFGWI-FGMDTKEILERLQFLLNFLDLPsEKRLVKN---LSGGQQRRVSFAVALMHDPELLIL 201
Cdd:TIGR04521 90 fpEHQLFEE-TVYKDIA-FGPKnLGLSEEEAEERVKEALELVGLD-EEYLERSpfeLSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDvAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
43-258 |
1.01e-30 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 120.76 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpGTRGSGVPGK-- 120
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD----GTDLTLLSGKel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 -----RVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLpSEKR--LVKNLSGGQQRRVSFAVALM 193
Cdd:cd03258 78 rkarrRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKAdaYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 194 HDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-253 |
1.20e-30 |
|
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: 119.67 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKR- 121
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI-GGRDVTDLP--PKDRd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLlDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 318068885 201 LDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH-YIEEARQAHTIGLMRSG 253
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDG 207
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
64-257 |
1.34e-30 |
|
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: 119.71 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 64 NLNMTVPKGTIyGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP---GTRGSGVP--GKRVGYMPQEIALYGEFSIQ 138
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTI-VLNGTVlfdSRKKINLPpqQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 139 ETMmyfgwIFGMDTKEILERLQF---LLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 214
Cdd:cd03297 94 ENL-----AFGLKRKRNREDRISvdeLLDLLGLdHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 318068885 215 SIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLA 257
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQY 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
57-254 |
1.21e-29 |
|
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: 115.56 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGS-GVPGKRVGYMPQEIALYGEf 135
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-IDGVDLRDLDlESLRKNIAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQEtmmyfgwifgmdtkeilerlqfllnfldlpsekrlvkN-LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 214
Cdd:cd03228 91 TIRE-------------------------------------NiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 318068885 215 SIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGH 254
Cdd:cd03228 134 LILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
41-256 |
2.64e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.79 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGK 120
Cdd:COG3839 2 ASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-IGGRDVTDLP--PKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 R-VGYMPQEIALYGEFSIQETMMyFG-WIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:COG3839 75 RnIAMVFQSYALYPHMTVYENIA-FPlKLRKVPKAEIDRRVREAAELLGLeDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLL 256
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAmTLADRIAVMNDGRIQ 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
58-266 |
4.09e-29 |
|
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: 122.32 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 58 ANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---RRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQE-----I 129
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGRRIGMVFQDpmtqlN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMyfgwIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:COG1123 98 PVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERrLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 209 DPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG1123 174 DVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
44-262 |
5.77e-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: 115.61 E-value: 5.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTrgsgvpgkrvG 123
Cdd:cd03219 2 EVRGLTKRFGGLV----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGEDIT----------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMPQEIA------------LYGEFSIQETMM----------YFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSG 180
Cdd:cd03219 67 LPPHEIArlgigrtfqiprLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLaDLADRPAGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 181 GQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEE 259
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
...
gi 318068885 260 SPS 262
Cdd:cd03219 226 TPD 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
45-264 |
7.66e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 115.36 E-value: 7.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 45 VRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgTRGSGVPGK---- 120
Cdd:cd03256 3 VENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG----TDINKLKGKalrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 ---RVGYMPQEIALYGEFSIQETM-------MYFGW-IFGMDTKEILERLQFLLNFLDLpSEK--RLVKNLSGGQQRRVS 187
Cdd:cd03256 76 lrrQIGMIFQQFNLIERLSVLENVlsgrlgrRSTWRsLFGLFPKEEKQRALAALERVGL-LDKayQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 188 FAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ--AHTIGLmRSGHLLAEESPSVL 264
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyaDRIVGL-KDGRIVFDGPPAEL 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
44-258 |
8.30e-29 |
|
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: 115.12 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKaygKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKRVG 123
Cdd:cd03267 22 SLKSLFK---RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-RRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 Y-MPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:cd03267 98 VvFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAE 258
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYD 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
53-236 |
1.32e-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: 114.29 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 53 GKKKNAN---QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR---RYMDAGEIFVlGGKPGTRGSgVPgKRVGYMP 126
Cdd:cd03234 11 LKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILF-NGQPRKPDQ-FQ-KCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 QEIALYGEFSIQETMmYFGWIFGM---DTKEILERL--QFLLNFL-DLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:cd03234 88 QDDILLPGLTVRETL-TYTAILRLprkSSDAIRKKRveDVLLRDLaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 318068885 201 LDEPTVGVDPLLRqsiwNHLVHITK---AGQKTVIITTH 236
Cdd:cd03234 167 LDEPTSGLDSFTA----LNLVSTLSqlaRRNRIVILTIH 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
43-262 |
1.41e-28 |
|
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: 114.20 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC-------IVGRRymDAGEIFVLGGKPGTRGS 115
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrlndlIPGAP--DEGEVLLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 GVPG--KRVGYMPQEIALYgEFSIQETMMYFGWIFGMDTKEIL-ERLQFLLNFLDLPSEkrlVKN------LSGGQQRRV 186
Cdd:cd03260 75 DVLElrRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDE---VKDrlhalgLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 187 SFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHItkAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLaEESPS 262
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAaRVADRTAFLLNGRLV-EFGPT 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
43-257 |
2.23e-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: 114.41 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRhafkaYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRY-MDAGEIFVLGGKPGT------Rgs 115
Cdd:COG1119 9 VTVR-----RGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGedvwelR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 gvpgKRVGYMPQEIALY--GEFSIQETMM--YFGWI--FGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSF 188
Cdd:COG1119 78 ----KRIGLVSPALQLRfpRDETVLDVVLsgFFDSIglYREPTDEQRERARELLELLGLAHlADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQA--HTIgLMRSGHLLA 257
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGitHVL-LLKDGRVVA 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-241 |
2.72e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.57 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGK 120
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-TLDGVPVTG----PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEFSIQETMMyFGWIF-GMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPEL 198
Cdd:COG4525 77 DRGVVFQKDALLPWLNVLDNVA-FGLRLrGVPKAERRARAEELLALVGLADfARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 318068885 199 LILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 241
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
44-266 |
3.14e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.59 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRgsgVP-GKR- 121
Cdd:COG1137 5 EAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF-LDGEDITH---LPmHKRa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 ---VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLpseKRLVKN----LSGGQQRRVSFAVALMH 194
Cdd:COG1137 77 rlgIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI---THLRKSkaysLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEarqahTIG------LMRSGHLLAEESPSVLLS 266
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGI-GVLITDHNVRE-----TLGicdrayIISEGKVLAEGTPEEILN 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
45-256 |
3.92e-28 |
|
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: 114.28 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 45 VRHAFKAYGKKKNANQVL---------NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGS 115
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILkktgqtvgvNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-DGQDIAAMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 -----GVPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFA 189
Cdd:cd03294 93 rkelrELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLeGWEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLL 256
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRLV 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
60-236 |
4.40e-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: 111.87 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR--YMDAGEIFVlGGKPgtRGSGVPGKRVGYMPQEIALYGEFSI 137
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLI-NGRP--LDKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMMYfgwifgmdTKEIlerlqfllnfldlpsekrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIW 217
Cdd:cd03213 100 RETLMF--------AAKL--------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*....
gi 318068885 218 NHLVHITKAGqKTVIITTH 236
Cdd:cd03213 152 SLLRRLADTG-RTIICSIH 169
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
50-268 |
6.54e-28 |
|
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: 112.78 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPG-TRGSGVPG--KRVGYMP 126
Cdd:TIGR02315 9 KVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITkLRGKKLRKlrRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 QEIALYGEFSIQETM------------MYFGWIFGMDTKEILERLQfLLNFLDLPSEKrlVKNLSGGQQRRVSFAVALMH 194
Cdd:TIGR02315 86 QHYNLIERLTVLENVlhgrlgykptwrSLLGRFSEEDKERALSALE-RVGLADKAYQR--ADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ--AHTIGLmRSGHLLAEESPS-----VLLSI 267
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyaDRIVGL-KAGEIVFDGAPSelddeVLRHI 241
|
.
gi 318068885 268 Y 268
Cdd:TIGR02315 242 Y 242
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
42-240 |
1.46e-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: 113.72 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPgKR 121
Cdd:TIGR03522 2 SIRVSSLTKLYGTQN----ALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQ-RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:TIGR03522 77 IGYLPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLrPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 318068885 201 LDEPTVGVDPllrqsiwNHLVHITK-----AGQKTVIITTHYIEE 240
Cdd:TIGR03522 157 LDEPTTGLDP-------NQLVEIRNvikniGKDKTIILSTHIMQE 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
39-236 |
1.85e-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: 108.97 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP--GTRGSG 116
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDGRDitGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 117 VPGKRVGYMPQEIALYGEFSIQETMM----------YFGWIFGM-----DTKEILERLQFLLNFLDL-PSEKRLVKNLSG 180
Cdd:COG0411 76 IARLGIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLprarrEEREARERAEELLERVGLaDRADEPAGNLSY 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 181 GQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH 236
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
22-265 |
2.56e-26 |
|
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: 114.09 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 22 QPNAVAAWGAPANGPrnTQAAVSVRHAFKAYGKkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAG 101
Cdd:COG4987 315 APPAVTEPAEPAPAP--GGPSLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 102 EIfVLGGKPGTRgsgVPG----KRVGYMPQEIALygeFSiqetmmyfgwifgmDT-----------------KEILERLQ 160
Cdd:COG4987 391 SI-TLGGVDLRD---LDEddlrRRIAVVPQRPHL---FD--------------TTlrenlrlarpdatdeelWAALERVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 161 fLLNFLD-LPS--EKRLV---KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIIT 234
Cdd:COG4987 450 -LGDWLAaLPDglDTWLGeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLI 526
|
250 260 270
....*....|....*....|....*....|.
gi 318068885 235 THYIEEARQAHTIGLMRSGHLLAEESPSVLL 265
Cdd:COG4987 527 THRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
54-255 |
3.11e-26 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 107.81 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 54 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR-VGYMPQEIALY 132
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL-LNGKDITNLP--PEKRdISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 133 GEFSIQETMMYFGWIFGMDTKEILER---------LQFLLNfldlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDKKEIERKvleiaemlgIDHLLN--------RKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKL 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-266 |
3.48e-26 |
|
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: 113.70 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 22 QPNAVAAWGAPANgPRNTQAAVSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAG 101
Cdd:COG4988 317 APEPAAPAGTAPL-PAAGPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 102 EIFVlGGKPGTRGSGVP-GKRVGYMPQE-----------IALYGEFSIQETMMyfgwifgmdtkEILERLQfLLNFLD-L 168
Cdd:COG4988 393 SILI-NGVDLSDLDPASwRRQIAWVPQNpylfagtirenLRLGRPDASDEELE-----------AALEAAG-LDEFVAaL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 169 PS--EKRL---VKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQ 243
Cdd:COG4988 460 PDglDTPLgegGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ 537
|
250 260
....*....|....*....|...
gi 318068885 244 AHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
42-255 |
7.85e-26 |
|
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: 106.65 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRgSGVPGKR 121
Cdd:cd03296 2 SIEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL-FGGEDATD-VPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEFSIQETMMyfgwiFGMDTK---------EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVA 191
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVA-----FGLRVKprserppeaEIRAKVHELLKLVQLDWlADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 192 LMHDPELLILDEPTVGVDPLLRQSI--W----NHLVHITkagqkTVIItTHYIEEARQ-AHTIGLMRSGHL 255
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 ... |
52-253 |
1.02e-25 |
|
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: 105.42 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKKKNanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRYMdaGEIFvLGGKPgtRGSGVPGKRVGYMPQEI 129
Cdd:cd03226 9 YKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKESS--GSIL-LNGKP--IKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 --ALYGEFSIQEtmMYFGwifGMDTKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTV 206
Cdd:cd03226 81 dyQLFTDSVREE--LLLG---LKELDAGNEQAETVLKDLDLYALKeRHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 207 GVDPLLRQSIWNHLVHITKAGqKTVIITTHYIE-EARQAHTIGLMRSG 253
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQG-KAVIVITHDYEfLAKVCDRVLLLANG 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
50-220 |
1.10e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtrgsgvPGKRVGYMPQEI 129
Cdd:COG0488 6 KSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----------KGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMM---------------------------------------YFGWIFGMDTKEILERLQFLLNFLDlps 170
Cdd:COG0488 71 PLDDDLTVLDTVLdgdaelraleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARAEEILSGLGFPEEDLD--- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 318068885 171 ekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTvgvdpllrqsiwNHL 220
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 ... |
43-255 |
1.19e-25 |
|
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: 105.30 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--K 120
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEFSIQETMMyFG--WIFGMDTKE-------ILERLQfLLNFLD-LPSEkrlvknLSGGQQRRVSFAV 190
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENIT-LApiKVKGMSKAEaeeraleLLEKVG-LADKADaYPAQ------LSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 191 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGM-TMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
43-264 |
1.37e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.04 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgVPGKRV 122
Cdd:PRK11432 7 VVLKNITKRFGS----NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDVTHRS-IQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGfEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVL 264
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
51-266 |
1.57e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 105.83 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 51 AYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--RRYmdAGEIfVLGGKPGTRGSgvPGKRV----GY 124
Cdd:COG0410 12 GYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGllPPR--SGSI-RFDGEDITGLP--PHRIArlgiGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 125 MPQEIALYGEFSIQETMMyFGWIFGMDTKEILERLQFLLN-FLDLpSEKR--LVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:COG0410 83 VPEGRRIFPSLTVEENLL-LGAYARRDRAEVRADLERVYElFPRL-KERRrqRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGV-TILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-220 |
1.65e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgTRGSGVpgkRV 122
Cdd:COG0488 316 LELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV---KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQE-IALYGEFSIQETMMYfgwifGMDTKEILERLQFLLNFLdLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELL 199
Cdd:COG0488 381 GYFDQHqEELDPDKTVLDELRD-----GAPGGTEQEVRGYLGRFL-FSGDDafKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180
....*....|....*....|.
gi 318068885 200 ILDEPTvgvdpllrqsiwNHL 220
Cdd:COG0488 455 LLDEPT------------NHL 463
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
51-260 |
3.93e-25 |
|
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: 104.53 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 51 AYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKRV----GYMP 126
Cdd:TIGR03410 9 YYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI-RLDGEDITKLP--PHERAragiAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 QEIALYGEFSIQETMMyfgwiFGMDT---------KEILERLQFLLNFLdlpseKRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:TIGR03410 82 QGREIFPRLTVEENLL-----TGLAAlprrsrkipDEIYELFPVLKEML-----GRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEES 260
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
43-262 |
4.41e-25 |
|
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: 106.68 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---RRYMDAGEIFVLG----GKPGTRGS 115
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGedllKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 GVPGKRVGYMPQE----------IalyGEfSIQETMMYFGwifGMDTKEILERLQFLLNFLDLPSEKRLVKN----LSGG 181
Cdd:COG0444 82 KIRGREIQMIFQDpmtslnpvmtV---GD-QIAEPLRIHG---GLSKAEARERAIELLERVGLPDPERRLDRypheLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 182 QQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHlLAEES 260
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVMYAGR-IVEEG 233
|
..
gi 318068885 261 PS 262
Cdd:COG0444 234 PV 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
49-288 |
2.24e-24 |
|
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: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 49 FKAYGKKknanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRVGYMPQE 128
Cdd:TIGR01257 938 FEPSGRP-----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV-GGKDIETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 IALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 208 VDPLLRQSIWNHLVHItKAGqKTVIITTHYIEEAR-QAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVFLKLSRIQSQ 286
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKY-RSG-RTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQ 1169
|
..
gi 318068885 287 KG 288
Cdd:TIGR01257 1170 RG 1171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
44-261 |
3.99e-24 |
|
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: 101.97 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGT---------RG 114
Cdd:TIGR04406 3 VAENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL-IDGQDIThlpmherarLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 115 sgvpgkrVGYMPQEIALYGEFSIQETMMYFGWIFG-MDTKEILERLQFLLNFLDLpseKRLVKN----LSGGQQRRVSFA 189
Cdd:TIGR04406 78 -------IGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQI---SHLRDNkamsLSGGERRRVEIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNhLVHITKAGQKTVIITTHYIEEarqahTIG------LMRSGHLLAEESP 261
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPIAVGDIKK-IIKHLKERGIGVLITDHNVRE-----TLDicdrayIISDGKVLAEGTP 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
77-261 |
4.46e-24 |
|
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: 103.73 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 77 LLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgVPGKR--VGYMPQEIALYGEFSIQETMMYFGWIFGMDTKE 154
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI-MLDGEDVTN---VPPHLrhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 155 ILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVII 233
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEfADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180
....*....|....*....|....*....
gi 318068885 234 TTHYIEEA-RQAHTIGLMRSGHLLAEESP 261
Cdd:TIGR01187 157 VTHDQEEAmTMSDRIAIMRKGKIAQIGTP 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
49-266 |
6.63e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 101.32 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 49 FKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR--VGYMP 126
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 QEIALYGEFSIQETMMyFGWIF--GMDTKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSFAVALMHDPE 197
Cdd:PRK09493 84 QQFYLFPHLTALENVM-FGPLRvrGASKEEAEKQARELLAKVGLaerahhyPSE------LSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHT-IGLMRSGHLLAEESPSVLLS 266
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGM-TMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
52-258 |
1.27e-23 |
|
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: 98.54 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYMPQEIAL 131
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDGVPVSDLEKALSSLISVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YgefsiqetmmyfgwifgmDTKeilerlqfLLNFLDLPsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 211
Cdd:cd03247 87 F------------------DTT--------LRNNLGRR--------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 318068885 212 LRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 258
Cdd:cd03247 133 TERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
62-236 |
1.28e-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: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGKRVGYMPQEIAL-YGEF----- 135
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV----NGQDVSDLRGRAIPYLRRKIGVvFQDFrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 -SIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEKR-LVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 213
Cdd:cd03292 93 rNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|...
gi 318068885 214 QSIWNHLVHITKAGqKTVIITTH 236
Cdd:cd03292 173 WEIMNLLKKINKAG-TTVVVATH 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
43-266 |
1.50e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.07 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--K 120
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEFSIQETMMYfG--WIFGMDTKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSFAVA 191
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLadkadayPAQ------LSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 192 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGM-TMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
61-255 |
1.84e-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: 98.27 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR----VGYMP---QEIALYG 133
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT-LDGKPVTRRS--PRDAiragIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EFSIQETMmyfgwifgmdtkeILERLqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 213
Cdd:cd03215 92 DLSVAENI-------------ALSSL------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 318068885 214 QSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:cd03215 141 AEIYRLIRELADAG-KAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
556-724 |
1.89e-23 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 98.88 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 556 IYGTMNPSFTDFVAPGVILTIVFFLAV-ALTSSALIIERTEGLLDRSWVAGV-SPFEILFSHVITQFVVMCGQTTLVLIF 633
Cdd:pfam01061 33 LFGNLGNQQGGLNRPGLLFFSILFNAFsALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 634 MLVVFGVT-NNGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVIWPIEGMPVVLRYISLCL 712
Cdd:pfam01061 113 VYFMVGLPpSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLN 192
|
170
....*....|..
gi 318068885 713 PLTLATSSLRSI 724
Cdd:pfam01061 193 PLTYAIEALRAN 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
65-266 |
1.97e-23 |
|
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: 102.50 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 65 LNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGV---PGKR-VGYMPQEIALYGEFSIQET 140
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflpPEKRrIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MMYFGW-IFGMDTKEILERLQFLLNfLDlPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNH 219
Cdd:TIGR02142 96 LRYGMKrARPSERRISFERVIELLG-IG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 220 LVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
42-253 |
2.21e-23 |
|
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: 97.67 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAfkaygkkKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP-GTRGSGVPGK 120
Cdd:cd03246 5 NVSFRYP-------GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-RLDGADiSQWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 RVGYMPQEIALYGEfSIQETMmyfgwifgmdtkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLI 200
Cdd:cd03246 77 HVGYLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 201 LDEPTVGVDPLLRQSIwNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSG 253
Cdd:cd03246 120 LDEPNSHLDVEGERAL-NQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-258 |
2.59e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvP 118
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-LDGEPVRFRS--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 G----KRVGYMPQEIALYGEFSIQETMMY------FGWIfgmDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVS 187
Cdd:COG1129 74 RdaqaAGIAIIHQELNLVPNLSVAENIFLgreprrGGLI---DWRAMRRRARELLARLGLDiDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 188 FAVALMHDPELLILDEPT-----VGVDPLLRqsiwnhLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:COG1129 151 IARALSRDARVLILDEPTaslteREVERLFR------IIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGT 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
43-253 |
3.13e-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: 98.31 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHA-FKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgsgvpGKR 121
Cdd:cd03250 1 ISVEDAsFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQEIALYGEfSIQETMmyfgwIFG--MDT---KEILERLQFLLNFLDLPS-------EKRLvkNLSGGQQRRVSFA 189
Cdd:cd03250 68 IAYVSQEPWIQNG-TIRENI-----LFGkpFDEeryEKVIKACALEPDLEILPDgdlteigEKGI--NLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSG 253
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
57-244 |
3.59e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgTRGsgvPGKRVGYMPQEIALYGEF- 135
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRA---GGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 -SIQETMM--------YFGWIFGMDTKEI---LERLQFLlnflDLpsEKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:NF040873 72 lTVRDLVAmgrwarrgLWRRLTRDDRAAVddaLERVGLA----DL--AGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQA 244
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRRA 185
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
36-266 |
8.80e-23 |
|
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: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYGKkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGT--- 112
Cdd:COG2274 467 LPRLKGDIELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGIDLRqid 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 113 ----RgsgvpgKRVGYMPQEIAL-YGefSIQETMMYFGwiFGMDTKEILERLQF--LLNFLD-LP-------SEKrlVKN 177
Cdd:COG2274 544 paslR------RQIGVVLQDVFLfSG--TIRENITLGD--PDATDEEIIEAARLagLHDFIEaLPmgydtvvGEG--GSN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 178 LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLA 257
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
....*....
gi 318068885 258 EESPSVLLS 266
Cdd:COG2274 690 DGTHEELLA 698
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-240 |
8.98e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.78 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKAYGKKKNAnqvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRgsgvpgkRVG 123
Cdd:COG4586 23 ALKGLFRREYREVEA---VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-------RKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMpQEIA--------LYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMH 194
Cdd:COG4586 93 FA-RRIGvvfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLgELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHY---IEE 240
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddIEA 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
43-261 |
1.01e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTrgsGVPG-KR 121
Cdd:PRK09452 15 VELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-LDGQDIT---HVPAeNR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 -VGYMPQEIALYGEFSIQETMMyfgwiFGMDTK-----EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMH 194
Cdd:PRK09452 87 hVNTVFQSYALFPHMTVFENVA-----FGLRMQktpaaEITPRVMEALRMVQLEEfAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLvhitKAGQKTVIIT----THYIEEA-----RqahtIGLMRSGHLLAEESP 261
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNEL----KALQRKLGITfvfvTHDQEEAltmsdR----IVVMRDGRIEQDGTP 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
42-256 |
1.07e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLscivgrRYMD------------AGEIFVLGGK 109
Cdd:PRK11124 2 SIQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLL------RVLNllemprsgtlniAGNHFDFSKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 110 PGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMYFGW-IFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVS 187
Cdd:PRK11124 72 PSDKAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKLLERLRLkPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 188 FAVALMHDPELLILDEPTVGVDPllrqSIWNHLVHITKAGQKTVI---ITTHYIEEARQAHT-IGLMRSGHLL 256
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDP----EITAQIVSIIRELAETGItqvIVTHEVEVARKTASrVVYMENGHIV 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
51-266 |
1.09e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 51 AYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP-GTRGSGVPGKRVGYMPQEI 129
Cdd:PRK11231 11 GYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-LGDKPiSMLSSRQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMY--------FGWIFGMDTKEI---LERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPEL 198
Cdd:PRK11231 86 LTPEGITVRELVAYgrspwlslWGRLSAEDNARVnqaMEQTR-INHLAD-----RRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 199 LILDEPTVGVDpLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK11231 160 VLLDEPTTYLD-INHQVELMRLMRELNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
61-241 |
1.10e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGKRVGYMPQEIALYGEFSIQET 140
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-TLDGKPVEG----PGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MMYFGWIFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNH 219
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKVGLEgAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170 180
....*....|....*....|..
gi 318068885 220 LVHITKAGQKTVIITTHYIEEA 241
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDIEEA 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
42-256 |
1.48e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLscivgrRYMD------------AGEIFVLGGK 109
Cdd:COG4161 2 SIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLL------RVLNlletpdsgqlniAGHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 110 PGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMYFG-WIFGMDTKEILERLQFLLNFLDLpSEK--RLVKNLSGGQQRRV 186
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRL-TDKadRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 187 SFAVALMHDPELLILDEPTVGVDPllrqSIWNHLVHITKAGQKTVI---ITTHYIEEARQ-AHTIGLMRSGHLL 256
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDP----EITAQVVEIIRELSQTGItqvIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
43-264 |
2.62e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.00 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFV-------LGGKP--GTR 113
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltaLSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 114 gsgvpgKRVGYMPQ------------------EIAlygefsiqetmmyfgwifGMDTKEILERLQFLLNFLDL------- 168
Cdd:COG1135 82 ------RKIGMIFQhfnllssrtvaenvalplEIA------------------GVPKAEIRKRVAELLELVGLsdkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 169 PSEkrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTI 247
Cdd:COG1135 138 PSQ------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRV 211
|
250
....*....|....*..
gi 318068885 248 GLMRSGHLLaeESPSVL 264
Cdd:COG1135 212 AVLENGRIV--EQGPVL 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
43-258 |
4.85e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 93.26 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRV 122
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEVSFASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GympqeIALygefsiqetmmyfgwifgmdtkeilerlqfllnfldlpsekrlVKNLSGGQQRRVSFAVALMHDPELLILD 202
Cdd:cd03216 76 G-----IAM-------------------------------------------VYQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
61-258 |
8.21e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPG----KRVGYMP---QEIALYG 133
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR-LDGKPVRIRS--PRdairAGIAYVPedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EFSIQETMMY--------FGWIfgmDTKEILERLQFLLNFLDL--PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:COG1129 344 DLSIRENITLasldrlsrGGLL---DRRRERALAEEYIKRLRIktPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGlSDRILVMREGRIVGE 475
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
62-283 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.88 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--KRVGYMPQeialYGEFSIQE 139
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirKKVGLVFQ----YPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 140 TMMY----FGWI-FGMDTKEILERLQFLLNFLDLPSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 211
Cdd:PRK13637 99 ETIEkdiaFGPInLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 212 LRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSvllSIYKCIS-LEEVFLKLSRI 283
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPR---EVFKEVEtLESIGLAVPQV 249
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
43-266 |
2.45e-21 |
|
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: 93.45 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKNAnqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgRRY-MDAGEIFVLGGKpgTRGSGVPGKR 121
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYdVDSGRILIDGHD--VRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 --VGYMPQEIALYGEfSIQETMMYfgWIFGMDTKEILERLQ------FLLNF---LDLPSEKRLVKnLSGGQQRRVSFAV 190
Cdd:cd03251 76 rqIGLVSQDVFLFND-TVAENIAY--GRPGATREEVEEAARaanaheFIMELpegYDTVIGERGVK-LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 191 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
43-266 |
2.72e-21 |
|
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: 94.10 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAY------GKKKNAnQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSG 116
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfGAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS-FRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 117 VPGKRVGYMPQEI--ALYGEFSIQETMmyfGWIFG--------MDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQR 184
Cdd:TIGR02769 81 KQRRAFRRDVQLVfqDSPSAVNPRMTV---RQIIGeplrhltsLDESEQKARIAELLDMVGLRSEdaDKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 185 RVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSV 263
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQ 237
|
...
gi 318068885 264 LLS 266
Cdd:TIGR02769 238 LLS 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
50-266 |
2.99e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.42 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR-VGYMPQE 128
Cdd:PRK10895 11 KAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 IALYGEFSIQETMMYFGWIF-GMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTV 206
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 207 GVDPLLRQSIWNHLVHITKAGQKtVIITTHYIEEA----RQAHTIGlmrSGHLLAEESPSVLLS 266
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLG-VLITDHNVRETlavcERAYIVS---QGHLIAHGTPTEILQ 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
43-236 |
7.32e-21 |
|
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: 89.43 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgTRGSGVpgkRV 122
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTV---KI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQeialygefsiqetmmyfgwifgmdtkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILD 202
Cdd:cd03221 66 GYFEQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|....
gi 318068885 203 EPTVGVDPLLRQSIWNHLvhitKAGQKTVIITTH 236
Cdd:cd03221 96 EPTNHLDLESIEALEEAL----KEYPGTVILVSH 125
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
45-253 |
8.00e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 8.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 45 VRHAFKAYgkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKR-VG 123
Cdd:PRK11607 22 IRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHVP--PYQRpIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMPQEIALYGEFSIQETMMyfgwiFG-----MDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIA-----FGlkqdkLPKAEIASRVNEMLGLVHMQEfAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSG 253
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRG 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
62-240 |
1.06e-20 |
|
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: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVpGKRVGYMPQEIALYGEFSIQETM 141
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-HQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MYFGWIFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHL 220
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSlYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|
gi 318068885 221 VHITKAGqKTVIITTHYIEE 240
Cdd:TIGR01257 2114 VSIIREG-RAVVLTSHSMEE 2132
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-236 |
1.53e-20 |
|
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: 95.89 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 16 NNDGGTQPNAVAAWGAPANGPRNTQAAVSVRHAfkaygkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR 95
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP--------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 96 RYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEfSIQETMMYF-GWIFGMDTKEILERLQfLLNFLD-LPS--E 171
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT-TVRENLRLArPDATDEELWAALERVG-LADWLRaLPDglD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 172 KRLV---KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIwnhLVHITKAGQ-KTVIITTH 236
Cdd:TIGR02868 463 TVLGeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITH 528
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-247 |
1.78e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.82 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 10 SAMAATNNDGGTQPNAVAAWGAPANGPRNTQAAVSVRHAfkaygkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLL 89
Cdd:TIGR02857 294 AEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYP--------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 90 SCIVGRRYMDAGEIfVLGGKPGTRGS-GVPGKRVGYMPQEIALYgEFSIQETM-MYFGWIFGMDTKEILER--LQFLLNF 165
Cdd:TIGR02857 366 NLLLGFVDPTEGSI-AVNGVPLADADaDSWRDQIAWVPQHPFLF-AGTIAENIrLARPDASDAEIREALERagLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 166 LDLPSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHItkAGQKTVIITTHYIEEAR 242
Cdd:TIGR02857 444 LPQGLDTPIGEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAA 521
|
....*
gi 318068885 243 QAHTI 247
Cdd:TIGR02857 522 LADRI 526
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
64-267 |
1.81e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.97 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 64 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIQETMM 142
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL-WNGQDLTALP--PAERpVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 143 yfgwiFGMDTK------------EILERLQfLLNFLD-LPSEkrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:COG3840 94 -----LGLRPGlkltaeqraqveQALERVG-LAGLLDrLPGQ------LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 210 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLSI 267
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
60-284 |
3.87e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlgGKPGTRGSGVPGKRVGYMPQEIALYGEFS--- 136
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDYAIPANLKKIKEVKRLRKEIGLVFQFPeyq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 137 -IQETM---MYFGWI-FGMDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:PRK13645 103 lFQETIekdIAFGPVnLGENKQEAYKKVPELLKLVQLPEDyvKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 210 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPsvlLSIYKCISLeevflkLSRIQ 284
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP---FEIFSNQEL------LTKIE 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
38-262 |
4.04e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGKKKnANqvlNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgv 117
Cdd:COG3845 1 MMPPALELRGITKRFGGVV-AN---DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DGKPVRIRS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PGK----RVGYMPQEIALYGEFSIQETMMY-----FGWIFGMDT-----KEILERLQFllnFLDLpseKRLVKNLSGGQQ 183
Cdd:COG3845 74 PRDaialGIGMVHQHFMLVPNLTVAENIVLgleptKGGRLDRKAarariRELSERYGL---DVDP---DAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 184 RRVSFAVALMHDPELLILDEPTVG-----VDPLLRqsiwnHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLA 257
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVltpqeADELFE-----ILRRLAAEG-KSIIFITHKLREVMAiADRVTVLRRGKVVG 221
|
....*
gi 318068885 258 EESPS 262
Cdd:COG3845 222 TVDTA 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-241 |
6.04e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.40 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKpgtRGSGV-PG 119
Cdd:PRK11000 2 ASVTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEK---RMNDVpPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 KR-VGYMPQEIALYGEFSIQETMMyFGW-IFGMDTKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDP 196
Cdd:PRK11000 74 ERgVGMVFQSYALYPHLSVAENMS-FGLkLAGAKKEEINQRVNQVAEVLQLAHLlDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 318068885 197 ELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 241
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEA 197
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
60-236 |
1.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.53 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEI----------------------FVLGGKPGTRGSGV 117
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvlekLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PG--KRVGYMPQ--EIALYgEFSIQETMMyFGWI-FGMDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAV 190
Cdd:PRK13651 101 KEirRRVGVVFQfaEYQLF-EQTIEKDII-FGPVsMGVSKEEAKKRAAKYIELVGLDESylQRSPFELSGGQKRRVALAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 318068885 191 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTH 236
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTH 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
38-285 |
1.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGKKKNanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGV 117
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PGKRVGYMPQ-------------EIAlygeFSIQETMMYFGWIfgmdtKEILERLQF---LLNFLDLPSEkrlvkNLSGG 181
Cdd:PRK13632 81 IRKKIGIIFQnpdnqfigatvedDIA----FGLENKKVPPKKM-----KDIIDDLAKkvgMEDYLDKEPQ-----NLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 182 QQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESP 261
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
250 260
....*....|....*....|....
gi 318068885 262 SVLLSiykcislEEVFLKLSRIQS 285
Cdd:PRK13632 227 KEILN-------NKEILEKAKIDS 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
62-279 |
2.33e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK---PGTRGSGVPG--KRVGYMPQ--EIALYge 134
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGERvitAGKKNKKLKPlrKKVGIVFQfpEHQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 fsiQETM---MYFGWI-FGMDTKEILERLQFLLNFLDLPsEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:PRK13634 100 ---EETVekdICFGPMnFGVSEEDAKQKAREMIELVGLP-EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 208 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPsvllsiykcislEEVFLK 279
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDaARYADQIVVMHKGTVFLQGTP------------REIFAD 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-236 |
2.62e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRY--MDAGEIFVLGGKPgtR 113
Cdd:TIGR00955 15 AQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgVKGSGSVLLNGMP--I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 114 GSGVPGKRVGYMPQEIALYGEFSIQETMMyFGWIFGMD----TKEILERLQFLLNFLDLPS-------EKRLVKNLSGGQ 182
Cdd:TIGR00955 93 DAKEMRAISAYVQQDDLFIPTLTVREHLM-FQAHLRMPrrvtKKEKRERVDEVLQALGLRKcantrigVPGRVKGLSGGE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 318068885 183 QRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTH 236
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIH 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
60-259 |
3.33e-19 |
|
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: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtRGSGVPGKRVGYMPqeialygEFSIQE 139
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGLGGGFNP-------ELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 140 TMMYFGWIFGMDTKEILERLQF------LLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 213
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEiiefseLGDFIDLP-----VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 318068885 214 QSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEE 259
Cdd:cd03220 179 EKCQRRLRELLKQG-KTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
60-255 |
1.02e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGvPGKRVGYMPQEIALYgefsiqE 139
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-RFHGTDVSRLHA-RDRKVGFVFQHYALF------R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 140 TMMYFGWI-FGM---------DTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:PRK10851 88 HMTVFDNIaFGLtvlprrerpNAAAIKAKVTQLLEMVQLAHlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 209 DPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
62-266 |
1.16e-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: 89.86 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGG-------KPGTRGSGVPGKRVGYMPQEIALYGE 134
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmtKPGPDGRGRAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 FSIQETM-----------------MYFGWIFGMDTK---EILERlqfllnfldLPSEkrlvknLSGGQQRRVSFAVALMH 194
Cdd:TIGR03269 380 RTVLDNLteaiglelpdelarmkaVITLKMVGFDEEkaeEILDK---------YPDE------LSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 266
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
52-266 |
1.28e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGT--RGSGVPGKRVGYMPQEI 129
Cdd:PRK11614 15 YGKI----QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI-VFDGKDITdwQTAKIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMYFGwiFGMDTKEILERLQFLLNFLDLPSEKRLVK--NLSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:PRK11614 90 RVFSRMTVEENLAMGG--FFAERDQFQERIKWVYELFPRLHERRIQRagTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 208 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
33-258 |
1.91e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 87.48 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 33 ANGPRNtqaAVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCG--KTTLLSCIVGRrymDAGEifvlggKP 110
Cdd:NF000106 7 SNGARN---AVEVRGLVKHFGEVK----AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP---DAGR------RP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 111 GTRGSGVPGKRV------GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQ 183
Cdd:NF000106 71 WRF*TWCANRRAlrrtig*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTeAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 184 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG-ATVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
43-266 |
2.05e-18 |
|
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: 85.23 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYgkKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRV 122
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEfSIQETMMYFGwiFGMDTKEILE--RLQFLLNF-LDLPSEKRLV-----KNLSGGQQRRVSFAVALMH 194
Cdd:cd03252 79 GVVLQENVLFNR-SIRDNIALAD--PGMSMERVIEaaKLAGAHDFiSELPEGYDTIvgeqgAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318068885 195 DPELLILDEPTVGVDPLLRQSIWNHLVHITKAgqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
68-266 |
2.47e-18 |
|
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: 87.46 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 68 TVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP---GTRGSGVP-GKR-VGYMPQEIALYGEFSIQETMM 142
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI-RLGGEVlqdSARGIFLPpHRRrIGYVFQEARLFPHLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 143 YfGW--------IFGMDtkEILERLQF--LLNfldlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 212
Cdd:COG4148 100 Y-GRkrapraerRISFD--EVVELLGIghLLD--------RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 213 RQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDEvARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
30-265 |
2.72e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.07 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 30 GAPANGPRNTQAAVSVRH-AFkAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMD--AGEIFVl 106
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENvSF-SYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL--RFYDptSGRILI- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 107 GGKPGT-------RgsgvpgKRVGYMPQEIALYgEFSIQETMMYFgwIFGMDTKEILE--RLQFLLNFLD-LPS------ 170
Cdd:COG1132 400 DGVDIRdltleslR------RQIGVVPQDTFLF-SGTIRENIRYG--RPDATDEEVEEaaKAAQAHEFIEaLPDgydtvv 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 171 EKRLVkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLM 250
Cdd:COG1132 471 GERGV-NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVL 547
|
250
....*....|....*
gi 318068885 251 RSGHLLAEESPSVLL 265
Cdd:COG1132 548 DDGRIVEQGTHEELL 562
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
54-284 |
3.00e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.44 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 54 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEI----FVLGGKPGTRGSGVPG---------- 119
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPyskkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 --KRVGYMPQ--EIALYGEfSIQETMMyFGWI-FGMDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVAL 192
Cdd:PRK13631 114 lrRRVSMVFQfpEYQLFKD-TIEKDIM-FGPVaLGVKKSEAKKLAKFYLNKMGLDDSylERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 193 MHDPELLILDEPTVGVDPLLRQSIWNhLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPsvllsiYKcI 271
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP------YE-I 263
|
250
....*....|...
gi 318068885 272 SLEEVFLKLSRIQ 284
Cdd:PRK13631 264 FTDQHIINSTSIQ 276
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-266 |
4.06e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 31 APANGPRNTQAAVSVRHAFKAYgkKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMDA--GEIfVLGG 108
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT--RAWDPqqGEI-LLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 109 KPGTRGS--------GVPGKRV----GYMPQEIALYGEFSIQETMmyfgwifgmdtKEILER--LQFLLNfldlpSEKRL 174
Cdd:PRK11160 402 QPIADYSeaalrqaiSVVSQRVhlfsATLRDNLLLAAPNASDEAL-----------IEVLQQvgLEKLLE-----DDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 175 V-------KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTI 247
Cdd:PRK11160 466 NawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRI 543
|
250
....*....|....*....
gi 318068885 248 GLMRSGHLLAEESPSVLLS 266
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLA 562
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
65-242 |
4.75e-18 |
|
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: 83.31 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 65 LNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIqETMMY 143
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LINGVDVTAAP--PADRpVSMLFQENNLFAHLTV-EQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 144 FGWIFGMD-TKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLV 221
Cdd:cd03298 93 LGLSPGLKlTAEDRQAIEVALARVGLAGlEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180
....*....|....*....|.
gi 318068885 222 HITKAGQKTVIITTHYIEEAR 242
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAK 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
52-265 |
5.99e-18 |
|
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: 83.43 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGK----RVGYMPQ 127
Cdd:cd03254 12 YDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI----DGIDIRDISRKslrsMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 EIALYGEfSIQETMMYFGWIFGMDTKEILERLQFLLNFLD-LP-------SEKRlvKNLSGGQQRRVSFAVALMHDPELL 199
Cdd:cd03254 85 DTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMkLPngydtvlGENG--GNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 200 ILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLL 265
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
36-269 |
6.02e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYGKKK-NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtRG 114
Cdd:COG1134 15 RLYHEPSRSLKELLLRRRRTRrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 115 SGVPGKRVGYMPqeialygEFSIQETMMYFGWIFGMDTKEILERLQF------LLNFLDLPsekrlVKNLSGGQQRRVSF 188
Cdd:COG1134 90 SALLELGAGFHP-------ELTGRENIYLNGRLLGLSRKEIDEKFDEivefaeLGDFIDQP-----VKTYSSGMRARLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLRQsiwnhlvhitKAGQK---------TVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:COG1134 158 AVATAVDPDILLVDEVLAVGDAAFQK----------KCLARirelresgrTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
250
....*....|.
gi 318068885 259 ESPSVLLSIYK 269
Cdd:COG1134 228 GDPEEVIAAYE 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
38-279 |
8.58e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCI-------VGRRYMDAGEIFVLGGKP 110
Cdd:PRK10619 1 MSENKLNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 111 GTRGsgVPGK--------RVGYMPQEIALYGEFSIQETMMYFG-WIFGMDTKEILERLQFLLNF--LDLPSEKRLVKNLS 179
Cdd:PRK10619 77 GQLK--VADKnqlrllrtRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKvgIDERAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 180 GGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ--AHTIgLMRSGHLLA 257
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHEMGFARHvsSHVI-FLHQGKIEE 232
|
250 260
....*....|....*....|..
gi 318068885 258 EESPSVLLSIYKCISLEEvFLK 279
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQ-FLK 253
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
60-266 |
1.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.06 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFV----LGGKPGTRGSGVPGKRVGYMPQ--EIALYg 133
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYIRPVRKRIGMVFQfpESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EFSIQETMMYFGWIFGMDTKEILERLQFLLnfLDLPSEKRLVK----NLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 210 PLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
56-236 |
1.54e-17 |
|
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: 81.64 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 56 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYMPQEIALYGEF 135
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETMMYFGWIFGMDTKEILERLQfLLNFLDLpsEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPlLRQS 215
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALA-AVGLTGF--EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVA 164
|
170 180
....*....|....*....|...
gi 318068885 216 IWNHLV--HITKAGqkTVIITTH 236
Cdd:TIGR01189 165 LLAGLLraHLARGG--IVLLTTH 185
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
61-257 |
1.63e-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: 86.63 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYgEFSIQET 140
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELF-PGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MMYFGWIFgmDTKEILE--RL----QFLLNFldlPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:TIGR01842 412 IARFGENA--DPEKIIEaaKLagvhELILRL---PDGYDTVigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 210 PLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQAHTIGLMRSGHLLA 257
Cdd:TIGR01842 487 EEGEQALANAIKALKARG-ITVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-259 |
1.71e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSGVPGKRV 122
Cdd:PRK15439 12 LCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI-GGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 G-YM-PQEIALYGEFSIQETMMyFGWIFGMDTKEILERLQFLLNF-LDLPSEKRLvknLSGGQQRRVSFAVALMHDPELL 199
Cdd:PRK15439 87 GiYLvPQEPLLFPNLSVKENIL-FGLPKRQASMQKMKQLLAALGCqLDLDSSAGS---LEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318068885 200 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIItTHYIEEARQ-AHTIGLMRSGHL-LAEE 259
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFI-SHKLPEIRQlADRISVMRDGTIaLSGK 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
54-242 |
1.77e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 54 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCI-------VGRryMDAGEIFVLGGKPGTRGSGVPGK---RVG 123
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGT--IRVGDITIDTARSLSQQKGLIRQlrqHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMPQEIALYGEFSIQETMMYFGWIF-GMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAgKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAgQKTVIITTHYIEEAR 242
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFAR 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
58-262 |
2.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 58 ANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG-----RRYMDAGEIFVLGGKPGTRGSGVPgKRVGYMPQ--EIA 130
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVR-KKVGVVFQfpESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 131 LYGEFSIQETMmyFG-WIFGMDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:PRK13643 97 LFEETVLKDVA--FGpQNFGIPKEKAEKIAAEKLEMVGLADEfwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 208 VDPLLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPS 262
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDvADYADYVYLLEKGHIISCGTPS 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
62-241 |
2.09e-17 |
|
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: 82.13 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRgsgvPGkrvgymPQEIALYGEFSIqetm 141
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-ILEGKQITE----PG------PDRMVVFQNYSL---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 myFGWI-----FGMDTKEIL------ERLQFLLNFLDL-----PSEKRlVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:TIGR01184 66 --LPWLtvrenIALAVDRVLpdlsksERRAIVEEHIALvglteAADKR-PGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 318068885 206 VGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 241
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
57-283 |
3.61e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP---GTRGSGVPGKRVGYMPQ--EIAL 131
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-FDGKPidySRKGLMKLRESVGMVFQdpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YGEfSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:PRK13636 96 FSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIeHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 211 LLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSVLLSiyKCISLEEVFLKLSRI 283
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFA--EKEMLRKVNLRLPRI 246
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
36-242 |
3.65e-17 |
|
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: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC-------IVGRRYmdAGEIFvLGG 108
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EGEIL-LDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 109 K----PGT-----RgsgvpgKRVGyM--------PqeialygeFSIQETMMYFGWIFGMDTKEIL-ERLQFLLNFLDLPS 170
Cdd:COG1117 78 EdiydPDVdvvelR------RRVG-MvfqkpnpfP--------KSIYDNVAYGLRLHGIKSKSELdEIVEESLRKAALWD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 171 EkrlVKN--------LSGGQQRRVSFAVALMHDPELLILDEPTVGVDP--------LLRQsiwnhLvhitkAGQKTVIIT 234
Cdd:COG1117 143 E---VKDrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieeLILE-----L-----KKDYTIVIV 209
|
....*...
gi 318068885 235 THYIEEAR 242
Cdd:COG1117 210 THNMQQAA 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
60-261 |
4.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.57 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG----GKPGTRGSGVPGKRVGYMPQ--EIALYg 133
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQfpEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLpSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL-SEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 318068885 211 LLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESP 261
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDvAEYADDVLVLEHGKLIKHASP 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
38-212 |
4.13e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.77 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGkkknANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGG-----KPGT 112
Cdd:COG4598 4 TAPPALEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRV-GGeeirlKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 113 RGSGVPGK---------RVGYMPQEIALYGEFSIQETMMyFGWI--FGMDTKEILERLQFLLNFLDLpSEKRLV--KNLS 179
Cdd:COG4598 79 DGELVPADrrqlqrirtRLGMVFQSFNLWSHMTVLENVI-EAPVhvLGRPKAEAIERAEALLAKVGL-ADKRDAypAHLS 156
|
170 180 190
....*....|....*....|....*....|...
gi 318068885 180 GGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 212
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPEL 189
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
66-242 |
5.02e-17 |
|
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: 80.68 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 66 NMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIQETM--- 141
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV-NDQSHTGLA--PYQRpVSMLFQENNLFAHLTVRQNIglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MYFGWIFGMDTKEILE---RLQFLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWN 218
Cdd:TIGR01277 95 LHPGLKLNAEQQEKVVdaaQQVGIADYLD-----RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180
....*....|....*....|....
gi 318068885 219 HLVHITKAGQKTVIITTHYIEEAR 242
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDAR 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
61-293 |
5.29e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.06 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTT-------LLSCIVGRRYM------DAGEIFVLGGKPGTrgsgvpgkrVGYMP- 126
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTiakhmnaLLIPSEGKVYVdgldtsDEENLWDIRNKAGM---------VFQNPd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 -QEIAlygefSIQETMMYFG-WIFGMDTKEILERLQFLLNFLDLPSEKRLVKN-LSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:PRK13633 96 nQIVA-----TIVEEDVAFGpENLGIPPEEIRERVDESLKKVGMYEYRRHAPHlLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPsvllsiykcislEEVFLKLSRI 283
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP------------KEIFKEVEMM 238
|
250
....*....|
gi 318068885 284 QSQKGDVTHV 293
Cdd:PRK13633 239 KKIGLDVPQV 248
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
59-284 |
5.84e-17 |
|
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: 81.05 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMD--AGEIFvLGGKPgTRGSGVPGKR--VGYMPQEIALYgE 134
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERFYDptSGEIL-LDGVD-IRDLNLRWLRsqIGLVSQEPVLF-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 FSIQETMMYfGwIFGMDTKEILE--RLQFLLNFL-DLPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELLILDEPTV 206
Cdd:cd03249 91 GTIAENIRY-G-KPDATDEEVEEaaKKANIHDFImSLPDGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 207 GVDPLLRQSIWNHLVHITKAgqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLlsiykcISLEEVFLKLSRIQ 284
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL------MAQKGVYAKLVKAQ 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
56-265 |
6.39e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 56 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEF 135
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETMMYFGWI-FGMDTKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 213
Cdd:PRK13647 95 STVWDDVAFGPVnMGLDKDEVERRVEEALKAVRMWDFRdKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 214 QSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLL 265
Cdd:PRK13647 175 ETLMEILDRLHNQG-KTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
60-283 |
7.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPG--KRVGYMPQ--EIALYGEf 135
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTVGIVFQnpDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETMMYFGWIFGMDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 214
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEgFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 215 SIWNHLVHITKAGQkTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLSIYKCIslEEVFLKLSRI 283
Cdd:PRK13639 175 QIMKLLYDLNKEGI-TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI--RKANLRLPRV 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
62-266 |
7.59e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 7.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRgSGVPGKR--VGYMPQ--EIALYGEfSI 137
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRklVGIVFQnpETQFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSI 216
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 318068885 217 WNHLVHITKAGqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK13644 176 LERIKKLHEKG-KTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
42-294 |
8.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKKNAnqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGE---IFVLGGKPGTRGSGVP 118
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRVGYMPQeialygefsiQETMMYFGWIFGMDTKEILERLQF-----------------LLNFLDlpSEKrlvKNLSGG 181
Cdd:PRK13640 83 REKVGIVFQ----------NPDNQFVGATVGDDVAFGLENRAVprpemikivrdvladvgMLDYID--SEP---ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 182 QQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESP 261
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
250 260 270
....*....|....*....|....*....|...
gi 318068885 262 svllsiykcislEEVFLKLSRIQSQKGDVTHVN 294
Cdd:PRK13640 228 ------------VEIFSKVEMLKEIGLDIPFVY 248
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
50-255 |
1.09e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtrgsgvpgkrvgympQEI 129
Cdd:PRK11153 9 KVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG-------------------QDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMYFGWIF----------------------GMDTKEILERLQFLLNFLDLpSEKRLV--KNLSGGQQRR 185
Cdd:PRK11153 70 TALSEKELRKARRQIGMIFqhfnllssrtvfdnvalplelaGTPKAEIKARVTELLELVGL-SDKADRypAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 186 VSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHL 255
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
57-241 |
1.17e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.52 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKG---TIyglLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgtrgsgvpgKRVGYMPQE-IALY 132
Cdd:COG1101 17 NEKRALDGLNLTIEEGdfvTV---IGSNGAGKSTLLNAIAGSLPPDSGSILIDG------------KDVTKLPEYkRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 133 -------------GEFSIQETMMY-------FGWIFGMDTKEIlERLQFLLNFLDLPSEKRL---VKNLSGGQQRRVSFA 189
Cdd:COG1101 82 igrvfqdpmmgtaPSMTIEENLALayrrgkrRGLRRGLTKKRR-ELFRELLATLGLGLENRLdtkVGLLSGGQRQALSLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA 241
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQA 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
39-256 |
1.49e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.20 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDAGEIFVLGGKPGTRGSGVP 118
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI--NRMNDLNPEVTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRVGY--MPQEIALYGE------FSIQETMMYFGWIFGMDTKEILerlqfllnflDLPSEKRL--------VKN----- 177
Cdd:PRK14239 76 SPRTDTvdLRKEIGMVFQqpnpfpMSIYENVVYGLRLKGIKDKQVL----------DEAVEKSLkgasiwdeVKDrlhds 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 178 ---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEA-RQAHTIGLMRSG 253
Cdd:PRK14239 146 algLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQAsRISDRTGFFLDG 223
|
...
gi 318068885 254 HLL 256
Cdd:PRK14239 224 DLI 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
44-216 |
1.99e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 44 SVRHAFKAYG-----KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgkpgTRGSGVP 118
Cdd:PRK10419 5 NVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG----EPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRVGYMPQEIAL-----YGEFSIQETMmyfGWIFG--------MDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQ 183
Cdd:PRK10419 81 RAQRKAFRRDIQMvfqdsISAVNPRKTV---REIIReplrhllsLDKAERLARASEMLRAVDLDDSvlDKRPPQLSGGQL 157
|
170 180 190
....*....|....*....|....*....|...
gi 318068885 184 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSI 216
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
43-262 |
2.16e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.06 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYgkKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGT-------Rgs 115
Cdd:PRK13635 6 IRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSeetvwdvR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 gvpgKRVGYMPQ-------------EIAlygeFSIQETmmyfgwifGMDTKEILERLQFLLN------FLDlpsekRLVK 176
Cdd:PRK13635 81 ----RQVGMVFQnpdnqfvgatvqdDVA----FGLENI--------GVPREEMVERVDQALRqvgmedFLN-----REPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 177 NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLL 256
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
....*.
gi 318068885 257 AEESPS 262
Cdd:PRK13635 220 EEGTPE 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
64-244 |
2.71e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 64 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrrymDAGEIFVLGGK---PGTRGSGVPG--KRVGYMPQEIALYGEFSIQ 138
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAG----TLSPAFSASGEvllNGRRLTALPAeqRRIGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 139 ETMMyfgwiFGMDTK----EILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLR 213
Cdd:COG4136 95 ENLA-----FALPPTigraQRRARVEQALEEAGLAGfADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190
....*....|....*....|....*....|....*
gi 318068885 214 QSI----WNHLvhitKAGQKTVIITTHYIEEARQA 244
Cdd:COG4136 170 AQFrefvFEQI----RQRGIPALLVTHDEEDAPAA 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
59-236 |
3.11e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 78.40 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL-YGefSI 137
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLfYG--TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMMYFGWIfgMDTKEILERLQF--LLNF-------LDLPSEKRlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:cd03245 95 RDNITLGAPL--ADDERILRAAELagVTDFvnkhpngLDLQIGER-GRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190
....*....|....*....|....*....|
gi 318068885 209 DpllrQSIWNHLVHITKA--GQKTVIITTH 236
Cdd:cd03245 172 D----MNSEERLKERLRQllGDKTLIIITH 197
|
|
| TagG |
COG1682 |
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport ... |
562-752 |
4.35e-16 |
|
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: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 562 PSFTDFVAPGviLTIVFFLAVALTSSALIIERTEGLLdRSwvAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVvFGVT 641
Cdd:COG1682 61 VPYALFLLAG--LLPWNFFSEALNRGSGSIVANAGLI-KK--VYFPREILPLARVLSALVNFLISLVVLLVVLLL-FGVP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 642 NNGDLFWVIVLTLLQGMCGMCFGFLISSVCELERNAIQLaLGSF-YPTLLLSGVIWPIEGMPVVLRYISLCLPLTLATSS 720
Cdd:COG1682 135 PSWTLLLLPLALLLLLLFGLGLGLLLAALNVFFRDVQQI-VGLLlQLLFFLSPVFYPLSTLPEPLRWLLLLNPLTHIIEL 213
|
170 180 190
....*....|....*....|....*....|...
gi 318068885 721 LRSILTRG-WAILESDVYIGYVSTLSWIVGFLV 752
Cdd:COG1682 214 FRAALLGGyLPDWLSLLYALLVSLVLLLLGLLL 246
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
62-255 |
5.75e-16 |
|
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: 82.69 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRryMDAGEifvlgGKPGTRGSgvpgkrVGYMPQEiALYGEFSIQETM 141
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE--MDKVE-----GHVHMKGS------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MYFGWIFGMDTKEILERLQFLLNFLDLPS-------EKRLvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 214
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPDLEILPSgdrteigEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 318068885 215 SIWNHLVHITKA-GQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:TIGR00957 798 HIFEHVIGPEGVlKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
55-236 |
6.21e-16 |
|
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: 76.90 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 55 KKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMD--AGEIFvLGGKPGTRGSgvpGKRVGYMPQEIALY 132
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEIL-INGRPLDKNF---QRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 133 GEFSIQETMMYFGWIFGmdtkeilerlqfllnfldlpsekrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 212
Cdd:cd03232 92 PNLTVREALRFSALLRG----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|....
gi 318068885 213 RQSIWNHLVHITKAGQkTVIITTH 236
Cdd:cd03232 144 AYNIVRFLKKLADSGQ-AILCTIH 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
43-209 |
7.88e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtrgSGVPGKRV 122
Cdd:PRK09544 5 VSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGE--FSIQETMMYFGWIFGMDTKEILERLQfLLNFLDLPSEKrlvknLSGGQQRRVSFAVALMHDPELLI 200
Cdd:PRK09544 70 GYVPQKLYLDTTlpLTVNRFLRLRPGTKKEDILPALKRVQ-AGHLIDAPMQK-----LSGGETQRVLLARALLNRPQLLV 143
|
....*....
gi 318068885 201 LDEPTVGVD 209
Cdd:PRK09544 144 LDEPTQGVD 152
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
43-268 |
8.38e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRV 122
Cdd:COG4604 2 IEIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMyFGWiF----GMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:COG4604 78 AILRQENHINSRLTVRELVA-FGR-FpyskGRLTAEDREIIDEAIAYLDLeDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 198 LLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESP------SVLLSIY 268
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAsCYADHIVAMKDGRVVAQGTPeeiitpEVLSDIY 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
36-263 |
9.53e-16 |
|
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: 77.09 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGgKPGTRGS 115
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-QDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 -----GVPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMD-----TKEILER--LQFLLNFLdlPSEkrlvknLSGGQQ 183
Cdd:COG4181 81 edaraRLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRdararARALLERvgLGHRLDHY--PAQ------LSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 184 RRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSV 263
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
61-266 |
1.27e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQET 140
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 M-M----YFGWIFGMD------TKEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:PRK09536 98 VeMgrtpHRSRFDTWTetdraaVERAMERTG-VAQFAD-----RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 210 PllrqsiwNHLVHITKAGQ------KTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK09536 172 I-------NHQVRTLELVRrlvddgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
54-256 |
1.53e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 54 KKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDA---GEIFVLGG---KPGTRGSGVPGKR--VGYM 125
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRtvqREGRLARDIRKSRanTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 126 PQEIALYGEFSIQETMMY------------FGWIFGMDTKEILERLQF--LLNFldlpSEKRlVKNLSGGQQRRVSFAVA 191
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIgalgstpfwrtcFSWFTREQKQRALQALTRvgMVHF----AHQR-VSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 192 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLL 256
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVF 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
60-279 |
1.66e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.54 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtRGSGVPGKRVGYMPQEIALYGE----- 134
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-------RGEPITKENIREVRKFVGLVFQnpddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 -FSIQ-ETMMYFGWI-FGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:PRK13652 91 iFSPTvEQDIAFGPInLGLDEETVAHRVSSALHMLGLEElRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 211 LLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPsvllsiykcislEEVFLK 279
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTV------------EEIFLQ 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
61-258 |
2.18e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR----VGYMPQE---IALYG 133
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR-LDGEDITGLS--PRERrrlgVAYIPEDrlgRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EFSIQETMM--------YFGWIFgMDTKEILERLQFLLNFLDL--PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:COG3845 350 DMSVAENLIlgryrrppFSRGGF-LDRKAIRAFAEELIEEFDVrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQ-AHTIGLMRSGHLLAE 258
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAG-AAVLLISEDLDEILAlSDRIAVMYEGRIVGE 483
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
66-241 |
3.18e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.77 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 66 NMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPGKR-VGYMPQEIALYGEFSIQETM--- 141
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-LNGQDHTTTP--PSRRpVSMLFQENNLFSHLTVAQNIglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MYFGWIFGMDTKEILERLQ---FLLNFLD-LPSEkrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIW 217
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIArqmGIEDLLArLPGQ------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180
....*....|....*....|....
gi 318068885 218 NHLVHITKAGQKTVIITTHYIEEA 241
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDA 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
52-266 |
3.52e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKKKNANQvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL 131
Cdd:PRK13642 14 YEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YGEFSIQETMMYFGWIF-GMDTKEILERLQ---FLLNFLDLPSekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:PRK13642 93 QFVGATVEDDVAFGMENqGIPREEMIKRVDealLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 208 VDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-262 |
4.57e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.72 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC------------IVGRRYMDAGEIFVLGGKPGTRgsgvpgkRVGYMPQ 127
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFKMDVIELRR-------RVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 EIALYGEFSIQETMMyfgwiFGM-------DTKEILERLQFLL----------NFLDLPSEKrlvknLSGGQQRRVSFAV 190
Cdd:PRK14247 90 IPNPIPNLSIFENVA-----LGLklnrlvkSKKELQERVRWALekaqlwdevkDRLDAPAGK-----LSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 191 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEE-ARQAHTIGLMRSGHLLaEESPS 262
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQaARISDYVAFLYKGQIV-EWGPT 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
41-266 |
5.01e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSgvPG- 119
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR-LNGRPLADWS--PAe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 --KRVGYMPQEIALYGEFSIQEtmmyfgwIFGM----------DTKEILERLQFLLNFLDLpsEKRLVKNLSGGQQRRVS 187
Cdd:PRK13548 74 laRRRAVLPQHSSLSFPFTVEE-------VVAMgraphglsraEDDALVAAALAQVDLAHL--AGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 188 FAVALM------HDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEES 260
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
....*.
gi 318068885 261 PSVLLS 266
Cdd:PRK13548 225 PAEVLT 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
50-258 |
5.50e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSG----VPGKRVGYM 125
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 126 PQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSFAVALMHDPEL 198
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLehranhrPSE------LSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 199 LILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 258
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
60-275 |
8.36e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP---GTRGSGVPGKRVGYM---PQEIALYG 133
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPldySKRGLLALRQQVATVfqdPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 EfsIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLL 212
Cdd:PRK13638 94 D--IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 213 RQSIWNHLVHITKAGQKtVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSvllSIYKCISLEE 275
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNH-VIISSHDIDLIYEiSDAVYVLRQGQILTHGAPG---EVFACTEAME 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
61-265 |
1.00e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGRRYMDAGEIFVLGGKP-GTRGSGVPGKRVGYMPQEIALYGEFSIQE 139
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILLDAQPlESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 140 --TMMYFGW--IFGMDTKEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDpLLRQ 214
Cdd:PRK10575 105 lvAIGRYPWhgALGRFGAADREKVEEAISLVGLkPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 215 SIWNHLVH-ITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPSVLL 265
Cdd:PRK10575 184 VDVLALVHrLSQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
60-211 |
1.38e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.80 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtRGSGVPG----------KRVGYMPQEI 129
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-------DGENIPAmsrsrlytvrKRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMmyfGWIFGMDTK--EILERLQFLLNFLD---------LPSEkrlvknLSGGQQRRVSFAVALMHDPEL 198
Cdd:PRK11831 94 ALFTDMNVFDNV---AYPLREHTQlpAPLLHSTVMMKLEAvglrgaaklMPSE------LSGGMARRAALARAIALEPDL 164
|
170
....*....|...
gi 318068885 199 LILDEPTVGVDPL 211
Cdd:PRK11831 165 IMFDEPFVGQDPI 177
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
61-265 |
1.41e-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: 77.47 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGS-GVPGKRVGYMPQEIALYGEfSIQE 139
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI-LLNGFSLKDIDrHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 140 TMMyFGWIFGMDTKEILERLQFL-----LNFLDLPSEKRLVK---NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 211
Cdd:TIGR01193 567 NLL-LGAKENVSQDEIWAACEIAeikddIENMPLGYQTELSEegsSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 318068885 212 LRQSIWNHLVHITkagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLL 265
Cdd:TIGR01193 646 TEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-205 |
2.31e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.47 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtrgsgvpgK- 120
Cdd:PRK15064 319 ALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------------Kw 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 ----RVGYMPQEIAlyGEFSIQETMmyFGWIfGMDTKE---------ILERLQFLLNflDLpseKRLVKNLSGGQQRRVS 187
Cdd:PRK15064 379 senaNIGYYAQDHA--YDFENDLTL--FDWM-SQWRQEgddeqavrgTLGRLLFSQD--DI---KKSVKVLSGGEKGRML 448
|
170
....*....|....*...
gi 318068885 188 FAVALMHDPELLILDEPT 205
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPT 466
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-256 |
2.56e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDAGEIFVLGGKPGTRGSGVPG---------KRVGYMPQEI 129
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF--NRLLELNEEARVEGEVRLFGRNIYSpdvdpievrREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMYFGWIFGM--DTKEILERLQFLLNFLDLPSE--KRL---VKNLSGGQQRRVSFAVALMHDPELLILD 202
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEvkDRLndyPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHY-IEEARQAHTIGLMRSGHLL 256
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
61-236 |
2.81e-14 |
|
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: 76.83 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgSGV------PG---KRVGYMPQEIAL 131
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLL---------DGVdirqidPAdlrRNIGYVPQDPRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 -YGefSIQETMMyfgwiFGM---DTKEILERLQF--LLNF-------LDLP-SEKRLvkNLSGGQQRRVSFAVALMHDPE 197
Cdd:TIGR03375 551 fYG--TLRDNIA-----LGApyaDDEEILRAAELagVTEFvrrhpdgLDMQiGERGR--SLSGGQRQAVALARALLRDPP 621
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 318068885 198 LLILDEPTVGVDpllrQSIWNHLVHITKA--GQKTVIITTH 236
Cdd:TIGR03375 622 ILLLDEPTSAMD----NRSEERFKDRLKRwlAGKTLVLVTH 658
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
50-236 |
3.63e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKNANQ--VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRY--MDAGEIFVLGGKPGTRGSGVpgkrvgym 125
Cdd:COG2401 32 EAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLI-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 126 pQEIALYGEFSiqetmmyfgwifgmDTKEILERLQflLNflDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:COG2401 104 -DAIGRKGDFK--------------DAVELLNAVG--LS--DAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|.
gi 318068885 206 VGVDPLLRQSIWNHLVHITKAGQKTVIITTH 236
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
63-210 |
3.72e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 63 NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTrgsGVPGKRVGYMP-----QEIALYGEFSI 137
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-LLRGQHIE---GLPGHQIARMGvvrtfQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMM----------YFGWIFGMDT-----KEILERLQFLLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:PRK11300 98 IENLLvaqhqqlktgLFSGLLKTPAfrraeSEALDRAATWLERVGLlEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
....*....
gi 318068885 202 DEPTVGVDP 210
Cdd:PRK11300 178 DEPAAGLNP 186
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
39-257 |
3.75e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYgkkKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLgGKPGTRgsGVP 118
Cdd:PRK15056 3 QQAGIVVNDVTVTW---RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIL-GQPTRQ--ALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRVGYMPQEIALYGEFSI---QETMM----YFGW--IFGMDTKEILERLQFLLNFLDLpsEKRLVKNLSGGQQRRVSFA 189
Cdd:PRK15056 77 KNLVAYVPQSEEVDWSFPVlveDVVMMgrygHMGWlrRAKKRDRQIVTAALARVDMVEF--RHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 190 VALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYIEEARQAHTIGLMRSGHLLA 257
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSVTEFCDYTVMVKGTVLA 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
61-236 |
3.76e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 75.94 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrrymdageifVLggkPGTRGS----GVP---------GKRVGYMPQ 127
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG----------VW---PPTAGSvrldGADlsqwdreelGRHIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 EIALYgEFSIQEtmmyfgwifgmdtkeilerlqfllN---FLDLPSEK-----RLV---------------------KNL 178
Cdd:COG4618 414 DVELF-DGTIAE------------------------NiarFGDADPEKvvaaaKLAgvhemilrlpdgydtrigeggARL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318068885 179 SGGQQRRVSFAVALMHDPELLILDEPTVGVDPL----LRQSIWNHlvhitKAGQKTVIITTH 236
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEgeaaLAAAIRAL-----KARGATVVVITH 525
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
51-266 |
5.72e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 51 AYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDA--GEIFVLGGKPGTRGSGVPGKRVGYMPQE 128
Cdd:PRK10253 16 GYGKYT----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL--SRLMTPahGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 IALYGEFSIQETM---------MYFGWifGMDTKEILERLQFLLNFLDLPSEKrlVKNLSGGQQRRVSFAVALMHDPELL 199
Cdd:PRK10253 90 ATTPGDITVQELVargryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQS--VDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 200 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQA-HTIGLmRSGHLLAEESPSVLLS 266
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYAsHLIAL-REGKIVAQGAPKEIVT 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
52-241 |
8.76e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKkknaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDAGEIFVLGGKPGTRGSGVPGK---------RV 122
Cdd:PRK14243 20 YGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCF--NRLNDLIPGFRVEGKVTFHGKNLYAPdvdpvevrrRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEfSIQETMMYFGWIFGM--DTKEILERLQFLLNFLDLPSEKrLVKN---LSGGQQRRVSFAVALMHDPE 197
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYGARINGYkgDMDELVERSLRQAALWDEVKDK-LKQSglsLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 318068885 198 LLILDEPTVGVDPLLRQSIwNHLVHITKAgQKTVIITTHYIEEA 241
Cdd:PRK14243 172 VILMDEPCSALDPISTLRI-EELMHELKE-QYTIIIVTHNMQQA 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
39-236 |
8.96e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLgGKPGTR----- 113
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQmdeea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 114 GSGVPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLpsEKRLV---KNLSGGQQRRVSFAV 190
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGL--GKRLDhlpAQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 318068885 191 ALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH 236
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-205 |
1.41e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.20 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 34 NGPRNTQAAVSVRHAFKAYGKKknanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtr 113
Cdd:TIGR03719 314 PGPRLGDKVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 114 GSGVpgkRVGYMPQE-IALYGEFSIQETMMYFGWIFGMDTKEILERL---QFllNFLDLPSEKRlVKNLSGGQQRRVSFA 189
Cdd:TIGR03719 382 GETV---KLAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgRF--NFKGSDQQKK-VGQLSGGERNRVHLA 455
|
170
....*....|....*.
gi 318068885 190 VALMHDPELLILDEPT 205
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPT 471
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
60-261 |
1.49e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.38 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGrrYMDageifvlggKPGTRGSGVPGKRVGYMPQE--IALYGEfsi 137
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILG--CLD---------KPTSGTYRVAGQDVATLDADalAQLRRE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 qetmmYFGWIF----------------------GMDTKEILERLQFLLNFLDL-------PSEkrlvknLSGGQQRRVSF 188
Cdd:PRK10535 87 -----HFGFIFqryhllshltaaqnvevpavyaGLERKQRLLRAQELLQRLGLedrveyqPSQ------LSGGQQQRVSI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHTIGLMRSGHLLAEESP 261
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
61-236 |
1.80e-13 |
|
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: 69.83 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQET 140
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-LLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MMYFGWIFGMDT-KEILERLQfLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD----PLLRQS 215
Cdd:cd03231 94 LRFWHADHSDEQvEEALARVG-LNGFEDRP-----VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEA 167
|
170 180
....*....|....*....|.
gi 318068885 216 IWNHLvhitkAGQKTVIITTH 236
Cdd:cd03231 168 MAGHC-----ARGGMVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
64-255 |
2.57e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 64 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGsgvPGKRVG----YMPQEIALYGEF---- 135
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TAQRLArglvYLPEDRQSSGLYldap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 ------SIQETMMYFgWIFGMDTKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:PRK15439 358 lawnvcALTHNRRGF-WIKPARENAVLERYRRALN-IKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 318068885 210 PLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-256 |
3.63e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.08 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSC------IVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIA 130
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 131 LYGEFSIQETMMYFGWIFGM-DTKEILERLQFLLNFLDLPSE--KRL---VKNLSGGQQRRVSFAVALMHDPELLILDEP 204
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLWKEvyDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 205 TVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEE-ARQAHTIGLMRSGHLL 256
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQvARVADYVAFLYNGELV 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
43-266 |
4.29e-13 |
|
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: 69.57 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMD--AGEIFVLG------GKPGTRg 114
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDvsSGSILIDGqdirevTLDSLR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 115 sgvpgKRVGYMPQEIALYgefsiQETMMY---FGWIFGMDtKEILERLQ------FLLNFLDLPSEK---RLVKnLSGGQ 182
Cdd:cd03253 75 -----RAIGVVPQDTVLF-----NDTIGYnirYGRPDATD-EEVIEAAKaaqihdKIMRFPDGYDTIvgeRGLK-LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 183 QRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAgqKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPS 262
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHE 220
|
....
gi 318068885 263 VLLS 266
Cdd:cd03253 221 ELLA 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
36-255 |
4.82e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 69.04 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYgKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGRRYMDAGEIFVLGGKPgtrgs 115
Cdd:cd03248 5 PDHLKGIVKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVA-LLENFYQPQGGQVLLDGKP----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 gVPGKRVGYMPQEIALYGE----F--SIQETMMYfgwifGMDTK---EILERLQ------FLLNFLDLPSEKRLVKN--L 178
Cdd:cd03248 78 -ISQYEHKYLHSKVSLVGQepvlFarSLQDNIAY-----GLQSCsfeCVKEAAQkahahsFISELASGYDTEVGEKGsqL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 179 SGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIwnHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV--QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
59-269 |
5.04e-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: 68.32 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR-RY-MDAGEIFvLGGKPGTRGSgvpgkrvgymPQEIALYGEF- 135
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYeVTEGEIL-FKGEDITDLP----------PEERARLGIFl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETMMYFGwifgmdtkeilERLQFLLNFLDlpsekrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQS 215
Cdd:cd03217 82 AFQYPPEIPG-----------VKNADFLRYVN--------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 216 IWNHLVHITKAGqKTVIITTHY--IEEARQAHTIGLMRSGHLLAEESPSVLLSIYK 269
Cdd:cd03217 143 VAEVINKLREEG-KSVLIITHYqrLLDYIKPDRVHVLYDGRIVKSGDKELALEIEK 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
61-277 |
5.36e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMD--AGEIFVLGGKPGTRGSgvpgKRVGYMPQEIALYGEFSIQ 138
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL----KRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 139 ETMMYFGWIF---GMDTKEILERLQFLLNFLDLPS-EKRLVKN-----LSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:PLN03211 159 ETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKcENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 210 PLLRQSIWNHLVHITKAGqKTVIITTHYIEEA--RQAHTIGLMRSGHLLAEESPSVLLSIYKCISLEEVF 277
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKG-KTIVTSMHQPSSRvyQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSF 307
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
43-205 |
7.64e-13 |
|
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: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAY-------GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGS 115
Cdd:COG4608 8 LEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL-FDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 GV---------------------PGKRVGympqEIalygefsIQETMMyfgwIFGMDTK-EILERLQFLLNFLDLPSE-- 171
Cdd:COG4608 87 GRelrplrrrmqmvfqdpyaslnPRMTVG----DI-------IAEPLR----IHGLASKaERRERVAELLELVGLRPEha 151
|
170 180 190
....*....|....*....|....*....|....
gi 318068885 172 KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:COG4608 152 DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
48-241 |
7.99e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 48 AFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKP------GTR-----GSG 116
Cdd:PRK11247 14 LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTAPlaeareDTRlmfqdARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 117 VPGKR----VGympqeIALYGEFSIQetmmyfgwifgmdTKEILERLQFLLNFLDLPSEkrlvknLSGGQQRRVSFAVAL 192
Cdd:PRK11247 93 LPWKKvidnVG-----LGLKGQWRDA-------------ALQALAAVGLADRANEWPAA------LSGGQKQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 193 MHDPELLILDEPTVGVDPLLR-------QSIWnhlvhitkagQK---TVIITTHYIEEA 241
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRiemqdliESLW----------QQhgfTVLLVTHDVSEA 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
62-209 |
1.05e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvpgkrvgymPQEIALYGEFSIQETM 141
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV-TLDGHEVVTRS----------PQDGLANGIVYISEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MYFGWIFGMDTKE--ILERLQFLLN----------------FLDL-----PSEKRLVKNLSGGQQRRVSFAVALMHDPEL 198
Cdd:PRK10762 337 KRDGLVLGMSVKEnmSLTALRYFSRaggslkhadeqqavsdFIRLfniktPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170
....*....|.
gi 318068885 199 LILDEPTVGVD 209
Cdd:PRK10762 417 LILDEPTRGVD 427
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
55-266 |
1.43e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 55 KKNANQ---VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKpgtrgsgVPGKRVGYMPQEIAL 131
Cdd:PRK13650 13 KYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-------LTEENVWDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 Y-----GEF--SIQETMMYFGWIF-GMDTKEILERLQFLLNFLDLPSEK-RLVKNLSGGQQRRVSFAVALMHDPELLILD 202
Cdd:PRK13650 86 VfqnpdNQFvgATVEDDVAFGLENkGIPHEEMKERVNEALELVGMQDFKeREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
62-283 |
1.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKRVGYMPQEIALYGEFS----I 137
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV-DDTLITSTS--KNKDIKQIRKKVGLVFQFPesqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMM---YFG-WIFGMDTKEILERLQFLLNFLDLpSEKRLVKN---LSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:PRK13649 100 EETVLkdvAFGpQNFGVSQEEAEALAREKLALVGI-SESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 211 LLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESPSvllSIYKCIS-LEEVFLKLSRI 283
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGM-TIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPK---DIFQDVDfLEEKQLGVPKI 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
55-236 |
1.75e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 55 KKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR---YMDAGEIFVLGGKpgtRGSGVPgKRVGYMPQEIAL 131
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRP---LDSSFQ-RSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YGEFSIQETMMYFGWI---FGMDTKEILERLQFLLNFLDLPSEKRLVKNLSGG-----QQRRVSFAVALMHDPELLI-LD 202
Cdd:TIGR00956 848 LPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEglnveQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTH 236
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIH 960
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
46-266 |
2.05e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.68 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 46 RHAFKAYGKKKNANQVLN---------NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSG 116
Cdd:PRK10070 19 QRAFKYIEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 117 ----VPGKRVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSEKR-LVKNLSGGQQRRVSFAVA 191
Cdd:PRK10070 99 elreVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHsYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 192 LMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEA-RQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
47-255 |
2.73e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 47 HAFKAYgkkKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTR--GSGVP--GKRV 122
Cdd:PRK10908 6 HVSKAY---LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW-FSGHDITRlkNREVPflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 123 GYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKaKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEE-ARQAHTIGLMRSGHL 255
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGV-TVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
53-244 |
3.43e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 53 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALY 132
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 133 GEfSIQETMMyFGWIFGMDTKEILERLQFLLNFlDLPSE--KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:PRK10247 94 GD-TVYDNLI-FPWQIRNQQPDPAIFLDDLERF-ALPDTilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*
gi 318068885 211 LLRQSIwNHLVH-ITKAGQKTVIITTHYIEEARQA 244
Cdd:PRK10247 171 SNKHNV-NEIIHrYVREQNIAVLWVTHDKDEINHA 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
64-236 |
3.72e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 64 NLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKPGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMY 143
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL-WQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 144 FGWIFGM----DTKEILERLQfLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLILDEP-----TVGVDPLLRq 214
Cdd:PRK13538 98 YQRLHGPgddeALWEALAQVG-LAGFEDVP-----VRQLSAGQQRRVALARLWLTRAPLWILDEPftaidKQGVARLEA- 170
|
170 180
....*....|....*....|...
gi 318068885 215 siwnHLV-HITKAGqkTVIITTH 236
Cdd:PRK13538 171 ----LLAqHAEQGG--MVILTTH 187
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-246 |
5.08e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 32 PANGPRntqaaVSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKpg 111
Cdd:PRK10938 255 PANEPR-----IVLNNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGR-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 112 TRGSGVP----GKRVGYMPQEIALygEFSIQETMM------YFGWIfGMdTKEILERLQFL----LNFLDLPseKRLVK- 176
Cdd:PRK10938 324 RRGSGETiwdiKKHIGYVSSSLHL--DYRVSTSVRnvilsgFFDSI-GI-YQAVSDRQQKLaqqwLDILGID--KRTADa 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 177 ---NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHT 246
Cdd:PRK10938 398 pfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACIT 470
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
58-253 |
5.16e-12 |
|
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: 67.19 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 58 ANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtRGSGvpgkRVGYMPQeIALYGEFSI 137
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------KHSG----RISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMmyfgwIFGMDTKE-----ILERLQFLLNFLDLPSEKRLVK-----NLSGGQQRRVSFAVALMHDPELLILDEPTVG 207
Cdd:cd03291 115 KENI-----IFGVSYDEyryksVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 318068885 208 VDPLLRQSIWNHLVHITKAgQKTVIITTHYIEEARQAHTIGLMRSG 253
Cdd:cd03291 190 LDVFTEKEIFESCVCKLMA-NKTRILVTSKMEHLKKADKILILHEG 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
43-239 |
7.97e-12 |
|
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: 68.29 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrryMDAGE------IFVLG--------G 108
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG---MDQYEptsgriIYHVAlcekcgyvE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 109 KPGTRGSGVPG------------------------KRVGYMPQE-IALYGEFSIQETMMYFGWIFGMDTKEILERLQFLL 163
Cdd:TIGR03269 74 RPSKVGEPCPVcggtlepeevdfwnlsdklrrrirKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 164 NFLDLpsEKR---LVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE 239
Cdd:TIGR03269 154 EMVQL--SHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
41-213 |
9.42e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 41 AAVSVRHAFKAYGkkkNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK------PGTRG 114
Cdd:PRK11650 2 AGLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRvvnelePADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 115 sgvpgkrVGYMPQEIALYGEFSIQETMMYFGWIFGMDTKEILERLQF------LLNFLDlpsekRLVKNLSGGQQRRVSF 188
Cdd:PRK11650 78 -------IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarileLEPLLD-----RKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|....*
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLR 213
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLR 170
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-236 |
1.06e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvGRRYMDAGEIFVlGGKPGTRGSGVPGKRVGY--MPQEIALYGE 134
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRV-EGRVEFFNQNIYERRVNLnrLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 ------FSIQETMMY----FGWIFGMDTKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELLILD 202
Cdd:PRK14258 96 kpnlfpMSVYDNVAYgvkiVGWRPKLEIDDIVESALKDADLWDEIKHKihKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....*
gi 318068885 203 EPTVGVDPLLRQSIwNHLVHITK-AGQKTVIITTH 236
Cdd:PRK14258 176 EPCFGLDPIASMKV-ESLIQSLRlRSELTMVIVSH 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
53-243 |
1.13e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 53 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLG---GKPGTRGSGVPGkrVGYMPQEI 129
Cdd:PRK09700 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAQLG--IGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETmMYFGW-----IFG---MDTKEILERLQFLLNFLDL---PSEKrlVKNLSGGQQRRVSFAVALMHDPEL 198
Cdd:PRK09700 90 SVIDELTVLEN-LYIGRhltkkVCGvniIDWREMRVRAAMMLLRVGLkvdLDEK--VANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 318068885 199 LILDEPTVG-----VDPLLrqSIWNHLvhitKAGQKTVIITTHYIEEARQ 243
Cdd:PRK09700 167 IIMDEPTSSltnkeVDYLF--LIMNQL----RKEGTAIVYISHKLAEIRR 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
61-249 |
1.19e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSgvPGKRVGYMPQEIALYGEFSIQET 140
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-KLDGGDIDDPD--VAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MMYFGWIFGMDTKEILERLQF--LLNFLDLPSekrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP----LLRQ 214
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAvgLAPLAHLPF-----GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaavaLFAE 168
|
170 180 190
....*....|....*....|....*....|....*
gi 318068885 215 SIWNHLvhitkAGQKTVIITTHYIEEARQAHTIGL 249
Cdd:PRK13539 169 LIRAHL-----AQGGIVIAATHIPLGLPGARELDL 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
60-205 |
1.35e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLgGKP----GTRGSGVPGkrVGYMPQEIALYGEF 135
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL-GKEvtfnGPKSSQEAG--IGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 136 SIQETMMY---FGWIFG-MDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:PRK10762 95 TIAENIFLgreFVNRFGrIDWKKMYAEADKLLARLNLRfSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
60-205 |
1.57e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKP----GTRGSGVPGKRVGYmpQEIALYGEF 135
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-LIDGQEmrfaSTTAALAAGVAIIY--QELHLVPEM 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 136 SIQETMMY------FGWIfgmDTKEILERLQFLLNFLDL---PSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:PRK11288 95 TVAENLYLgqlphkGGIV---NRRLLNYEAREQLEHLGVdidPDTP--LKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
56-236 |
2.01e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 56 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTRGSgvPGKRVGYMPQEIALYGEF 135
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGD--RSRFMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETMMYFGWIFGMDTKEILERLQFLLNFLDlpSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP----L 211
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQMPGSALAIVGLAG--YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLegitL 175
|
170 180
....*....|....*....|....*
gi 318068885 212 LRQSIWNHLvhitkAGQKTVIITTH 236
Cdd:PRK13543 176 VNRMISAHL-----RGGGAALVTTH 195
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
62-253 |
2.70e-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: 63.89 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR----VGYMPQEIALYGEfSI 137
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMMyFGWIFGMDT-KEILE--RLQFLLNFLDLPSEKRLVK---NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 211
Cdd:cd03290 96 EENIT-FGSPFNKQRyKAVTDacSLQPDIDLLPFGDQTEIGErgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 318068885 212 LRQSIWNH-LVHITKAGQKTVIITTHYIEEARQAHTIGLMRSG 253
Cdd:cd03290 175 LSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
61-236 |
2.71e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtrGSGVPGKRVGYMpQEIALYGE------ 134
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-------RQSIKKDLCTYQ-KQLCFVGHrsginp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 -FSIQETmMYFGWIFGMDTKEILE--RLQFLLNFLDLPSEKrlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 211
Cdd:PRK13540 88 yLTLREN-CLYDIHFSPGAVGITElcRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*.
gi 318068885 212 LRQSIWNHL-VHITKAGqkTVIITTH 236
Cdd:PRK13540 162 SLLTIITKIqEHRAKGG--AVLLTSH 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
62-280 |
2.74e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.77 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQ--EIALYGefSIQE 139
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQnpDNQFVG--SIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 140 TMMYFGWI-FGMDTKEILERLQFLLNFLDL----PSEKrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQ 214
Cdd:PRK13648 103 YDVAFGLEnHAVPYDEMHRRVSEALKQVDMleraDYEP---NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 215 SIWNhLVHITKAGQKTVIIT-THYIEEARQAHTIGLMRSGHLLAEESPSvllSIYKCI-SLEEVFLKL 280
Cdd:PRK13648 180 NLLD-LVRKVKSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGTPT---EIFDHAeELTRIGLDL 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
51-205 |
3.20e-11 |
|
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: 66.63 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 51 AYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKT-TLLScIVG----RRYMDAGEIFVLG----GKPGTRGSGVPGKR 121
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRllpdPAAHPSGSILFDGqdllGLSERELRRIRGNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 VGYMPQE----------IalygEFSIQETMMyfgWIFGMDTKEILERLQFLLNFLDLPSEKRLVK----NLSGGQQRRVS 187
Cdd:COG4172 94 IAMIFQEpmtslnplhtI----GKQIAEVLR---LHRGLSGAAARARALELLERVGIPDPERRLDayphQLSGGQRQRVM 166
|
170
....*....|....*...
gi 318068885 188 FAVALMHDPELLILDEPT 205
Cdd:COG4172 167 IAMALANEPDLLIADEPT 184
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
60-210 |
3.28e-11 |
|
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: 63.99 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRrYM-DAGEIFVLggkpgTRGSGVPgkRVGYMPQEI-ALYgefsi 137
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGN-YLpDSGSILVR-----HDGGWVD--LAQASPREIlALR----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETMmyfGWI--F--------------------GMDTKEILERLQFLLNFLDLPseKRL----VKNLSGGQQRRVSFAVA 191
Cdd:COG4778 92 RRTI---GYVsqFlrviprvsaldvvaepllerGVDREEARARARELLARLNLP--ERLwdlpPATFSGGEQQRVNIARG 166
|
170
....*....|....*....
gi 318068885 192 LMHDPELLILDEPTVGVDP 210
Cdd:COG4778 167 FIADPPLLLLDEPTASLDA 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-205 |
3.98e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 34 NGPRNTQAAVSVRHAFKAYGKKknanqVL-NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgt 112
Cdd:PRK11819 316 PGPRLGDKVIEAENLSKSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 113 rGSGVpgkRVGYMPQ-------EIALYGEFSIQETMMYFGwifgmdTKEILERL---QFllNFLDLPSEKRlVKNLSGGQ 182
Cdd:PRK11819 384 -GETV---KLAYVDQsrdaldpNKTVWEEISGGLDIIKVG------NREIPSRAyvgRF--NFKGGDQQKK-VGVLSGGE 450
|
170 180
....*....|....*....|...
gi 318068885 183 QRRVSFAVALMHDPELLILDEPT 205
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
60-238 |
4.68e-11 |
|
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: 63.58 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIY-----GLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtrgsGVPGKRVGYMPQEIALYGE 134
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 135 FSIQETMMYFGWIFGMDTK---EILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPL 211
Cdd:cd03237 76 GTVRDLLSSITKDFYTHPYfktEIAKPLQ-IEQILD-----REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190
....*....|....*....|....*....|....
gi 318068885 212 LRqsiwnhlVHITKA-------GQKTVIITTHYI 238
Cdd:cd03237 150 QR-------LMASKVirrfaenNEKTAFVVEHDI 176
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
36-255 |
4.79e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 36 PRNTQAAVSVRHAFKAYGKKKNaNQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgS 115
Cdd:TIGR00958 472 PLNLEGLIEFQDVSFSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---------D 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 GVP---------GKRVGYMPQEIALYGEfSIQETMMYFGWIFGMDTKEILERLQFLLNFL-DLPS-------EKRlvKNL 178
Cdd:TIGR00958 542 GVPlvqydhhylHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNgydtevgEKG--SQL 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 179 SGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNhlvhITKAGQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
38-254 |
7.67e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.41 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGKKKNanqvLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTR---G 114
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 115 SGVPGKRV------GYMPQEIA--LYGEFS----IQETMMYFGW----------IFGMDTKEI-LERLQfllnflDLPSe 171
Cdd:PRK11701 78 LSEAERRRllrtewGFVHQHPRdgLRMQVSaggnIGERLMAVGArhygdirataGDWLERVEIdAARID------DLPT- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 172 krlvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD--------PLLRQsiwnhLVHITkagQKTVIITTHYIEEARQ 243
Cdd:PRK11701 151 -----TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarllDLLRG-----LVREL---GLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 318068885 244 -AHTIGLMRSGH 254
Cdd:PRK11701 218 lAHRLLVMKQGR 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
61-210 |
9.85e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTiyGLL--GASGCGKTTLLSCIV-------GR-RYMDAGEIFVLGGKPgtrgsgvpgkrvgYMPQ--- 127
Cdd:COG4178 378 LLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAglwpygsGRiARPAGARVLFLPQRP-------------YLPLgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 -EIALY----GEFSiQETMmyfgwifgmdtKEILER--LQFLLNFLDLpsEKRLVKNLSGGQQRRVSFAVALMHDPELLI 200
Cdd:COG4178 443 rEALLYpataEAFS-DAEL-----------REALEAvgLGHLAERLDE--EADWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170
....*....|
gi 318068885 201 LDEPTVGVDP 210
Cdd:COG4178 509 LDEATSALDE 518
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
62-257 |
1.21e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR-VGYMPQEIALYGEFSIQET 140
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 M----------------MYfgwifgMDTKEILERLQFLLNfldlPSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEP 204
Cdd:PRK10982 94 MwlgryptkgmfvdqdkMY------RDTKAIFDELDIDID----PRAK--VATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 205 TVGvdplLRQSIWNHLVHITKAGQKT---VIITTHYIEEARQ-AHTIGLMRSGHLLA 257
Cdd:PRK10982 162 TSS----LTEKEVNHLFTIIRKLKERgcgIVYISHKMEEIFQlCDEITILRDGQWIA 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-254 |
2.60e-10 |
|
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: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlggkpgtRGSGvpgkRVGYMPQeIALYGEFSIQET 140
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------KHSG----RISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MmyfgwIFGMDTKE-----ILERLQFLLNFLDLPSEKRLVK-----NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:TIGR01271 507 I-----IFGLSYDEyrytsVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 318068885 211 LLRQSIWNHLVHITKAgQKTVIITTHYIEEARQAHTIGLMRSGH 254
Cdd:TIGR01271 582 VTEKEIFESCLCKLMS-NKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
39-254 |
2.65e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.58 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 39 TQAAVSVRHAFKAYGKKKNanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFvLGGKP-GTRGSGV 117
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR-LDGRPlSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PGKRVGYMPQE-IALYGEFSIQETMmyfgwifGMDTKE-----ILERLQFLLNFLDLPS--EKRLVK---NLSGGQQRRV 186
Cdd:PRK10790 413 LRQGVAMVQQDpVVLADTFLANVTL-------GRDISEeqvwqALETVQLAELARSLPDglYTPLGEqgnNLSVGQKQLL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 187 SFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGH 254
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
50-236 |
2.69e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrryMDA---GEIFVLggkpgtrgsgvPGKRVGYMP 126
Cdd:PRK11819 14 KVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKefeGEARPA-----------PGIKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 127 QEIALYGEFSIQETMMYfgwifGM-DTKEILER------------------------LQFLLNFLD-------------- 167
Cdd:PRK11819 77 QEPQLDPEKTVRENVEE-----GVaEVKAALDRfneiyaayaepdadfdalaaeqgeLQEIIDAADawdldsqleiamda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 168 --LPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTvgvdpllrqsiwNHL----V-----HITK-AGqkTVIITT 235
Cdd:PRK11819 152 lrCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT------------NHLdaesVawleqFLHDyPG--TVVAVT 217
|
.
gi 318068885 236 H 236
Cdd:PRK11819 218 H 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
50-236 |
2.69e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.42 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgsgVPGKRVGYMPQEI 129
Cdd:TIGR03719 12 KVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMMYfgwifGM-DTKEILER------------------------LQFLL----------------NFLDL 168
Cdd:TIGR03719 78 QLDPTKTVRENVEE-----GVaEIKDALDRfneisakyaepdadfdklaaeqaeLQEIIdaadawdldsqleiamDALRC 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 169 PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPllrQSI-W--NHLvhitKAGQKTVIITTH 236
Cdd:TIGR03719 153 PPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVaWleRHL----QEYPGTVVAVTH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
43-264 |
3.13e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAYGKKKnanqVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDA--GEIFVLGGKPGTRG-SGVPG 119
Cdd:TIGR02633 2 LEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 KRVGYMPQEIALYGEFSIQETMMYFGWI----FGMDTKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALM 193
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNvtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 194 HDPELLILDEPTVGvdpLLRQ--SIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVL 264
Cdd:TIGR02633 158 KQARLLILDEPSSS---LTEKetEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTM 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-258 |
4.18e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 42 AVSVRHAFKAYgKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR-RYMDAGEIFVlggkpgtRGSgvpgk 120
Cdd:PLN03232 614 AISIKNGYFSW-DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVI-------RGS----- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 rVGYMPQEIALYGEfSIQETMMyfgwiFGMDTKEilER------LQFLLNFLDLPSEKRLVK------NLSGGQQRRVSF 188
Cdd:PLN03232 681 -VAYVPQVSWIFNA-TVRENIL-----FGSDFES--ERywraidVTALQHDLDLLPGRDLTEigergvNISGGQKQRVSM 751
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 189 AVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITThyieearQAHTIGLMRSGHLLAE 258
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTN-------QLHFLPLMDRIILVSE 814
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
48-255 |
4.56e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 48 AFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMDA--GEIfvlggkpgtRGSGVPGKRVgym 125
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVseGDI---------RFHDIPLTKL--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 126 pQEIALYGEFSI-QETMMYFGWIFGMD--------TKEILERLQFLLN----FLDLPS-------EKRLVknLSGGQQRR 185
Cdd:PRK10789 383 -QLDSWRSRLAVvSQTPFLFSDTVANNialgrpdaTQQEIEHVARLASvhddILRLPQgydtevgERGVM--LSGGQKQR 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 186 VSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
62-273 |
7.00e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG-RRYMD-AGEIFvLGGKP----GTRGSGVPGKRVGYmpQEIALYGEF 135
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEII-FEGEElqasNIRDTERAGIAIIH--QELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETM------MYFGWifgMDTKEILERLQFLLNFLDL---PSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTV 206
Cdd:PRK13549 98 SVLENIflgneiTPGGI---MDYDAMYLRAQKLLAQLKLdinPATP--VGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 207 gvdPLLRQSIwNHLVHIT---KAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEEsPSVLLSIYKCISL 273
Cdd:PRK13549 173 ---SLTESET-AVLLDIIrdlKAHGIACIYISHKLNEvKAISDTICVIRDGRHIGTR-PAAGMTEDDIITM 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
63-209 |
7.23e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 63 NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKR-VGYMPQ---EIALYGEFSIQ 138
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITEsrrDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 139 ETMMY--------FGWIFGM----DTKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTV 206
Cdd:PRK09700 360 QNMAIsrslkdggYKGAMGLfhevDEQRTAENQRELLA-LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
...
gi 318068885 207 GVD 209
Cdd:PRK09700 439 GID 441
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
62-205 |
7.89e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIY-----GLLGASGCGKTTLLScivgrryMDAGEIfvlggKPgTRGSGVPGKRVGYMPQEIALYGEFS 136
Cdd:PRK13409 350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAK-------LLAGVL-----KP-DEGEVDPELKISYKPQYIKPDYDGT 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318068885 137 IQETMMYFGWIFG--MDTKEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:PRK13409 417 VEDLLRSITDDLGssYYKSEIIKPLQ-LERLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
56-266 |
8.93e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 56 KNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG--------RRYMDAGEIfVLGGKPGTRgsgVPGKRVG---- 123
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDV-TLNGEPLAA---IDAPRLArlra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMPQEIALYGEFSIQETMM-------YFGWIFGMDTKEILERLQFLLNFLDLpsEKRLVKNLSGGQQRRVSFAVAL---- 192
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIVLlgryphaRRAGALTHRDGEIAWQALALAGATAL--VGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 193 -----MHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
61-266 |
9.34e-10 |
|
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: 62.04 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgSGVP---------GKRVGYMPQEIAL 131
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL---------DGHDladytlaslRRQVALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YGEfSIQETMMYfGWIFGMDTKEILERLQ--FLLNFLD-LPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:TIGR02203 418 FND-TIANNIAY-GRTEQADRAEIERALAaaYAQDFVDkLPLGLDTPigengVLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 204 PTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-262 |
1.08e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSC-------IVGRRYmdAGEIfVLGGKP--GTRGSGVPGKRVGYMPQEIAL 131
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDV-LLGGRSifNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YgEFSIQETMMYfgwifGMDTKEILERLQFL------LNFLDL--PSEKRLVKN---LSGGQQRRVSFAVALMHDPELLI 200
Cdd:PRK14271 113 F-PMSIMDNVLA-----GVRAHKLVPRKEFRgvaqarLTEVGLwdAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318068885 201 LDEPTVGVDPLLRQSIWNHLVHItkAGQKTVIITTHYI-EEARQAHTIGLMRSGHLLaEESPS 262
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLaQAARISDRAALFFDGRLV-EEGPT 246
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
60-237 |
1.28e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.31 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR-RY-MDAGEIFVLGgkpgtrgsgvpgKRVGYM-PQEIALYGEF- 135
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKYeVTSGSILLDG------------EDILELsPDERARAGIFl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQE-------TMMYF-----GWIFG--MDTKEILERLQFLLNFLDLPSE--KRLV-KNLSGGQQRRVSFAVALMHDPEL 198
Cdd:COG0396 82 AFQYpveipgvSVSNFlrtalNARRGeeLSAREFLKLLKEKMKELGLDEDflDRYVnEGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 199 LILDEPTVGVDpllrqsIW---------NHLvhitKAGQKTVIITTHY 237
Cdd:COG0396 162 AILDETDSGLD------IDalrivaegvNKL----RSPDRGILIITHY 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
57-204 |
2.05e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTV----PKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGK---PGTRGSGVP--GKRVGYMPQ 127
Cdd:PRK11144 5 NFKQQLGDLCLTVnltlPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRvlfDAEKGICLPpeKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 EIALYGEFSIQETMMYfgwifGMDTKEileRLQF--LLNFLDL-PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEP 204
Cdd:PRK11144 84 DARLFPHYKVRGNLRY-----GMAKSM---VAQFdkIVALLGIePLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
62-203 |
2.96e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.29 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTR-GSGVPGKRVGYmpQEIALYGefsiqeT 140
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAiSSGLNGQLTGI--ENIELKG------L 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 141 MMyfgwifGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDE 203
Cdd:PRK13545 112 MM------GLTKEKIKEIIPEIIEFADIGKfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
62-205 |
3.01e-09 |
|
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: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIY-----GLLGASGCGKTTLLScivgrryMDAGEIfvlggKPgTRGSGVPGKRVGYMPQEIalygEFS 136
Cdd:COG1245 351 YGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAK-------ILAGVL-----KP-DEGEVDEDLKISYKPQYI----SPD 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 137 IQETMMYFgwIFGMDTK---------EILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:COG1245 414 YDGTVEEF--LRSANTDdfgssyyktEIIKPLG-LEKLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
178-255 |
4.61e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 4.61e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 178 LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHL 255
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
45-209 |
5.15e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 45 VRHaFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR---RYmdAGEIFVLGGKPGTRGsgvpgkr 121
Cdd:PRK13549 262 VRN-LTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAypgRW--EGEIFIDGKPVKIRN------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 vgymPQEIALYGEFSIQETMMYFGWIFGMDTKE-----ILERLQFLlNFLDLPSE--------KRL----------VKNL 178
Cdd:PRK13549 332 ----PQQAIAQGIAMVPEDRKRDGIVPVMGVGKnitlaALDRFTGG-SRIDDAAElktilesiQRLkvktaspelaIARL 406
|
170 180 190
....*....|....*....|....*....|.
gi 318068885 179 SGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
38-266 |
1.52e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 38 NTQAAVSVRHAFKAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKT-TLLSCIvgrRYMDAGEIFVLGGKPGTRGS- 115
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL---RLLPSPPVVYPSGDIRFHGEs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 116 ----------GVPGKRVGYMPQE--IALYGEFSIqETMMY--FGWIFGMDTK----EI---LERL---QFLLNFLDLPSE 171
Cdd:PRK15134 78 llhaseqtlrGVRGNKIAMIFQEpmVSLNPLHTL-EKQLYevLSLHRGMRREaargEIlncLDRVgirQAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 172 krlvknLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLM 250
Cdd:PRK15134 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVM 230
|
250
....*....|....*.
gi 318068885 251 RSGHLLAEESPSVLLS 266
Cdd:PRK15134 231 QNGRCVEQNRAATLFS 246
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
50-236 |
3.43e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 50 KAYGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR---YMDaGEIfvlggkpgtRGSGVPGKR----- 121
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtggYIE-GDI---------RISGFPKKQetfar 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 122 -VGYMPQEIALYGEFSIQETMMYFGwiFGMDTKEIL--ERLQFLLNFLDLPSEKRL---------VKNLSGGQQRRVSFA 189
Cdd:PLN03140 954 iSGYCEQNDIHSPQVTVRESLIYSA--FLRLPKEVSkeEKMMFVDEVMELVELDNLkdaivglpgVTGLSTEQRKRLTIA 1031
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 318068885 190 VALMHDPELLILDEPTVGVDPlLRQSIWNHLVHITKAGQKTVIITTH 236
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDA-RAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
65-261 |
4.02e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 65 LNMTVPKGTIYGLLGASGCGKTTLLSCIVGRrYMDAGEIFvLGGKPGTRGSGVP-GKRVGY----------MP--QEIAL 131
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQ-FAGQPLEAWSAAElARHRAYlsqqqtppfaMPvfQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YGEFSIQETmmyfgwifgmDTKEILERLQFLLNFLD-LPsekRLVKNLSGGQQRRVSFA-VALMHDPE------LLILDE 203
Cdd:PRK03695 93 HQPDKTRTE----------AVASALNEVAEALGLDDkLG---RSVNQLSGGEWQRVRLAaVVLQVWPDinpagqLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 318068885 204 PTVGVDpLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSGHLLAEESP 261
Cdd:PRK03695 160 PMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRR 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
60-209 |
4.11e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMD--AGEIFvLGGKPgTRGSGVP---GKRVGYMPQEIALYG- 133
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVF-KDGKE-VDVSTVSdaiDAGLAYVTEDRKGYGl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 134 --EFSIQETMMY--------FGWIfgMDTKEIL--ERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:NF040905 352 nlIDDIKRNITLanlgkvsrRGVI--DENEEIKvaEEYRKKMN-IKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
....*...
gi 318068885 202 DEPTVGVD 209
Cdd:NF040905 429 DEPTRGID 436
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-238 |
4.13e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 23 PNAVAAWGAPA-NGPRNTQAAVSVRHAFKAYGKKKNANQV-----LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRR 96
Cdd:PTZ00243 631 PSSASRHIVEGgTGGGHEATPTSERSAKTPKMKTDDFFELepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 97 YMDAGEIFVlggkpgtrgsgvpGKRVGYMPQEiALYGEFSIQETMMYFgwifgmdTKEILERLQFLLNFLDLPSEKRLVK 176
Cdd:PTZ00243 711 EISEGRVWA-------------ERSIAYVPQQ-AWIMNATVRGNILFF-------DEEDAARLADAVRVSQLEADLAQLG 769
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 177 ------------NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGqKTVIITTHYI 238
Cdd:PTZ00243 770 ggleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG-KTRVLATHQV 842
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
59-239 |
4.51e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL------- 131
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIfsgtfrk 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 ----YGEFSIQETmmyfgWIFGMDT--KEILERLQFLLNFLdlpsekrLVKN---LSGGQQRRVSFAVALMHDPELLILD 202
Cdd:TIGR01271 1311 nldpYEQWSDEEI-----WKVAEEVglKSVIEQFPDKLDFV-------LVDGgyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|....*..
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHitKAGQKTVIITTHYIE 239
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVE 1413
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
53-205 |
5.11e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.23 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 53 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLlscivGR---RYMDA-GEIFVLGgkpgTRGSGVPGKRVGYMPQE 128
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL-----GLallRLIPSeGEIRFDG----QDLDGLSRRALRPLRRR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 IAL-----YGEFS--------IQETMMYFGwiFGMDTKEILERLQFLLNFLDLPSEKRlvkN-----LSGGQQRRVSFAV 190
Cdd:COG4172 364 MQVvfqdpFGSLSprmtvgqiIAEGLRVHG--PGLSAAERRARVAEALEEVGLDPAAR---HrypheFSGGQRQRIAIAR 438
|
170
....*....|....*
gi 318068885 191 ALMHDPELLILDEPT 205
Cdd:COG4172 439 ALILEPKLLVLDEPT 453
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
57-237 |
5.43e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDageifVLGGKPGTRGSGVPGKRvgymPQEIALYGEF- 135
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK-----ILEGDILFKGESILDLE----PEERAHLGIFl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQetmmYFGWIFGMDTKEILE-----RLQFL-------LNFLDLPSEK-RLVK------------NLSGGQQRRVSFAV 190
Cdd:CHL00131 89 AFQ----YPIEIPGVSNADFLRlaynsKRKFQglpeldpLEFLEIINEKlKLVGmdpsflsrnvneGFSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 318068885 191 ALMHDPELLILDEPTVGVDPLLRQSIwNHLVHITKAGQKTVIITTHY 237
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKII-AEGINKLMTSENSIILITHY 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
40-253 |
7.36e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 40 QAAVSVRHAFKAYgKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtRGSgvpg 119
Cdd:PLN03130 612 LPAISIKNGYFSW-DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI------RGT---- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 120 krVGYMPQeIALYGEFSIQETMMyFGWIFGMDTKEILERLQFLLNFLDLPSEKRLVK------NLSGGQQRRVSFAVALM 193
Cdd:PLN03130 681 --VAYVPQ-VSWIFNATVRDNIL-FGSPFDPERYERAIDVTALQHDLDLLPGGDLTEigergvNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 194 HDPELLILDEPTVGVDPLLRQSIWNHLVHiTKAGQKTVIITTHYIEEARQAHTIGLMRSG 253
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
57-239 |
7.80e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 53.65 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgSGVPGKRVGymPQEiaLYGEFS 136
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI---------DGVDISKIG--LHD--LRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 137 I--QETMMYFGWI------FGMDTKE----ILERLQFLLNFLDLPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELL 199
Cdd:cd03244 82 IipQDPVLFSGTIrsnldpFGEYSDEelwqALERVGLKEFVESLPGGLDTVveeggENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 318068885 200 ILDEPTVGVDP----LLRQSIWNHLVHitkagqKTVIITTHYIE 239
Cdd:cd03244 162 VLDEATASVDPetdaLIQKTIREAFKD------CTVLTIAHRLD 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
178-368 |
8.24e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 178 LSGGQQRRVSFAVALMHDPELLILDEPTVGVD---PLLRQSIWNHLvhitKAGQ-KTVIITTHYIEEARQAHTIGLMRSg 253
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVQKTINNL----KGNEnRITIIIAHRLSTIRYANTIFVLSN- 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 254 hllAEESPSVLLSIykcisLEEVFLKLSRIQSQKGDVTHVNFSKMDKPSSSQEGG--VVGLNFHQSkevLINDSNGSIYT 331
Cdd:PTZ00265 655 ---RERGSTVDVDI-----IGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGsyIIEQGTHDA---LMKNKNGIYYT 723
|
170 180 190
....*....|....*....|....*....|....*...
gi 318068885 332 L-NQEPYSPPPSrrNNNPNDEEScqDCYSNLCKITSKG 368
Cdd:PTZ00265 724 MiNNQKVSSKKS--SNNDNDKDS--DMKSSAYKDSERG 757
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
176-269 |
1.23e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 176 KNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTI-------- 247
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIvvfnnpdr 1436
|
90 100
....*....|....*....|...
gi 318068885 248 -GLMRSGHLLAEESPSVLLSIYK 269
Cdd:PTZ00265 1437 tGSFVQAHGTHEELLSVQDGVYK 1459
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
62-205 |
1.78e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG----RRYmdAGEIfVLGGKP----GTRGSgvpgKRVGY--MPQEIAL 131
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphGSY--EGEI-LFDGEVcrfkDIRDS----EALGIviIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 YGEFSIQETMMY------FGWIfgmDTKEILERLQFLLNFLDLP-SEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEP 204
Cdd:NF040905 90 IPYLSIAENIFLgnerakRGVI---DWNETNRRARELLAKVGLDeSPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
.
gi 318068885 205 T 205
Cdd:NF040905 167 T 167
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
62-255 |
1.85e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlGGKPGTrgsgvPGKRVGYMPQEIALYGEFSIQETM 141
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVT-----AEQPEDYRKLFSAVFTDFHLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 M-----------YFGWifgmdtkeiLERLQfLLNFLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:PRK10522 413 LgpegkpanpalVEKW---------LERLK-MAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318068885 211 LLRQSIWNHLVHITKAGQKTVIITTH---YIEearQAHTIGLMRSGHL 255
Cdd:PRK10522 483 HFRREFYQVLLPLLQEMGKTIFAISHddhYFI---HADRLLEMRNGQL 527
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-253 |
2.39e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 30 GAPANGPRNTQAAVSVRHAFKAYGKKK-------NANQVLNNLNMTVPKGTIYGLLGASGCGKTT----LLSCIVGRrym 98
Cdd:PRK15134 263 GDPVPLPEPASPLLDVEQLQVAFPIRKgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ--- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 99 daGEIfVLGGKP---GTRGSGVPGKR---VGYMPQEIALYGEFSIQETMmyfgwifgmdtKEILERLQFLLNF------- 165
Cdd:PRK15134 340 --GEI-WFDGQPlhnLNRRQLLPVRHriqVVFQDPNSSLNPRLNVLQII-----------EEGLRVHQPTLSAaqreqqv 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 166 --------LDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHY 237
Cdd:PRK15134 406 iavmeevgLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
250
....*....|....*..
gi 318068885 238 IEEARQ-AHTIGLMRSG 253
Cdd:PRK15134 486 LHVVRAlCHQVIVLRQG 502
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
43-284 |
2.93e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.87 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 43 VSVRHAFKAY-GKKKNAnqvLNNLNMTVPKGTIYGLLGASGCGKTTLLScIVGRRY-MDAGEIFVLGgkPGTRGSGVPGK 120
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPA---LRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYdIDEGEILLDG--HDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 121 R--VGYMPQEIALY-------------GEFSIQE-----TMMYfgwifGMDTKEILErlqfllNFLDLPSEKRLVkNLSG 180
Cdd:PRK11176 416 RnqVALVSQNVHLFndtianniayartEQYSREQieeaaRMAY-----AMDFINKMD------NGLDTVIGENGV-LLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 181 GQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKagQKTVIITTHYIEEARQAHTIGLMRSGHLLAEES 260
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGT 561
|
250 260
....*....|....*....|....
gi 318068885 261 PSVLLsiykciSLEEVFLKLSRIQ 284
Cdd:PRK11176 562 HAELL------AQNGVYAQLHKMQ 579
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
57-210 |
3.85e-07 |
|
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: 50.62 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfvlgGKPgtrgsgvPGKRVGYMPQEialygefs 136
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMP-------EGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 137 iqeTMMYFGwifgmdT-KEILERlqfllnfldlPSEKRLvknlSGGQQRRVSFAVALMHDPELLILDEPTVGVDP 210
Cdd:cd03223 73 ---PYLPLG------TlREQLIY----------PWDDVL----SGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
59-266 |
4.12e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.16 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDaGEIFVLGGKPGTRGSGVPGKRVGYMPQEIAL------- 131
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIfsgtfrk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 ----YGEFSIQETmmyfgWIFGMDT--KEILERLQFLLNFLdlpsekrLVKN---LSGGQQRRVSFAVALMHDPELLILD 202
Cdd:cd03289 96 nldpYGKWSDEEI-----WKVAEEVglKSVIEQFPGQLDFV-------LVDGgcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318068885 203 EPTVGVDPLLRQSIWNHLVHitKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
62-258 |
4.23e-07 |
|
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: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGR---RYmdAGEIFVLGGKPGTRGSG---------VPG--KRVGYMPQ 127
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAypgKF--EGNVFINGKPVDIRNPAqairagiamVPEdrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 eIALYGEFSIQETMMYFGWIFGMDTKEI------LERLQFLLNFLDLPsekrlVKNLSGGQQRRVSFAVALMHDPELLIL 201
Cdd:TIGR02633 354 -LGVGKNITLSVLKSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLP-----IGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 202 DEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 258
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
58-220 |
4.32e-07 |
|
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: 53.60 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 58 ANQVL-NNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgrrymdaGEIFVLGGkpGTRGSGVPGKrVGYMPQEiALYGEFS 136
Cdd:TIGR00954 463 NGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELWPVYG--GRLTKPAKGK-LFYVPQR-PYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 137 IQETMMYFGWIFGM--------DTKEILERLQfLLNFLDLPSEKRLVKN----LSGGQQRRVSFAVALMHDPELLILDEP 204
Cdd:TIGR00954 531 LRDQIIYPDSSEDMkrrglsdkDLEQILDNVQ-LTHILEREGGWSAVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170
....*....|....*.
gi 318068885 205 TVGVDPLLRQSIWNHL 220
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLC 625
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
71-247 |
5.34e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.68 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 71 KGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLggkpgtrgsgvpgkrvgympqeialygefsiqetmmyfgwifgm 150
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 151 DTKEILERLQFLLNFLDLPSEKrlvKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDP-----LLRQSIWNHLVHITK 225
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKK---ASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLLLLKS 113
|
170 180
....*....|....*....|..
gi 318068885 226 AGQKTVIITTHYIEEARQAHTI 247
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLR 135
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
66-258 |
5.93e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 66 NMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYM--PQE------IALYgefSI 137
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-YLDGKPIDIRSPRDAIRAGIMlcPEDrkaegiIPVH---SV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QETM--------MYFGWIF-GMDTKEILERLQFLLNfLDLPSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:PRK11288 349 ADNInisarrhhLRAGCLInNRWEAENADRFIRSLN-IKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 318068885 209 DPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAE 258
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
53-255 |
8.09e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 53 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTlLSCIVGrrymdageifvlGGKPGTRGSGVPGKRVGYMPQEIALY 132
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKST-LSNIIG------------GSLSPTVGKVDRNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 133 GEFSIQETMMYFGWIFGMDTKEILERLQFLLNFLDLPS-EKRLVKNLSGGQQRRVSFAVALMHDPELLILDEP-TVGVDP 210
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 318068885 211 LLRQSIwnHLVHITKAGQKTVIITTHYIEEARQAHT-IGLMRSGHL 255
Cdd:PRK13546 178 FAQKCL--DKIYEFKEQNKTIFFVSHNLGQVRQFCTkIAWIEGGKL 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
59-237 |
8.29e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRymdagEIFVLGGKPGTRGSGV----PGKRVG---YM----PQ 127
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-----DYEVTGGTVEFKGKDLlelsPEDRAGegiFMafqyPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 EIA-----LYGEFSIQETMMYFGwifgmdtKEILERLQFL------LNFLDLPSE--KRLVK-NLSGGQQRRVSFAVALM 193
Cdd:PRK09580 89 EIPgvsnqFFLQTALNAVRSYRG-------QEPLDRFDFQdlmeekIALLKMPEDllTRSVNvGFSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 318068885 194 HDPELLILDEPTVGVDpLLRQSIWNHLVHITKAGQKTVIITTHY 237
Cdd:PRK09580 162 LEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
52-302 |
1.09e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 52 YGKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---------------------------RRYMDAGEIF 104
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrvmaeklefngqdlqrisekeRRNLVGAEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 105 VLGGKPGTrgSGVPGKRVGYmpqeialygefSIQETMMYFGwifGMDTKEILERLQFLLNFLDLPS-EKRL---VKNLSG 180
Cdd:PRK11022 93 MIFQDPMT--SLNPCYTVGF-----------QIMEAIKVHQ---GGNKKTRRQRAIDLLNQVGIPDpASRLdvyPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 181 GQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHLLaEE 259
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVV-ET 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 260 SPSVllSIYKC----------ISLEEVFLKLSRIQSQKGDVThvnfSKMDKPS 302
Cdd:PRK11022 236 GKAH--DIFRAprhpytqallRALPEFAQDKARLASLPGVVP----GKYDRPN 282
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
61-236 |
1.70e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGKRVGYMPQ---EIALYG--EF 135
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF----PGNWQLAWVNQETPALPQpalEYVIDGdrEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 136 SIQETMM--------------YFGWIFGMDTKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELL 199
Cdd:PRK10636 92 RQLEAQLhdanerndghaiatIHGKLDAIDAWTIRSRAASLLHGLGFSNEQleRPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 318068885 200 ILDEPTVGVDplLRQSIWnhLVHITKAGQKTVIITTH 236
Cdd:PRK10636 172 LLDEPTNHLD--LDAVIW--LEKWLKSYQGTLILISH 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
62-235 |
2.08e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKPGTRGSGVPGKRVGYM-----PQEIALYGEFS 136
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI-TLHGKKINNHNANEAINHGFAlvteeRRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 137 IQETMM------YFGWIFGMDTKEILERLQFLLNFLDL--PSEKRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV 208
Cdd:PRK10982 343 IGFNSLisnirnYKNKVGLLDNSRMKSDTQWVIDSMRVktPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180
....*....|....*....|....*..
gi 318068885 209 DPLLRQSIWNHLVHITKAGQKTVIITT 235
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISS 449
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
60-209 |
2.23e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 48.95 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVgrRYMDA--GEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEfSI 137
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALF--RFLEAeeGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318068885 138 QETMMYFGwifGMDTKEILERLQFllnfldlpSEKRLvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:cd03369 99 RSNLDPFD---EYSDEEIYGALRV--------SEGGL--NLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
145-220 |
2.64e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318068885 145 GWIFGMDTKEILERLqfllnflDLPSEKRLvKNLSGGQQRRVSFAVALMHDPELLILDEPTvgvdpllrqsiwNHL 220
Cdd:PRK11147 132 LWQLENRINEVLAQL-------GLDPDAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPT------------NHL 187
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
60-253 |
2.76e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG---RRYMDAGEIFVLGGKPGTRGSgvPGKRVGYMPQEIALYgefs 136
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkDNWHVTADRFRWNGIDLLKLS--PRERRKIIGREIAMI---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 137 IQETMMYfgwifgMD-TKEILERL-------QF-----------------LLNFLDLPSEKRLVKN----LSGGQQRRVS 187
Cdd:COG4170 95 FQEPSSC------LDpSAKIGDQLieaipswTFkgkwwqrfkwrkkraieLLHRVGIKDHKDIMNSypheLTEGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 188 FAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEE-ARQAHTIGLMRSG 253
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESiSQWADTITVLYCG 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
62-247 |
4.58e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTLLScivgrrymdagEIFVLGGKpgtrgsgvpgKRVGYMPQeialygEFSIQETM 141
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGK----------ARLISFLP------KFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 142 MyfgwifgmdtkeiLERLQFL----LNFLDLpseKRLVKNLSGGQQRRVSFAVALMHDPE--LLILDEPTVGVDPLLRQS 215
Cdd:cd03238 64 F-------------IDQLQFLidvgLGYLTL---GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|..
gi 318068885 216 IWNHLVHITKAGQkTVIITTHYIEEARQAHTI 247
Cdd:cd03238 128 LLEVIKGLIDLGN-TVILIEHNLDVLSSADWI 158
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
63-236 |
5.15e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 63 NNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGrrymdageifVLGGKPGTRGSGV-PGKRVGYMPQ---------EIAL- 131
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMG----------LLAANGRIGGSATfNGREILNLPEkelnklraeQISMi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 132 ----------YGEFSIQ--ETMMYFGwifGMDTKEILERLQFLLNFLDLPSEKRLVK----NLSGGQQRRVSFAVALMHD 195
Cdd:PRK09473 103 fqdpmtslnpYMRVGEQlmEVLMLHK---GMSKAEAFEESVRMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 318068885 196 PELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTH 236
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
62-247 |
5.28e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 62 LNNLNMTVPKGTIYGLLGASGCGKTTL-LSCIVG---RRYMD-----AGEIFVLGGKPGT---------------RGSGV 117
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAegqRRYVEslsayARQFLGQMDKPDVdsieglspaiaidqkTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PGKRVGympqeialygefSIQETMMYFGWIFGMDTkeILERLQFLLNF-LDLPSEKRLVKNLSGGQQRRVSFAVALMHDP 196
Cdd:cd03270 91 PRSTVG------------TVTEIYDYLRLLFARVG--IRERLGFLVDVgLGYLTLSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318068885 197 E--LLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHTI 247
Cdd:cd03270 157 TgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHV 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
173-255 |
8.48e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 173 RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQAHTIGLMRS 252
Cdd:PRK10938 131 RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
...
gi 318068885 253 GHL 255
Cdd:PRK10938 211 CTL 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
59-249 |
1.15e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 59 NQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkPGTRGSGVPGKRVGYMPQEIALYGEFSIQ 138
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY----KNCNINNIAKPYCTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 139 ETMMYFGWIFgmDTKEILERLQFLLNFLDLPSEKrlVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWN 218
Cdd:PRK13541 89 ENLKFWSEIY--NSAETLYAAIHYFKLHDLLDEK--CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
170 180 190
....*....|....*....|....*....|.
gi 318068885 219 HLVHITKAGqKTVIITTHYIEEARQAHTIGL 249
Cdd:PRK13541 165 LIVMKANSG-GIVLLSSHLESSIKSAQILQL 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
53-234 |
1.60e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.49 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 53 GKKKNANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDA---GEIfVLGGKPGTRGSGVPGKRVGYMPQEI 129
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDI-HYNGIPYKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 130 ALYGEFSIQETMmYFgwifgmdtkeileRLQFLLNfldlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVD 209
Cdd:cd03233 93 VHFPTLTVRETL-DF-------------ALRCKGN--------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|....*
gi 318068885 210 PLLRQSIWNHLVHITKAGQKTVIIT 234
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFVS 175
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
64-255 |
1.68e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.00 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 64 NLNMTVPKGTIYGLLGASGCGKTtlLSCIV-------GRRYMdAGEIfVLGGKPgTRGSGVPGKRVGYMPQE-------- 128
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAalgilpaGVRQT-AGRV-LLDGKP-VAPCALRGRKIATIMQNprsafnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 --IALYGefsiQETMMYFGwifgmdtkeILERLQFLLNFLD---LPSEKRLVK----NLSGGQQRRVSFAVALMHDPELL 199
Cdd:PRK10418 96 htMHTHA----RETCLALG---------KPADDATLTAALEavgLENAARVLKlypfEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 200 ILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIE-EARQAHTIGLMRSGHL 255
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRI 219
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
579-761 |
3.58e-05 |
|
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: 46.23 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 579 FLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVVFGVT-------NNGDLFWVIV 651
Cdd:pfam12679 80 VIAALLGADAIAGERERGTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALAITlalgdplDLGDLLLLVA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 652 LTLLQG--MCGMCFGFLISSVCELERNAIQLALGSFYPTLLLSGVI-----------WPIEGMPVVLRYISlclPLTLAT 718
Cdd:pfam12679 160 ASVLLAlaLVFLSIGLLLSSVARSTRTAAAIALGLFFVLAILWPIVlyglaellagpAPPQELLDFLLFLN---PTSPYN 236
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 318068885 719 SSLRSILTRGWAILESDVYIGYVSTLSWIVGFLVLTLLVLRAK 761
Cdd:pfam12679 237 TLLSTILAGSDLSLYGSTATNLLILLAWIAVPLALAYVLFKRK 279
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
60-209 |
3.83e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.50 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTL---LSCI----VGRRYMDAGEifVLGGKPGTR---------------GSGV 117
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIetptGGELYYQGQD--LLKADPEAQkllrqkiqivfqnpyGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 118 PGKRVGYMPQEIALygefsIQETMmyfgwifgmDTKEILERLQFLLNFLDLPSE--KRLVKNLSGGQQRRVSFAVALMHD 195
Cdd:PRK11308 107 PRKKVGQILEEPLL-----INTSL---------SAAERREKALAMMAKVGLRPEhyDRYPHMFSGGQRQRIAIARALMLD 172
|
170
....*....|....
gi 318068885 196 PELLILDEPTVGVD 209
Cdd:PRK11308 173 PDVVVADEPVSALD 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
69-236 |
3.90e-05 |
|
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: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 69 VPKGTIYGLLGASGCGKTTLLSCIVGRRymdageifvlggKPGTRGSGVPGKRVGYMPQEIalygefsiqetmmyfgwif 148
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQL------------IPNGDNDEWDGITPVYKPQYI------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 149 gmdtkeilerlqfllnfldlpsekrlvkNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQ 228
Cdd:cd03222 71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
....*...
gi 318068885 229 KTVIITTH 236
Cdd:cd03222 123 KTALVVEH 130
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
69-205 |
5.17e-05 |
|
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: 46.70 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 69 VPK-GTIYGLLGASGCGKTTLLScIVgrrymdAGEIFV-LG--GKPGT--------RGSG--------VPGK-RVGYMPQ 127
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALK-IL------SGELKPnLGdyDEEPSwdevlkrfRGTElqdyfkklANGEiKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 128 EIALYGEF----------SIQETMMYfgwifgmdtKEILERLQfLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPE 197
Cdd:COG1245 168 YVDLIPKVfkgtvrelleKVDERGKL---------DELAEKLG-LENILD-----RDISELSGGELQRVAIAAALLRDAD 232
|
....*...
gi 318068885 198 LLILDEPT 205
Cdd:COG1245 233 FYFFDEPS 240
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
174-248 |
8.16e-05 |
|
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: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 174 LVKNLSGGQQRRV--SFAVALMHDPE--LLILDEPTVGVDPLLRQSIWNHLVHITKaGQKTVIITTHY---IEEARQAHT 246
Cdd:cd03227 74 TRLQLSGGEKELSalALILALASLKPrpLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLpelAELADKLIH 152
|
..
gi 318068885 247 IG 248
Cdd:cd03227 153 IK 154
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-236 |
9.67e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 153 KEILERLQFLLNF-LDLPSEKRLVKNLSGGQQRRVSFA-------VALMHdpellILDEPTVGVDPLLRQSIWNHLVHIT 224
Cdd:TIGR00630 463 KEIRERLGFLIDVgLDYLSLSRAAGTLSGGEAQRIRLAtqigsglTGVLY-----VLDEPSIGLHQRDNRRLINTLKRLR 537
|
90
....*....|..
gi 318068885 225 KAGQkTVIITTH 236
Cdd:TIGR00630 538 DLGN-TLIVVEH 548
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
60-236 |
1.01e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLscivgrRYMDAGEI-------FVLGGKPGTRGSGVPG---------KRVG 123
Cdd:PLN03073 191 DLIVDASVTLAFGRHYGLVGRNGTGKTTFL------RYMAMHAIdgipkncQILHVEQEVVGDDTTAlqcvlntdiERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 124 YMPQEIALYGEFSIQETMMYFGWiFGMDTK-------------EILERLQFL------------LNFLDLPSE--KRLVK 176
Cdd:PLN03073 265 LLEEEAQLVAQQRELEFETETGK-GKGANKdgvdkdavsqrleEIYKRLELIdaytaearaasiLAGLSFTPEmqVKATK 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 177 NLSGGQQRRVSFAVALMHDPELLILDEPTVGVDplLRQSIWNHlVHITKaGQKTVIITTH 236
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLE-TYLLK-WPKTFIVVSH 399
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
72-256 |
1.36e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 72 GTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIfVLGGKpgtRGSGVPGKRVGYMPQEIAL-----YGE--------FSIQ 138
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEI-IFNGQ---RIDTLSPGKLQALRRDIQFifqdpYASldprqtvgDSIM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 139 ETMMYFGWIFGmdtKEILERLQFLLNFLDLPSEK--RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSI 216
Cdd:PRK10261 426 EPLRVHGLLPG---KAAAARVAWLLERVGLLPEHawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 318068885 217 WNHLVHITKA-GQKTVIITTHYIEEARQAHTIGLMRSGHLL 256
Cdd:PRK10261 503 INLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
79-236 |
1.91e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 79 GASGCGKTTLLSCIvgrrymdageifvlggKPGTRGSGVPGKRVGYMPQEIALYGEFSIQETMMYfgWIFGMDTKEILER 158
Cdd:cd03240 29 GQNGAGKTTIIEAL----------------KYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAF--ENANGKKYTITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 159 LQFLLNFLDLPSEK------RLVKNLSGGQQR------RVSFAVALMHDPELLILDEPTVGVDpllRQSIWNHLVHITKA 226
Cdd:cd03240 91 LAILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEE 167
|
170
....*....|....
gi 318068885 227 --GQKT--VIITTH 236
Cdd:cd03240 168 rkSQKNfqLIVITH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-267 |
2.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 119 GKRvgYMPQ--EIALYGE--FSIQETMMYFGWIFGMDTKEILERLQFL----LNFLDLpseKRLVKNLSGGQQRRVSFAV 190
Cdd:PRK00635 748 GKR--FLPQvlEVRYKGKniADILEMTAYEAEKFFLDEPSIHEKIHALcslgLDYLPL---GRPLSSLSGGEIQRLKLAY 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 191 ALMH---DPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQkTVIITTHYIEEARQAHTI------GLMRSGHLLAEESP 261
Cdd:PRK00635 823 ELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVVKVADYVlelgpeGGNLGGYLLASCSP 901
|
....*.
gi 318068885 262 SVLLSI 267
Cdd:PRK00635 902 EELIHL 907
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
60-266 |
2.81e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 60 QVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVG-----------RRYMDagEIFVLGGKPGTRGSGVpGKRVGYMPQE 128
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadRMRFD--DIDLLRLSPRERRKLV-GHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 129 --IALYGEFSIQETMMYF--GWI--------FGMDTKEILErlqfLLNFLDLPSEKRLVKN----LSGGQQRRVSFAVAL 192
Cdd:PRK15093 98 pqSCLDPSERVGRQLMQNipGWTykgrwwqrFGWRKRRAIE----LLHRVGIKDHKDAMRSfpyeLTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 193 MHDPELLILDEPTVGVDPLLRQSIWNHLVHITKAGQKTVIITTHYIEEARQ-AHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
61-266 |
6.62e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYG---EFSI 137
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSgtvRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 138 QEtmmyFGWIFGMDTKEILERLQFL----LNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGV---- 208
Cdd:PLN03232 1331 DP----FSEHNDADLWEALERAHIKdvidRNPFGLDAEvSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVdvrt 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 209 DPLLRQSIWNHLVHItkagqkTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PLN03232 1407 DSLIQRTIREEFKSC------TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-205 |
6.95e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 6.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 318068885 154 EILERLqFLLNFLDlpsekRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT 205
Cdd:PRK13409 195 EVVERL-GLENILD-----RDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
57-266 |
1.07e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.43 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 57 NANQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVlggkpgtrgsgvPGKRVGYMPQEiALYGEFS 136
Cdd:cd03288 32 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI------------DGIDISKLPLH-TLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 137 I--QETMMYFGWI-FGMDTK---------EILERLQFLLNFLDLPSEKRLV-----KNLSGGQQRRVSFAVALMHDPELL 199
Cdd:cd03288 99 IilQDPILFSGSIrFNLDPEckctddrlwEALEIAQLKNMVKSLPGGLDAVvteggENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 318068885 200 ILDEPTVGVDpLLRQSIWNHLVhITKAGQKTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:cd03288 179 IMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-255 |
1.34e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 42.26 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 24 NAVAAWGAPANG--PRNTQAAVSVRHAFKAYGKKKnanQVLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIvgRRYMD-- 99
Cdd:PRK13657 314 DAVPDVRDPPGAidLGRVKGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDpq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 100 AGEIFVLGGKpgTRGSGVPGKR--VGYMPQEIALYGEfSIQETM-----------MYfgwifgmdtkEILERLQfLLNFL 166
Cdd:PRK13657 389 SGRILIDGTD--IRTVTRASLRrnIAVVFQDAGLFNR-SIEDNIrvgrpdatdeeMR----------AAAERAQ-AHDFI 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 167 dLPSEKRLVKN-------LSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHITKaGQKTVIItTHYIE 239
Cdd:PRK13657 455 -ERKPDGYDTVvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFII-AHRLS 531
|
250
....*....|....*.
gi 318068885 240 EARQAHTIGLMRSGHL 255
Cdd:PRK13657 532 TVRNADRILVFDNGRV 547
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
149-236 |
2.25e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 149 GMDTKEILERLQFLLNFLDLPSEK----RLVKNLSGGQQRRVSFAVALMHDPELLILDEPTVGVDPLLRQSIWNHLVHIT 224
Cdd:PRK10261 136 GASREEAMVEAKRMLDQVRIPEAQtilsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQ 215
|
90
....*....|..
gi 318068885 225 KAGQKTVIITTH 236
Cdd:PRK10261 216 KEMSMGVIFITH 227
|
|
| pip_yhgE_Cterm |
TIGR03062 |
YhgE/Pip C-terminal domain; This family contains the C-terminal domain of a family of multiple ... |
578-762 |
3.08e-03 |
|
YhgE/Pip C-terminal domain; This family contains the C-terminal domain of a family of multiple membrane-spanning proteins of Gram-positive bacteria. One member was shown to be a host protein essential for phage infection, so many members of this family are called "phage infection protein". A separate model, TIGR03061, represents the conserved N-terminal domain. The domains are separated by regions highly variable in both length and sequence, often containing extended heptad repeats as described in model TIGR03057.
Pssm-ID: 274414 [Multi-domain] Cd Length: 208 Bit Score: 39.86 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 578 FFLAVALTSSAL---IIERTegLLDRSWVAGVSPFEILFSHVITQFVVMCGQTTLVLIFMLVVFG--VTNNGDLFWVIVL 652
Cdd:TIGR03062 28 YFLSLALFVGALvlnLIFPP--LSRRALPKSARSWRIALAKLLPGGLIGVIQAIILYGVLILALGldPAHPPATFGFAIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 653 TllqgmcGMCFGFLISSVcelerNAIQLALGSFYPTLLL------SGVIWPIEGMPVVLRYISLCLPLTLATSSLRSILT 726
Cdd:TIGR03062 106 T------SLTFMAIIQFL-----VALFGSVGRFLALVLLvlqlgsSGGTFPIELLPAFFQAIHPFLPMTYSVNGLRQLIS 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 318068885 727 RG-WAILESDVYIgyvsTLSWIVGFLVLTLLVLRAKR 762
Cdd:TIGR03062 175 GGdDSTLWQAVAV----LLLILVIFLALSLLSARRKR 207
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
61-266 |
5.31e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 61 VLNNLNMTVPKGTIYGLLGASGCGKTTLLSCIVGRRYMDAGEIFVLGGKPGTRGSGVPGKRVGYMPQEIALYGEfSIQET 140
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 141 MMYFGWIFGMDTKEILERLQF----LLNFLDLPSE-KRLVKNLSGGQQRRVSFAVALMHDPELLILDEPT----VGVDPL 211
Cdd:PLN03130 1333 LDPFNEHNDADLWESLERAHLkdviRRNSLGLDAEvSEAGENFSVGQRQLLSLARALLRRSKILVLDEATaavdVRTDAL 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 318068885 212 LRQSIWNHLvhitKAGqkTVIITTHYIEEARQAHTIGLMRSGHLLAEESPSVLLS 266
Cdd:PLN03130 1413 IQKTIREEF----KSC--TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-210 |
5.53e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 5.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318068885 153 KEILE----RLQFLLNfLDLP--SEKRLVKNLSGGQQRRVSFAVALmhDPELL----ILDEPTVGVDP 210
Cdd:PRK00635 447 EEVLQglksRLSILID-LGLPylTPERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHP 511
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
571-762 |
7.53e-03 |
|
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: 38.26 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 571 GVILTIVFFLAVALTSSALIIERTEGLLDRSWVAGVSPFEILFSHVITQFVVmcgqttlVLIFMLVVFgvtnngdLFWVI 650
Cdd:COG1277 55 SLLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGKFLGALLV-------LLLALLITF-------LLALL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318068885 651 VLTLLQGMCGMCFGFLISsvcelernaiqlalgsFYPTLLLSGVIwpiegmpvvlrYISLCLPL-TLATSSLRSILTrgw 729
Cdd:COG1277 121 LGLLLFGSPPPDLGAILG----------------FYLGLLLLGLA-----------FLAIGLFIsALTRNQIVAAIL--- 170
|
170 180 190
....*....|....*....|....*....|...
gi 318068885 730 AILesdVYIGYVSTLSWIVGFLVLTLLVLRAKR 762
Cdd:COG1277 171 AIA---LWLLLVILLAWIVLFLALAYLRFKRRD 200
|
|
| |
