|
Name |
Accession |
Description |
Interval |
E-value |
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-341 |
6.30e-124 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 359.85 E-value: 6.30e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 2 IYV-DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkINISPKDRKI 77
Cdd:COG1118 3 IEVrNISKRFGSFTLLDDVSLEiasGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----TNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENIKVGIR-----EGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIIL 152
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRvrppsKAEI-RARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 153 LDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSSCLISGC 232
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 233 KNFSEIEKISDTklfAKDWDVELETSDKILETHKVLGIRSHFIEF--EKSEENSFEVEVDKVIEDVFTYIILVRKKGAIK 310
Cdd:COG1118 237 VNVLRGRVIGGQ---LEADGLTLPVAEPLPDGPAVAGVRPHDIEVsrEPEGENTFPATVARVSELGPEVRVELKLEDGEG 313
|
330 340 350
....*....|....*....|....*....|....*
gi 2646445281 311 S-IRVEVTKDIWE---KVEGQEhLFITLRKEDLIL 341
Cdd:COG1118 314 QpLEAEVTKEAWAelgLAPGDP-VYLRPRPARVFL 347
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-207 |
3.22e-91 |
|
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: 271.86 E-value: 3.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYVDIEKNFGKFNLRTKFEFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYL 80
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYALFPNMNVYENIKVGIREGENFDKLIM--EKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFS 158
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRKRNREDRISvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2646445281 159 ALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-344 |
1.57e-72 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.83 E-value: 1.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYVDIE---KNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD 74
Cdd:COG3842 3 MPALELEnvsKRYGDVTALDDVSLSiepGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------LPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 75 RKIGYLFQDYALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEI 150
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLRmrgvPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 151 ILLDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT-FSSCLI 229
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATrFVADFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 230 sGCKNF--SEIEKISDTKLFAKDWDVELETSDKILETHKV-LGIRSHFIEF-EKSEENSFEVEVDKViedVF---TYIIL 302
Cdd:COG3842 237 -GEANLlpGTVLGDEGGGVRTGGRTLEVPADAGLAAGGPVtVAIRPEDIRLsPEGPENGLPGTVEDV---VFlgsHVRYR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2646445281 303 VRKKGAiKSIRVEVTKDIWEKVEGQEHLFITLRKEDLILLEE 344
Cdd:COG3842 313 VRLGDG-QELVVRVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-207 |
1.06e-70 |
|
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: 219.31 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEF---DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKDRKIGYLF 81
Cdd:cd03259 5 GLSKTYGSVRALDDLSLtvePGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYALFPNMNVYENIKVGIREG----ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPF 157
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRgvpkAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 158 SALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-207 |
5.92e-67 |
|
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: 214.58 E-value: 5.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYVDIEKNFGKFNLRTKFEF-DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGY 79
Cdd:COG4148 2 MLEVDFRLRRGGFTLDVDFTLpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 80 LFQDYALFPNMNVYENIKVGIR------EGENFDKLImeklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILL 153
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKrapraeRRISFDEVV----ELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 154 DEPFSALDDYLKWKIeLEVGEVLRK-YKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG4148 158 DEPLAALDLARKAEI-LPYLERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-292 |
3.63e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 209.93 E-value: 3.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKF------NLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKDRKIG 78
Cdd:COG3839 8 NVSKSYGGVealkdiDLDIE---DGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD------LPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 79 YLFQDYALFPNMNVYENI----KV-GIREGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILL 153
Cdd:COG3839 79 MVFQSYALYPHMTVYENIafplKLrKVPKAEI-DRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 154 DEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK-TFSSCLI-SG 231
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAnLFVAGFIgSP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 232 CKNFSEIEkISDTKLFAKDWDVELETSDKILETHKV-LGIRSHFIEFEKSEENSFEVEVDKV 292
Cdd:COG3839 238 PMNLLPGT-VEGGGVRLGGVRLPLPAALAAAAGGEVtLGIRPEHLRLADEGDGGLEATVEVV 298
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-222 |
2.93e-61 |
|
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: 196.02 E-value: 2.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRT-KFEFDN-EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsEKKINISPKDRKIGYLFQ 82
Cdd:cd03299 5 NLSKDWKEFKLKNvSLEVERgDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG------KDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 83 DYALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFS 158
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKkrkvDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 159 ALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-231 |
1.44e-58 |
|
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: 193.02 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 2 IYVDIEKNFGKFNLRTKFEFD-NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYL 80
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPgQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYALFPNMNVYENIKVGIR------EGENFDKLImeklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKrarpseRRISFERVI----ELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 155 EPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK------SEELMKKKELFKNPKTFSSCL 228
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRvaaagpIAEVWASPDLPWLAREDQGSL 236
|
...
gi 2646445281 229 ISG 231
Cdd:TIGR02142 237 IEG 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-211 |
1.44e-55 |
|
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: 180.53 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYVDIEKNFGKFNLRTKFEF---DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKDRKI 77
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLdiaDGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD------LPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENI----KVGIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILL 153
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIafglKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 154 DEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEEL 211
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-223 |
5.59e-55 |
|
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: 179.74 E-value: 5.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 6 IEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDRKIGYLFQ 82
Cdd:cd03300 6 VSKFYGGFVALDGVSLDikeGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI------TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 83 DYALFPNMNVYENIKVGIREGENFDKLIMEKLEEM----RISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFS 158
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEAldlvQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 159 ALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-207 |
3.89e-53 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 178.53 E-value: 3.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYVDIEKNFGKFNLRTKFEF-DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGY 79
Cdd:PRK11144 1 MLELNFKQQLGDLCLTVNLTLpAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 80 LFQDYALFPNMNVYENIKVGIREG--ENFDKLImeklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPF 157
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGMAKSmvAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 158 SALDdyLKWKIEL--EVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK11144 157 ASLD--LPRKRELlpYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
22-206 |
4.58e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.97 E-value: 4.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinISPKDRKIGYLFQDYALFPNMNVYENIKVGIR 101
Cdd:COG1116 36 AGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP---------VTGPGPDRGVVFQEPALLPWLTVLDNVALGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 ----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLR 177
Cdd:COG1116 107 lrgvPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQ 186
|
170 180
....*....|....*....|....*....
gi 2646445281 178 KYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:COG1116 187 ETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-223 |
6.45e-52 |
|
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: 172.14 E-value: 6.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 4 VDIEKNFGKFNL--RTKFEFDN-EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfDSEKKiniSPKDRKIGYL 80
Cdd:cd03296 6 RNVSKRFGDFVAldDVSLDIPSgELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDV---PVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYALFPNMNVYENIKVGIRE--------GENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIIL 152
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVkprserppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 153 LDEPFSALDDylkwKIELEVGEVLRKYK----TPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:cd03296 160 LDEPFGALDA----KVRKELRRWLRRLHdelhVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-205 |
1.22e-51 |
|
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: 170.73 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinISPKDRKIGYLFQDYALFPNMNVYENIKVGIR 101
Cdd:cd03293 29 EGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---------VTGPGPDRGYVFQQDALLPWLTVLDNVALGLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGENFDKLIMEK----LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLR 177
Cdd:cd03293 100 LQGVPKAEARERaeelLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWR 179
|
170 180
....*....|....*....|....*...
gi 2646445281 178 KYKTPTILVSHSREEVYRLCKEICVMSK 205
Cdd:cd03293 180 ETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-207 |
3.59e-51 |
|
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: 168.13 E-value: 3.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKkiNISPKDRKIGYLF 81
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNieaGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED--ELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYALFPNMNVYENIkvgiregenfdklimekleemrishlkdkkIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03229 83 QDFALFPHLTVLENI------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 162 DYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-207 |
1.69e-50 |
|
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: 168.23 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFD-SEKKINisPKDRKIGYLFQDYALFPNMNVYENIKVGIRE 102
Cdd:COG1127 32 EILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELY--ELRRRIGMLFQGGALFDSLTVFENVAFPLRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 GENFDK-----LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLR 177
Cdd:COG1127 110 HTDLSEaeireLVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRD 189
|
170 180 190
....*....|....*....|....*....|
gi 2646445281 178 KYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG1127 190 ELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-222 |
1.26e-49 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 169.49 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYV-DIEKNFGKFNLRT-KFEF-DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDRKI 77
Cdd:NF040840 1 MIRIeNLSKDWKEFKLRDiSLEVkEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDI------TNLPPEKRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENIKVGIREGENFDKLIMEKLEEM----RISHLKDKKIYEISGGEKQRVALARLLINKPEIILL 153
Cdd:NF040840 75 AYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEImellGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 154 DEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:NF040840 155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPK 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-219 |
2.51e-47 |
|
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: 159.97 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFD-SEKKINisPKDRKIGYL 80
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDvrrGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELY--RLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYALFPNMNVYENIKVGIREGENF-----DKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDE 155
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTRLseeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 156 PFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFK 219
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-207 |
4.56e-47 |
|
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: 158.81 E-value: 4.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkiNISPKDR------KIGYLFQDYALFPNMNVYENIK 97
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS------KLSEKELaafrrrHIGFVFQSFNLLPDLTALENVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 V-----GIREGENFDKlIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEV 172
Cdd:cd03255 105 LplllaGVPKKERRER-AEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDS----ETGKEV 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646445281 173 GEVLRK----YKTPTILVSHSReEVYRLCKEICVMSKGK 207
Cdd:cd03255 180 MELLRElnkeAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-237 |
6.07e-47 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 163.08 E-value: 6.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKDRKIGYLFQDYALFPNMNVYENIKVGI 100
Cdd:PRK11607 43 YKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH------VPPYQRPINMMFQSYALFPHMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REgenfDKL----IMEKLEEM-RISHLKD---KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEV 172
Cdd:PRK11607 117 KQ----DKLpkaeIASRVNEMlGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 173 GEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSSCLISGCKNFSE 237
Cdd:PRK11607 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-207 |
1.82e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.51 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTK------FEFD-NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkiNISPKDR-- 75
Cdd:COG1136 9 NLTKSYGTGEGEVTalrgvsLSIEaGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS------SLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 76 ----KIGYLFQDYALFPNMNVYENIKV-----GIREGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLIN 146
Cdd:COG1136 83 lrrrHIGFVFQFFNLLPELTALENVALplllaGVSRKER-RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 147 KPEIILLDEPFSALDDylkwKIELEVGEVL----RKYKTPTILVSHSrEEVYRLCKEICVMSKGK 207
Cdd:COG1136 162 RPKLILADEPTGNLDS----KTGEEVLELLrelnRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-207 |
2.08e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.91 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYVD-IEKNFGKFNLRTKFEFD-NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKDRKIG 78
Cdd:COG3840 1 MLRLDdLTYRYGDFPLRFDLTIAaGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------LPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 79 YLFQDYALFPNMNVYENIKVGIREGENFD----KLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRPGLKLTaeqrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 155 EPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-222 |
2.12e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 158.96 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFG------KFNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDRKIG 78
Cdd:PRK09452 19 GISKSFDgkevisNLDLTIN---NGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------THVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 79 YLFQDYALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRmqktPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 155 EPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-219 |
6.51e-45 |
|
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: 153.64 E-value: 6.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNISPKD-----RKIGYLFQ--DYALFpNMNVYE 94
Cdd:COG1122 26 KGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK---------DITKKNlrelrRKVGLVFQnpDDQLF-APTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 95 NIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIEL 170
Cdd:COG1122 96 DVAFGPEnlglPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD--PRGRREL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 171 EvgEVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK------SEELMKKKELFK 219
Cdd:COG1122 174 L--ELLKRLNkegKTVIIVTHDLDLVAELADRVIVLDDGRivadgtPREVFSDYELLE 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-223 |
7.63e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 157.17 E-value: 7.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 6 IEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfDSEKkinISPKDRKIGYLFQ 82
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDipsGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSR---LHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 83 DYALFPNMNVYENIKVGI-----REGEN---FDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLtvlprRERPNaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 155 EPFSALDDylkwKIELEVGEVLRK----YKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:PRK10851 162 EPFGALDA----QVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-207 |
1.04e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLFQDYALFPNMNVYENIKV----- 98
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-----RRIGYVPQEPALYPDLTVRENLRFfarly 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkwkIEL--EVGEVL 176
Cdd:COG1131 102 GLPRKE-ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD------PEArrELWELL 174
|
170 180 190
....*....|....*....|....*....|....
gi 2646445281 177 RKYKTP--TILVS-HSREEVYRLCKEICVMSKGK 207
Cdd:COG1131 175 RELAAEgkTVLLStHYLEEAERLCDRVAIIDKGR 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
1.41e-44 |
|
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: 153.03 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYV-DIEKNFGKFNLRTK------FEFD-NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKinisP 72
Cdd:COG1124 1 MLEVrNLSVSYGQGGRRVPvlkdvsLEVApGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 73 KDRKIGYLFQDY--ALFPNMNVYENIKVGIREGENFDklIMEKLEEMRI-----SHLKDKKIYEISGGEKQRVALARLLI 145
Cdd:COG1124 77 FRRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPD--REERIAELLEqvglpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 146 NKPEIILLDEPFSALDDYLKWKIeLEVGEVLRK-YKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEI-LNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-188 |
2.11e-43 |
|
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: 149.22 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISpkDRKIGYLF 81
Cdd:cd03262 5 NLHKSFGDFHVLKGIDLTvkkGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL--RQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYALFPNMNVYENIKVGIREGENFDK-----LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEP 156
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPIKVKGMSKaeaeeRALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 2646445281 157 FSALDDylkwkiELeVGEVLR------KYKTPTILVSH 188
Cdd:cd03262 163 TSALDP------EL-VGEVLDvmkdlaEEGMTMVVVTH 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-222 |
1.98e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.91 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfDSEKKINISPKDRKIGYLFQD--YALFPNMNVYENIKVGIR 101
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL-TKLSRRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 -----EGENFDKLIMEKLEEMRIS-HLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKIELEVGEV 175
Cdd:COG1123 371 lhgllSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 176 LRKYKTPT----ILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:COG1123 447 LRDLQRELgltyLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
2.19e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.06 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYV-DIEKNFGKF------NLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispK 73
Cdd:COG1126 1 MIEIeNLHKSFGDLevlkgiSLDVE---KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN---K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 74 DR-KIGYLFQDYALFPNMNVYENI-----KVGIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINK 147
Cdd:COG1126 75 LRrKVGMVFQQFNLFPHLTVLENVtlapiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 148 PEIILLDEPFSALDDylkwkiELeVGEVLR------KYKTPTILVSHsrE-----EVyrlCKEICVMSKGKSEELMKKKE 216
Cdd:COG1126 155 PKVMLFDEPTSALDP------EL-VGEVLDvmrdlaKEGMTMVVVTH--EmgfarEV---ADRVVFMDGGRIVEEGPPEE 222
|
....*..
gi 2646445281 217 LFKNPKT 223
Cdd:COG1126 223 FFENPQH 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-207 |
9.43e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 9.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFPNMnVYENIK--V 98
Cdd:COG4619 26 GECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA------MPPPEwrRQVAYVPQEPALWGGT-VRDNLPfpF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIREgENFDKLIMEK-LEEMRISH-LKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:COG4619 99 QLRE-RKFDRERALElLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYL 177
|
170 180 190
....*....|....*....|....*....|.
gi 2646445281 177 RKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG4619 178 AEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-207 |
3.11e-41 |
|
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: 143.38 E-value: 3.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKInispKDRKIGYLFQ--DYALFpNMNVYENIKV 98
Cdd:cd03225 25 KKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVFQnpDDQFF-GPTVEEEVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKIELEVGE 174
Cdd:cd03225 100 GLEnlglPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD----PAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2646445281 175 VLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03225 176 LLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
22-207 |
7.56e-41 |
|
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: 143.65 E-value: 7.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFPNMNVYENIKVG 99
Cdd:COG1120 26 PGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS------LSRRElaRRIAYVPQEPPAPFGLTVRELVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 --------IREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIelE 171
Cdd:COG1120 100 ryphlglfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD--LAHQL--E 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 172 VGEVLRKY-----KTpTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG1120 176 VLELLRRLarergRT-VVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-207 |
7.98e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.50 E-value: 7.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKD-----RKIGYLFQDYALFPNMNVYENIK----- 97
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL------SRLKRREipylrRRIGVVFQDFRLLPDRTVYENVAlplrv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVLR 177
Cdd:COG2884 107 TGKSRKE-IRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEI-MELLEEIN 184
|
170 180 190
....*....|....*....|....*....|
gi 2646445281 178 KYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG2884 185 RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-158 |
8.43e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.09 E-value: 8.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKiniSPKdRKIGYLFQDYALFPNMNVYENIKVGIREG 103
Cdd:pfam00005 12 EILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK---SLR-KEIGYVFQDPQLFPRLTVRENLRLGLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 104 ENFDKLI---MEK-LEEMRISHLKDKKI----YEISGGEKQRVALARLLINKPEIILLDEPFS 158
Cdd:pfam00005 88 GLSKREKdarAEEaLEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-222 |
3.08e-40 |
|
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: 141.56 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKiNISPKDRKIGYLFQDYALFPNMNVYENI----KVG 99
Cdd:cd03258 32 EIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGK-ELRKARRRIGMIFQHFNLLSSRTVFENValplEIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD--------DYLKwKIELE 171
Cdd:cd03258 111 GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettqsilALLR-DINRE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 172 VGevlrkyktPTI-LVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:cd03258 190 LG--------LTIvLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
24-193 |
1.42e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 139.15 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPD---KGRIILNGRVLFDsekkinISPKDRKIGYLFQDYALFPNMNVYENIKVGI 100
Cdd:COG4136 28 EILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA------LPAEQRRIGILFQDDLLFPHLSVGENLAFAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 RE---GENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLR 177
Cdd:COG4136 102 PPtigRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIR 181
|
170
....*....|....*.
gi 2646445281 178 KYKTPTILVSHSREEV 193
Cdd:COG4136 182 QRGIPALLVTHDEEDA 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-223 |
4.74e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.78 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGK------FNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfDSEKKINISPKDRKIG 78
Cdd:PRK11432 11 NITKRFGSntvidnLNLTIK---QGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI------DGEDVTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 79 YLFQDYALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKmlgvPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 155 EPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-221 |
5.66e-39 |
|
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: 139.32 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQDYALFPNMNVYENIKVGIr 101
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGL- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGENFDKLI-----MEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:cd03294 128 EVQGVPRAEreeraAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2646445281 177 RKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:cd03294 208 AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-207 |
1.67e-38 |
|
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: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINiSPKDRKIGYLFQDY--ALFPNMNVYENIKVGIR 101
Cdd:cd03257 32 ETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KIRRKEIQMVFQDPmsSLNPRMTIGEQIAEPLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 ------EGENFDKLIMEKLEEMRIS-HLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGE 174
Cdd:cd03257 111 ihgklsKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKK 190
|
170 180 190
....*....|....*....|....*....|...
gi 2646445281 175 VLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03257 191 LQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-207 |
2.08e-38 |
|
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: 136.10 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLFQDYALFPNMNVYENIKV-- 98
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-----QSLGYCPQFDALFDELTVREHLRFya 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 ---GIREGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLK---WKIELEV 172
Cdd:cd03263 101 rlkGLPKSEI-KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRraiWDLILEV 179
|
170 180 190
....*....|....*....|....*....|....*
gi 2646445281 173 GEvlrkyKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03263 180 RK-----GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-207 |
1.46e-37 |
|
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: 132.52 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKF----NLRTKFEfDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYL 80
Cdd:cd03230 5 NLSKRYGKKtaldDISLTVE-KGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-----RRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYALFPNMNVYENIKVgiregenfdklimekleemrishlkdkkiyeiSGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:cd03230 79 PEEPSLYENLTVRENLKL--------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 161 DdylkWKIELEVGEVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03230 127 D----PESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-210 |
1.52e-37 |
|
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: 134.23 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEK-----PDKGRIILNGRVLFDseKKINISPKDRKIGYLFQDYALFPnMNVYENIK 97
Cdd:cd03260 26 GEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYD--LDVDVLELRRRVGMVFQKPNPFP-GSIYDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VG-----IREGENFDKLIMEKLEEMRIS-HLKDK-KIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIEl 170
Cdd:cd03260 103 YGlrlhgIKLKEELDERVEEALRKAALWdEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIE- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 171 evgEVLRKYKTPT--ILVSHSREEVYRLCKEICVMSKGKSEE 210
Cdd:cd03260 182 ---ELIAELKKEYtiVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-207 |
2.43e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.48 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQdyalfpnmnvyenikvgi 100
Cdd:cd03214 25 GEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------LSPKElaRKIAYVPQ------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 regenfdklimeKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIelEVGEVLRKY- 179
Cdd:cd03214 81 ------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD--IAHQI--ELLELLRRLa 144
|
170 180 190
....*....|....*....|....*....|..
gi 2646445281 180 ----KTpTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03214 145 rergKT-VVMVLHDLNLAARYADRVILLKDGR 175
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-207 |
2.64e-36 |
|
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: 131.52 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MIYV-DIEKNFGKFNLRTKFEF---DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRK 76
Cdd:COG4555 1 MIEVeNLSKKYGKVPALKDVSFtakDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-----RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 77 IGYLFQDYALFPNMNVYENIKVGIREGENFDKLIMEKLEE----MRISHLKDKKIYEISGGEKQRVALARLLINKPEIIL 152
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEElielLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 153 LDEPFSALDdylkWKIELEVGEVLRKYKTP--TILVS-HSREEVYRLCKEICVMSKGK 207
Cdd:COG4555 156 LDEPTNGLD----VMARRLLREILRALKKEgkTVLFSsHIMQEVEALCDRVVILHKGK 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-226 |
3.09e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.96 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEkPDKGRIilNGRVLFDSEKKINISPKDR--KIGYLFQD--YALFPnMNVYENIKVG 99
Cdd:COG1123 33 ETVALVGESGSGKSTLALALMGLL-PHGGRI--SGEVLLDGRDLLELSEALRgrRIGMVFQDpmTQLNP-VTVGDQIAEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IREG----ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEV 175
Cdd:COG1123 109 LENLglsrAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLREL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 176 LRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSS 226
Cdd:COG1123 189 QRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-222 |
5.73e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 133.62 E-value: 5.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 4 VDIEKNFgkfNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKpdkgriILNGRVLFDSEKKINISPKDRKIGYLFQD 83
Cdd:PRK11000 16 VVISKDI---NLDIH---EGEFVVFVGPSGCGKSTLLRMIAGLED------ITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 84 YALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKlagaKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 160 LDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
28-207 |
1.02e-35 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 128.91 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKiNISPKDRKIGYLFQDYALFPNMNVYENIKVGIR----EG 103
Cdd:TIGR02673 33 LTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGR-QLPLLRRRIGVVFQDFRLLPDRTVYENVALPLEvrgkKE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVLRKYKTPT 183
Cdd:TIGR02673 112 REIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERI-LDLLKRLNKRGTTV 190
|
170 180
....*....|....*....|....
gi 2646445281 184 ILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR02673 191 IVATHDLSLVDRVAHRVIILDDGR 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-220 |
5.48e-35 |
|
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: 135.35 E-value: 5.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSlTL-KCIAGIEKPDKGRIILNGRvlfDSEkkiNISPKD--RKIGYLFQDYALFpNMNVYENIKVGi 100
Cdd:COG2274 502 ERVAIVGRSGSGKS-TLlKLLLGLYEPTSGRILIDGI---DLR---QIDPASlrRQIGVVLQDVFLF-SGTIRENITLG- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 reGENFDkliMEKLEE-MRISHLKDK----------KIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDylk 165
Cdd:COG2274 573 --DPDAT---DEEIIEaARLAGLHDFiealpmgydtVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDA--- 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 166 wKIELEVGEVLRKYKTP--TILVSHsREEVYRLCKEICVMSKGK------SEELMKKKELFKN 220
Cdd:COG2274 645 -ETEAIILENLRRLLKGrtVIIIAH-RLSTIRLADRIIVLDKGRivedgtHEELLARKGLYAE 705
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-207 |
6.12e-35 |
|
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: 126.84 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEkkinisPKDRKIGYLFQDYALFPNMNVYENIKVGIREG 103
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP------PADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 ENF---DKLIMEK-LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKY 179
Cdd:cd03298 99 LKLtaeDRQAIEVaLARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180
....*....|....*....|....*...
gi 2646445281 180 KTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-200 |
7.83e-35 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 126.58 E-value: 7.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 4 VDIEKNFG------KFNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKI 77
Cdd:TIGR03608 2 KNISKKFGdkvildDLNLTIE---KGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENIKVGI----REGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILL 153
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLkykkLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646445281 154 DEPFSALDDYLKWKIeLEVGEVLRKYKTPTILVSHSrEEVYRLCKEI 200
Cdd:TIGR03608 159 DEPTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHD-PEVAKQADRV 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-221 |
2.31e-34 |
|
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: 126.26 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsekkINISPKD-----RKIGYLFQDYALFPNMNVYENI 96
Cdd:cd03295 26 KGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG---------EDIREQDpvelrRKIGYVIQQIGLFPHMTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 ----KVGIREGENFDKLIMEKLEEMRI--SHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIEL 170
Cdd:cd03295 97 alvpKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 171 EVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:cd03295 177 EFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-217 |
3.91e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNISPKDRKIGYLFQDYAL---FPnMNVYENIKVGI 100
Cdd:COG1121 33 EFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---------PPRRARRRIGYVPQRAEVdwdFP-ITVRDVVLMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGENF-------DK-LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIEL-E 171
Cdd:COG1121 103 YGRRGLfrrpsraDReAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD--AATEEALyE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 172 VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSK-----GKSEELMKKKEL 217
Cdd:COG1121 181 LLRELRREGKTILVVTHDLGAVREYFDRVLLLNRglvahGPPEEVLTPENL 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-206 |
9.05e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 125.36 E-value: 9.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkinISP-KDRkiGYLFQDYALFPNMNVYENIKVGI 100
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--------TGPgADR--GVVFQKDALLPWLNVLDNVAFGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 R-----EGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEV 175
Cdd:COG4525 102 RlrgvpKAER-RARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
170 180 190
....*....|....*....|....*....|.
gi 2646445281 176 LRKYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:COG4525 181 WQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
24-207 |
1.29e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.40 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKD-----RKIGYLFQDYALFPNMNVYENIKV 98
Cdd:COG3638 30 EFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV------TALRGRAlrrlrRRIGMIFQQFNLVPRLSVLTNVLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GiREGE---------NFDK----LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD---- 161
Cdd:COG3638 104 G-RLGRtstwrsllgLFPPedreRALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDpkta 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 162 ----DYLKwkielevgEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG3638 183 rqvmDLLR--------RIAREDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-222 |
2.58e-33 |
|
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: 124.49 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdSEKKINISPKDRKIGYLFQ--DYALFPNmNVYENIKVG 99
Cdd:TIGR04521 30 DGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDIT-AKKKKKLKDLRKKVGLVFQfpEHQLFEE-TVYKDIAFG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IRegeNF-------DKLIMEKLEEMRISH-LKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIEL- 170
Cdd:TIGR04521 108 PK---NLglseeeaEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD--PKGRKEIl 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 171 -EVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:TIGR04521 183 dLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-207 |
3.84e-33 |
|
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: 120.43 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQdyalfpnmnvyenikvgire 102
Cdd:cd00267 25 GEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI----AKLPLEELRRRIGYVPQ-------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 genfdklimekleemrishlkdkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKYKTp 182
Cdd:cd00267 81 ---------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT- 132
|
170 180
....*....|....*....|....*
gi 2646445281 183 TILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd00267 133 VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-226 |
3.98e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlFD-SEKKINISPKDRKIGYLFQ--DYALFPNmNVYENIKV 98
Cdd:PRK13637 32 DGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG---VDiTDKKVKLSDIRKKVGLVFQypEYQLFEE-TIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIRE-GENFDKLIMEKLEEMRI-----SHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEV 172
Cdd:PRK13637 108 GPINlGLSEEEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 173 GEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSS 226
Cdd:PRK13637 188 KELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-207 |
4.15e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.77 E-value: 4.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 12 KFNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsEKKINISPKDRKIGYLFQDYALFPNMN 91
Cdd:PRK10771 17 RFDLTVE---RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 92 VYENIKVGIREGENFDKLIMEKLEE----MRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWK 167
Cdd:PRK10771 88 VAQNIGLGLNPGLKLNAAQREKLHAiarqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2646445281 168 IELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-206 |
4.54e-33 |
|
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: 122.57 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekKINISPKDRKIgyLFQDYALFPNMNVYENIKVGI--- 100
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-------QITEPGPDRMV--VFQNYSLLPWLTVRENIALAVdrv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 ----REGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:TIGR01184 83 lpdlSKSER-RAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIW 161
|
170 180 190
....*....|....*....|....*....|
gi 2646445281 177 RKYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:TIGR01184 162 EEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-208 |
1.11e-32 |
|
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: 120.85 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINISPKDRkIGYLF 81
Cdd:cd03269 5 NVTKRFGRVTALDDISFSvekGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAARNR-IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYALFPNMNVYENIK-------VGIREGEnfdKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:cd03269 77 EERGLYPKMKVIDQLVylaqlkgLKKEEAR---RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 155 EPFSALDDYLKWKIELEVGEVLRKYKTpTILVSHSREEVYRLCKEICVMSKGKS 208
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-223 |
1.30e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 124.57 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEkkinisPKDRKIGYLFQDYALFPNMNVYENIKVG-- 99
Cdd:PRK11650 29 DGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE------PADRDIAMVFQNYALYPHMSVRENMAYGlk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IRegeNFDK-LIMEKLEE----MRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGE 174
Cdd:PRK11650 103 IR---GMPKaEIEERVAEaariLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2646445281 175 VLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:PRK11650 180 LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPAS 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-207 |
2.15e-32 |
|
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: 120.21 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKiNISPKDRKIGYLFQDYALFPNMNVYENIKVGIR-- 101
Cdd:cd03292 28 EFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR-AIPYLRRKIGVVFQDFRLLPDRNVYENVAFALEvt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 --EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVLRKY 179
Cdd:cd03292 107 gvPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKA 185
|
170 180
....*....|....*....|....*...
gi 2646445281 180 KTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03292 186 GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-161 |
3.63e-32 |
|
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: 120.37 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNG-RVLFDSEKKINiSPKdRKIGYLFQDYALFPNMNVYENIKVG--- 99
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtDINKLKGKALR-QLR-RQIGMIFQQFNLIERLSVLENVLSGrlg 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 100 ----IREGENF----DKLI-MEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03256 106 rrstWRSLFGLfpkeEKQRaLAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-207 |
6.59e-32 |
|
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: 117.48 E-value: 6.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFpNMNVYENIkvgire 102
Cdd:cd03228 28 GEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL----RDLDLESLRKNIAYVPQDPFLF-SGTIRENI------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 genfdklimekleemrishlkdkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKIELEVGEVLRKY--- 179
Cdd:cd03228 97 ---------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD----PETEALILEALRALakg 145
|
170 180
....*....|....*....|....*...
gi 2646445281 180 KTpTILVSHsREEVYRLCKEICVMSKGK 207
Cdd:cd03228 146 KT-VIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-207 |
8.62e-32 |
|
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: 118.62 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlFDSEKkiniSPKD--RKIGYLFQDYALFPNMNVYENIKVG 99
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVK----EPAEarRRLGFVSDSTGLYDRLTARENLEYF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALdDYLKWKIELEVGEV 175
Cdd:cd03266 103 AGlyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL-DVMATRALREFIRQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 2646445281 176 LRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03266 182 LRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-207 |
2.72e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 117.92 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGK--------FNLRtkfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDRK 76
Cdd:cd03219 5 GLTKRFGGlvalddvsFSVR-----PGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI------TGLPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 77 ---IGYLFQDYALFPNMNVYENIKVG--IREGENF------------DKLIMEKLEEMRISHLKDKKIYEISGGEKQRVA 139
Cdd:cd03219 74 rlgIGRTFQIPRLFPELTVLENVMVAaqARTGSGLllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 140 LARLLINKPEIILLDEPFSALDDYLKWkielEVGEVLRKYKTP--TIL-VSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETE----ELAELIRELRERgiTVLlVEHDMDVVMSLADRVTVLDQGR 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-161 |
7.40e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.67 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNIS--PKDRK----IGYLFQDYALFPNMNVYENIK 97
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---------DIThlPMHKRarlgIGYLPQEASIFRKLTVEDNIL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 98 vGIREGENFDK-LIMEK----LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG1137 101 -AVLELRKLSKkEREERleelLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-223 |
1.02e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKD-----RKIGYLFQDYALFPNMNVYENIK- 97
Cdd:PRK11153 32 EIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL------TALSEKElrkarRQIGMIFQHFNLLSSRTVFDNVAl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 ----VGIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD--------DYLK 165
Cdd:PRK11153 106 plelAGTPKAE-IKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpattrsilELLK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 166 wkielevgEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:PRK11153 185 --------DINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-206 |
1.10e-30 |
|
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: 115.71 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 19 FEFDN-EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNISPKDRKIGYLFQDYAL---FPnMNVYE 94
Cdd:cd03235 20 FEVKPgEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---------PLEKERKRIGYVPQRRSIdrdFP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 95 NIKVGIREGENF--------DKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKW 166
Cdd:cd03235 90 VVLMGLYGHKGLfrrlskadKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD--PKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 167 KIEL-EVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:cd03235 168 QEDIyELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-223 |
1.45e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 118.64 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSlTL-KCIAGIEKPDKGRIILNGRVLfdsekkINISPKD-----RKIGYLFQDYALFPNMNVYENI- 96
Cdd:COG1135 32 EIFGIIGYSGAGKS-TLiRCINLLERPTSGSVLVDGVDL------TALSERElraarRKIGMIFQHFNLLSSRTVAENVa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 ---KV-GIREGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD--------DYL 164
Cdd:COG1135 105 lplEIaGVPKAEI-RKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsilDLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 165 KwkielevgEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:COG1135 184 K--------DINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
24-161 |
2.10e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.88 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEkkiniSPKDRKIGYLFQDYALFPNMNVYENIKV--GIR 101
Cdd:COG4133 29 EALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-----EDYRRRLAYLGHADGLKPELTVRENLRFwaALY 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG4133 104 GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-207 |
2.21e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 114.62 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIilngrvLFDSEKKINISPKDRKIGYLF 81
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHvkkGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI------TFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYALFPNMNVYENIKVGIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646445281 162 -DYLKWKIELEVGevLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03268 159 pDGIKELRELILS--LRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-207 |
3.66e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNISPKDR-KIGYLFQDYALFPNMNVYENI------ 96
Cdd:COG4152 28 EIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---------PLDPEDRrRIGYLPEERGLYPKMKVGEQLvylarl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KvGIREGENfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD----DYLKwkielev 172
Cdd:COG4152 99 K-GLSKAEA-KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvnvELLK------- 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2646445281 173 gEVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG4152 170 -DVIRELAakgTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-161 |
5.79e-30 |
|
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: 114.18 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekKINISPKDRK----IGYLFQDYALFPNMNVYENIKVG 99
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ-------DITKLPMHKRarlgIGYLPQEASIFRKLTVEENILAV 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 100 IREGENFDKLIMEKLEEM----RISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03218 100 LEIRGLSKKEREEKLEELleefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-207 |
6.68e-30 |
|
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: 113.44 E-value: 6.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 19 FEFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLFQDYALFPNMNVYENIKV 98
Cdd:cd03264 21 LTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-----RRIGYLPQEFGVYPNFTVREFLDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 -----GIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylKWKIEL--- 170
Cdd:cd03264 96 iawlkGIPSKE-VKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP--EERIRFrnl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2646445281 171 --EVGEvlrkykTPTILVS-HSREEVYRLCKEICVMSKGK 207
Cdd:cd03264 173 lsELGE------DRIVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-165 |
7.81e-30 |
|
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: 114.32 E-value: 7.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFD-SEKKINISpkDRKIGYLFQDYALFPNMNVYENIKVG--- 99
Cdd:TIGR02315 29 EFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKL--RRRIGMIFQHYNLIERLTVLENVLHGrlg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 ----IREGENF----DKLI-MEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD--------D 162
Cdd:TIGR02315 107 ykptWRSLLGRfseeDKERaLSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDpktskqvmD 186
|
...
gi 2646445281 163 YLK 165
Cdd:TIGR02315 187 YLK 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-207 |
8.58e-30 |
|
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: 113.68 E-value: 8.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDR---KIGYLFQDYALFPNMNVYENIKVG 99
Cdd:cd03224 26 GEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI------TGLPPHERaraGIGYVPEGRRIFPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 --IREGENFDKLIME------KLEEMRishlkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELE 171
Cdd:cd03224 100 ayARRRAKRKARLERvyelfpRLKERR-----KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP----KIVEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 172 VGEVLRKYKTP--TILVShsrEEVYRLCKEI----CVMSKGK 207
Cdd:cd03224 171 IFEAIRELRDEgvTILLV---EQNARFALEIadraYVLERGR 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-222 |
7.26e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 113.61 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKP---DKGRIILNGRVLFDsekkinISPKD------RKIGYLFQD-Y-ALFPNMN 91
Cdd:COG0444 31 GETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK------LSEKElrkirgREIQMIFQDpMtSLNPVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 92 VYENIKVGIREGENFDK-----LIMEKLEEMRI----SHLKDkkiY--EISGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:COG0444 105 VGDQIAEPLRIHGGLSKaeareRAIELLERVGLpdpeRRLDR---YphELSGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 161 DdylkWKIELEVGEVL----RKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:COG0444 182 D----VTIQAQILNLLkdlqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-220 |
2.79e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.26 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFpNMNVYENIKVGiR 101
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD------LTLESlrRQIGVVPQDTFLF-SGTIRENIRYG-R 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGENFDKlIMEKLEEMR----ISHLKDKkiYE---------ISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKI 168
Cdd:COG1132 439 PDATDEE-VEEAAKAAQahefIEALPDG--YDtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALD----TET 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 169 ELEVGEVLRKY---KTpTILVSHsreevyRL-----CKEICVMSKGK------SEELMKKKELFKN 220
Cdd:COG1132 512 EALIQEALERLmkgRT-TIVIAH------RLstirnADRILVLDDGRiveqgtHEELLARGGLYAR 570
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-161 |
2.95e-28 |
|
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: 110.06 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekKINISPKDRK----I 77
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSvksGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQ-------DITHLPMHERarlgI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENIKVGIREGENFDKLIMEK-----LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIIL 152
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREErlealLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
....*....
gi 2646445281 153 LDEPFSALD 161
Cdd:TIGR04406 159 LDEPFAGVD 167
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-223 |
3.03e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlFDSEKKINISPKD---RKIGYLFQDYALFPNMNVYEN----- 95
Cdd:COG4161 29 ETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ-FDFSQKPSEKAIRllrQKVGMVFQQYNLWPHLTVMENlieap 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 96 IKV-GIREGENFDKlIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEVGE 174
Cdd:COG4161 108 CKVlGLSKEQAREK-AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP----EITAQVVE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 175 VLRKYKTPTI---LVSHSREEVYRLCKEICVMSKGKSEElMKKKELFKNPKT 223
Cdd:COG4161 183 IIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHFTQPQT 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-207 |
3.15e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSlTL-KCIAGIEKPDKGRIILNGRvlfdsEKKINiSPKD---RKIGYLFQDYALFPNMNVYENIKVG 99
Cdd:COG3845 32 EIHALLGENGAGKS-TLmKILYGLYQPDSGEILIDGK-----PVRIR-SPRDaiaLGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 iREGENFDKLIMEKLEEM--RIS---HLK---DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSAL-----Ddylkw 166
Cdd:COG3845 105 -LEPTKGGRLDRKAARARirELSeryGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqeaD----- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2646445281 167 kielEVGEVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG3845 179 ----ELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
24-222 |
3.32e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILnGRVLFDSEKKIN-----ISPKDRKIGYLFQDYALFPNMNVYENIKV 98
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLSqqkglIRQLRQHVGFVFQNFNLFPHRTVLENIIE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 G--IREGENFDKLIM---EKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLkwkieleVG 173
Cdd:PRK11264 109 GpvIVKGEPKEEATArarELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL-------VG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 174 EVLR------KYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK11264 182 EVLNtirqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-207 |
6.01e-27 |
|
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: 105.75 E-value: 6.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlFDSEKkinISPKD--RKIGYLFQDYALFpNMNVYENIKVGIR 101
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---TDIRQ---LDPADlrRNIGYVPQDVTLF-YGTLRDNITLGAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGEnfDKLIMEKLE---------------EMRIShlkdKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkw 166
Cdd:cd03245 104 LAD--DERILRAAElagvtdfvnkhpnglDLQIG----ERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM---- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 167 KIELEVGEVLRKYKTP-TILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03245 174 NSEERLKERLRQLLGDkTLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-222 |
1.17e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCI--AGIEKPD---KGRIILNGRVLFdsekkiniSPKD-----RK-IGYLFQDYALFPn 89
Cdd:PRK14239 29 YPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIY--------SPRTdtvdlRKeIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 90 MNVYENIKVGIREGENFDKlimEKLEEMRISHLKDKKIYE------------ISGGEKQRVALARLLINKPEIILLDEPF 157
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDK---QVLDEAVEKSLKGASIWDevkdrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 158 SALDDYLKWKIELEVGEVLRKYKtpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-207 |
1.44e-26 |
|
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: 104.76 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKF------NLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlFDSEKKinisPKD--RK 76
Cdd:cd03265 5 NLVKKYGDFeavrgvSFRVR---RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVRE----PREvrRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 77 IGYLFQDYALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIIL 152
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARlygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 153 LDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-207 |
5.84e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.82 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNgrvlfdsEKKINISP----KDRKIGYLFQDYALFPNMNVYENIK-- 97
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-------DEDISLLPlharARRGIGYLPQEASIFRRLSVYDNLMav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIRE---GENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIElEVGE 174
Cdd:PRK10895 103 LQIRDdlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK-RIIE 181
|
170 180 190
....*....|....*....|....*....|...
gi 2646445281 175 VLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10895 182 HLRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
5.99e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 1 MI-YVDIEKNFGK------FNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKInispk 73
Cdd:PRK09493 1 MIeFKNVSKHFGPtqvlhnIDLNID---QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 74 dRKI----GYLFQDYALFPNMNVYENIKVGIRE-----GENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLL 144
Cdd:PRK09493 73 -RLIrqeaGMVFQQFYLFPHLTALENVMFGPLRvrgasKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 145 INKPEIILLDEPFSALDDYLKWKIeLEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-203 |
6.73e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 106.73 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLlgaSGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKD------RKIGYLFQDYALFPNMNVYENI-- 96
Cdd:COG4175 58 IMGL---SGSGKSTLVRCLNRLIEPTAGEVLIDGEDI------TKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVaf 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 --KV-GIREGENFDKlIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD--------DYLk 165
Cdd:COG4175 129 glEIqGVPKAERRER-AREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDplirremqDEL- 206
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646445281 166 wkIELEvgEVLRKyktpTIL-VSHSREEVYRLCKEICVM 203
Cdd:COG4175 207 --LELQ--AKLKK----TIVfITHDLDEALRLGDRIAIM 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-223 |
7.26e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.90 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNG---RVLFDSEKKINISPKDR------KIGYLFQDYALFPNMNVYE 94
Cdd:PRK10619 32 DVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQLKVADKNQlrllrtRLTMVFQHFNLWSHMTVLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 95 NIK------VGIREGENFDKLIMeKLEEMRISH-LKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLkwk 167
Cdd:PRK10619 112 NVMeapiqvLGLSKQEARERAVK-YLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL--- 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 168 ieleVGEVLR-------KYKTpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:PRK10619 188 ----VGEVLRimqqlaeEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-218 |
1.26e-25 |
|
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: 103.73 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkiNISPKDRK-----IGYLFQDY--ALFPNMNVYENI 96
Cdd:TIGR02769 38 ETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY------QLDRKQRRafrrdVQLVFQDSpsAVNPRMTVRQII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGIREGENFDKL-----IMEKLEEM--RISHLkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIE 169
Cdd:TIGR02769 112 GEPLRHLTSLDESeqkarIAELLDMVglRSEDA-DKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVIL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2646445281 170 LEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELF 218
Cdd:TIGR02769 191 ELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-207 |
1.48e-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: 101.56 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNISPKDR--KIGYLFQD--YALFPNmNVYENIKV 98
Cdd:cd03226 26 GEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---------PIKAKERrkSIGYVMQDvdYQLFTD-SVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylKWKIElEVGEVLRK 178
Cdd:cd03226 96 GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKNME-RVGELIRE 171
|
170 180 190
....*....|....*....|....*....|..
gi 2646445281 179 YKTPT---ILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03226 172 LAAQGkavIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-200 |
1.68e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.59 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQDYALFPNMNVYENIKVGIREG 103
Cdd:PRK11629 36 EMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 ENFDKLIMEKLEEMRISHLKDKKIY----EISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKY 179
Cdd:PRK11629 116 KKKPAEINSRALEMLAAVGLEHRANhrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQ 195
|
170 180
....*....|....*....|.
gi 2646445281 180 KTPTILVSHSREEVYRLCKEI 200
Cdd:PRK11629 196 GTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-207 |
2.89e-25 |
|
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: 101.58 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIekpDKGRIILNGRVLFDSEKkinISPKD--RKIGYLFQDYALFPNMNVYENIK--VG 99
Cdd:cd03234 34 QVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGQILFNGQP---RKPDQfqKCVAYVRQDDILLPGLTVRETLTytAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IREGENFDKLIMEKLEE-MRISHLKD-----KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKwkieLEVG 173
Cdd:cd03234 108 LRLPRKSSDAIRKKRVEdVLLRDLALtriggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA----LNLV 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 2646445281 174 EVLRKY--KTPTILVS-HS-REEVYRLCKEICVMSKGK 207
Cdd:cd03234 184 STLSQLarRNRIVILTiHQpRSDLFRLFDRILLLSSGE 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-220 |
5.90e-25 |
|
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: 101.08 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfDSEKKINISPKDRKIGYLFQDYALFpNMNVYENIKVGIREG 103
Cdd:cd03249 30 KTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLRWLRSQIGLVSQEPVLF-DGTIAENIRYGKPDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 EnfdklimeklEEMRISHLKDKKIYEI-------------------SGGEKQRVALARLLINKPEIILLDEPFSALDDyl 164
Cdd:cd03249 105 T----------DEEVEEAAKKANIHDFimslpdgydtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATSALDA-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 165 kwKIELEVGEVL---RKYKTpTILVSHsreevyRLC-----KEICVMSKGK------SEELMKKKELFKN 220
Cdd:cd03249 173 --ESEKLVQEALdraMKGRT-TIVIAH------RLStirnaDLIAVLQNGQvveqgtHDELMAQKGVYAK 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-207 |
6.09e-25 |
|
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: 98.65 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 4 VDIEKNFGK--------FNLRTkfefdNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDSekkinisPKD 74
Cdd:cd03216 4 RGITKRFGGvkaldgvsLSVRR-----GEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKeVSFAS-------PRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 75 RkigylfqdyalfpnmnvyenIKVGIregenfdklimekleEMrishlkdkkIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:cd03216 72 A--------------------RRAGI---------------AM---------VYQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 155 EPFSALDDylkwkieLEVGEV------LRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03216 108 EPTAALTP-------AEVERLfkvirrLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-203 |
6.12e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSlTL-KCIAGIEKPDKGRIILNGRVL-FDsekkiniSPKD---RKIGYLFQDYALFPNMNVYENIKV 98
Cdd:COG1129 31 EVHALLGENGAGKS-TLmKILSGVYQPDSGEILLDGEPVrFR-------SPRDaqaAGIAIIHQELNLVPNLSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GiREGENFDKL-----------IMEKLeEMRISHlkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYlkwk 167
Cdd:COG1129 103 G-REPRRGGLIdwramrrrareLLARL-GLDIDP--DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER---- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 168 ielEVG---EVLRKYK---TPTILVSHSREEVYRLCKEICVM 203
Cdd:COG1129 175 ---EVErlfRIIRRLKaqgVAIIYISHRLDEVFEIADRVTVL 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-191 |
1.76e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKfnlRTKFE------FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdsekkinisPKDRKIG 78
Cdd:COG0488 3 NLSKSFGG---RPLLDdvslsiNPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------------PKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 79 YLFQDYALFPNMNVYENIKVGIRE------------------GENFDKL--IMEKLEEM-------RI----SHLK---- 123
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTVLDGDAElraleaeleeleaklaepDEDLERLaeLQEEFEALggweaeaRAeeilSGLGfpee 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 124 --DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLKWkieLEvgEVLRKYKTPTILVSHSRE 191
Cdd:COG0488 145 dlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDlESIEW---LE--EFLKNYPGTVLVVSHDRY 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-207 |
1.90e-24 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 99.40 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGK------FNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkiNISPKD-RKI 77
Cdd:TIGR03740 5 NLSKRFGKqtavnnISLTVP---KNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH---------PWTRKDlHKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENIKV-----GIREGEnfdklIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIIL 152
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLKVhttllGLPDSR-----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 153 LDEPFSALDDYlkwKIElEVGEVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR03740 148 LDEPTNGLDPI---GIQ-ELRELIRSFPeqgITVILSSHILSEVQQLADHIGIISEGV 201
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-206 |
1.90e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINISPKDRkiGYLFQDYALFPNMNVYENIKVGIR-- 101
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-------KPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQla 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 --EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKY 179
Cdd:PRK11248 99 gvEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQET 178
|
170 180
....*....|....*....|....*..
gi 2646445281 180 KTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:PRK11248 179 GKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-223 |
3.56e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlFDSEKKINisPKD-----RKIGYLFQDYALFPNMNVYEN- 95
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH-FDFSKTPS--DKAirelrRNVGMVFQQYNLWPHLTVQQNl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 96 ----IKV-GIREGENFDKlIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIEL 170
Cdd:PRK11124 104 ieapCRVlGLSKDQALAR-AEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP----EITA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 171 EVGEVLRKYKTPTI---LVSHSREEVYRLCKEICVMSKGKSEElMKKKELFKNPKT 223
Cdd:PRK11124 179 QIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVE-QGDASCFTQPQT 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-215 |
4.97e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 102.91 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFPnMNVYENIKVGI 100
Cdd:COG4988 363 GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD------LDPASwrRQIAWVPQNPYLFA-GTIRENLRLGR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGEnfDKLIMEKLEEMRISHLK-------DKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLkwkiE 169
Cdd:COG4988 436 PDAS--DEELEAALEAAGLDEFVaalpdglDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET----E 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 170 LEVGEVLRKY---KTpTILVSHsREEVYRLCKEICVMSKGK------SEELMKKK 215
Cdd:COG4988 510 AEILQALRRLakgRT-VILITH-RLALLAQADRILVLDDGRiveqgtHEELLAKN 562
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
24-207 |
7.58e-24 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.13 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFPNmNVYENIkvgireg 103
Cdd:cd03246 29 ESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI----SQWDPNELGDHVGYLPQDDELFSG-SIAENI------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 enfdklimekleemrishlkdkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVLRKYKTPT 183
Cdd:cd03246 97 --------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL-NQAIAALKAAGATR 149
|
170 180
....*....|....*....|....
gi 2646445281 184 ILVSHsREEVYRLCKEICVMSKGK 207
Cdd:cd03246 150 IVIAH-RPETLASADRILVLEDGR 172
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-207 |
1.18e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.11 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsEKKINISPKDR-KIGYL 80
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHvqrGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG------EPVPSRARHARqRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYALFPNMNVYENIKVGIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEP 156
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRyfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 157 FSALDDYLKWKIELEVGEVLRKYKTpTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-221 |
1.34e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.49 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNG---RVLFDSEKKiniSPKDRKIGYLFQDYALFPNMNVYENIKV 98
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELR---EVRRKKIAMVFQSFALMPHMTVLDNTAF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIR----EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGE 174
Cdd:PRK10070 130 GMElagiNAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646445281 175 VLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:PRK10070 210 LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-207 |
5.82e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.33 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfDSEKKINISPKDRKIGYLFQDYALFPNMNVYENIKVGI--- 100
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-TRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLiia 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 -REGENFDKLIMEKLEemRISHLKDKKIYEI--SGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVLR 177
Cdd:PRK10908 108 gASGDDIRRRVSAALD--KVGLLDKAKNFPIqlSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI-LRLFEEFN 184
|
170 180 190
....*....|....*....|....*....|
gi 2646445281 178 KYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10908 185 RVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-208 |
8.40e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLFQDYALFPNMNVYENIKVGIR-- 101
Cdd:PRK13536 68 ECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR-----ARIGVVPQFDNLDLEFTVRENLLVFGRyf 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 --EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKY 179
Cdd:PRK13536 143 gmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG 222
|
170 180
....*....|....*....|....*....
gi 2646445281 180 KTpTILVSHSREEVYRLCKEICVMSKGKS 208
Cdd:PRK13536 223 KT-ILLTTHFMEEAERLCDRLCVLEAGRK 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-207 |
1.32e-22 |
|
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: 93.27 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDS-----EKKINISPKDRKigylfqDYALFPNMNVYENIK 97
Cdd:cd03215 27 EIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSprdaiRAGIAYVPEDRK------REGLVLDLSVAENIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGiregenfdklimekleemriSHLkdkkiyeiSGGEKQRVALARLLINKPEIILLDEPFSALDdylkwkIE--LEVGEV 175
Cdd:cd03215 101 LS--------------------SLL--------SGGNQQKVVLARWLARDPRVLILDEPTRGVD------VGakAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....*
gi 2646445281 176 LRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03215 147 IRELAdagKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-222 |
1.56e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.72 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCI---------AGIEkpdkGRIILNGRVLFDseKKINISPKDRKIGYLFQDYALFPnMNV 92
Cdd:COG1117 36 ENKVTALIGPSGCGKSTLLRCLnrmndlipgARVE----GEILLDGEDIYD--PDVDVVELRRRVGMVFQKPNPFP-KSI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 YENIKVGIRE-GENFDKLIMEKLEE-MRISHL----KDK---KIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDY 163
Cdd:COG1117 109 YDNVAYGLRLhGIKSKSELDEIVEEsLRKAALwdevKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 164 LKWKIElEVGEVLRK-YktpTI-LVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:COG1117 189 STAKIE-ELILELKKdY---TIvIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-207 |
1.62e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.38 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAG--IEKPDKGRIILNGRVLFDSEKKinispkdRKIGYLFQDYALFPNMNVYENIkvg 99
Cdd:cd03213 34 PGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR-------KIIGYVPQDDILHPTLTVRETL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 iregenfdklimekleeMRISHLKDkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALDDYLkwkiELEVGEVLRKY 179
Cdd:cd03213 104 -----------------MFAAKLRG-----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS----ALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|..
gi 2646445281 180 -KT-PTILVS-HS-REEVYRLCKEICVMSKGK 207
Cdd:cd03213 158 aDTgRTIICSiHQpSSEIFELFDKLLLLSQGR 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-219 |
1.82e-22 |
|
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: 94.22 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFpNMNVYENIKVGiREGENFD 107
Cdd:cd03253 32 IVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDSLRRAIGVVPQDTVLF-NDTIGYNIRYG-RPDATDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 108 KLImeklEEMRISHLKDKKI-----YE---------ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVG 173
Cdd:cd03253 106 EVI----EAAKAAQIHDKIMrfpdgYDtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREI-QAAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 174 EVLRKYKTpTILVSHSREEVYRlCKEICVMSKGK------SEELMKKKELFK 219
Cdd:cd03253 181 RDVSKGRT-TIVIAHRLSTIVN-ADKIIVLKDGRivergtHEELLAKGGLYA 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-221 |
2.89e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDkGRIILNGRVLFDS----EKKINISPKDRKIGYLFQDYALFPnMNVYENI 96
Cdd:PRK14258 31 YQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNqniyERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGI-----REGENFDKLIMEKLEEM----RISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWK 167
Cdd:PRK14258 109 AYGVkivgwRPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMK 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 168 IELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSE-----ELMKKKELFKNP 221
Cdd:PRK14258 189 VESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRigqlvEFGLTKKIFNSP 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-161 |
3.00e-22 |
|
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: 93.65 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFD-SEkkinispkD-------RKIGYLFQDYALFPNMNVYEN 95
Cdd:COG4181 39 ESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlDE--------DararlraRHVGFVFQSFQLLPTLTALEN 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 96 IKV-----GIREGEnfdKLIMEKLEEM----RISHlkdkkiY--EISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG4181 111 VMLplelaGRRDAR---ARARALLERVglghRLDH------YpaQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-219 |
5.42e-22 |
|
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: 96.76 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFpNMNVYENIKVGiR 101
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD------LDEDDlrRRIAVVPQRPHLF-DTTLRENLRLA-R 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGENFDKLI--MEK--LEEMrISHLKDK---KIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIEL 170
Cdd:COG4987 434 PDATDEELWaaLERvgLGDW-LAALPDGldtWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDA----ATEQ 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 171 EVGEVLRKY---KTpTILVSHSREEVyRLCKEICVMS------KGKSEELMKKKELFK 219
Cdd:COG4987 509 ALLADLLEAlagRT-VLLITHRLAGL-ERMDRILVLEdgriveQGTHEELLAQNGRYR 564
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-190 |
6.93e-22 |
|
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: 96.54 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 27 GLLGASGSGKSLTLKCIAGIEKPdkgriilngrvlFDSEKKIniSPkDRKIGYLFQDYALFPNMNVYENIKVGIRE---- 102
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKD------------FNGEARP--QP-GIKVGYLPQEPQLDPTKTVRENVEEGVAEikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 --------------GENFDKLI--MEKLE---------------EMRISHLK----DKKIYEISGGEKQRVALARLLINK 147
Cdd:TIGR03719 100 ldrfneisakyaepDADFDKLAaeQAELQeiidaadawdldsqlEIAMDALRcppwDADVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2646445281 148 PEIILLDEPFSALD-DYLKWkieLEvgEVLRKYKTPTILVSHSR 190
Cdd:TIGR03719 180 PDMLLLDEPTNHLDaESVAW---LE--RHLQEYPGTVVAVTHDR 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-188 |
9.48e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.15 E-value: 9.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVL--FDSEKKINISPKDrkIGYLFQDYALFPNMNVYENIKV--- 98
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEARAKLRAKH--VGFVFQSFMLIPTLNALENVELpal 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 --GIREGENFDKLImEKLEEM----RISHLKDkkiyEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEV 172
Cdd:PRK10584 115 lrGESSRQSRNGAK-ALLEQLglgkRLDHLPA----QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170
....*....|....*.
gi 2646445281 173 GEVLRKYKTPTILVSH 188
Cdd:PRK10584 190 FSLNREHGTTLILVTH 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-161 |
1.21e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 93.64 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD-----RKIGYLFQD-YA-LFPNMNVY--- 93
Cdd:COG4608 45 ETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG------LSGRElrplrRRMQMVFQDpYAsLNPRMTVGdii 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 94 -ENIKV-GIREGENFDKLIMEKLEE--MRISHLkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG4608 119 aEPLRIhGLASKAERRERVAELLELvgLRPEHA-DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-156 |
1.28e-21 |
|
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: 91.97 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDR---KIGYLFQDYALFPNMNVYENIKVGI 100
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI------TGLPPHRIarlGIGYVPEGRRIFPSLTVEENLLLGA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 101 REGENFDKlIMEKLEEmrishlkdkkIYEI---------------SGGEKQRVALARLLINKPEIILLDEP 156
Cdd:COG0410 104 YARRDRAE-VRADLER----------VYELfprlkerrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-207 |
1.40e-21 |
|
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: 91.63 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLF-QDYALFPNMNVYENIKV-- 98
Cdd:cd03267 46 KGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-----RRIGVVFgQKTQLWWDLPVIDSFYLla 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 ---GIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEV 175
Cdd:cd03267 121 aiyDLPPAR-FKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
170 180 190
....*....|....*....|....*....|..
gi 2646445281 176 LRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03267 200 NRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-222 |
1.47e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTkfefdNEIMGLLGASGSGKSLT----LKCIAGiekpdKGRIILNGRVLFDSEKKiNISPKDRKIGYLFQD--YAL 86
Cdd:PRK15134 307 FTLRP-----GETLGLVGESGSGKSTTglalLRLINS-----QGEIWFDGQPLHNLNRR-QLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 87 FPNMNVYENIKVGIR------EGENFDKLIMEKLEEMRIS-HLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PRK15134 376 NPRLNVLQIIEEGLRvhqptlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 160 LDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-210 |
3.15e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinispkdrKIGYLF 81
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRidrGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYALF-PNMNVYENIkvgiREGenfdkliMEKLEEMRI-SHLKD---------KKIYEISGGEKQRVALARLLINKPEI 150
Cdd:COG0488 385 QHQEELdPDKTVLDEL----RDG-------APGGTEQEVrGYLGRflfsgddafKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 151 ILLDEPFSALDdylkwkIE----LEvgEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEE 210
Cdd:COG0488 454 LLLDEPTNHLD------IEtleaLE--EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-222 |
4.14e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEK--KINISPKDRKIGYLFQDYALFPNMNVYENIKV- 98
Cdd:PRK14246 35 NNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 ----GIREGENFDKLIMEKLEEM----RISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIEL 170
Cdd:PRK14246 115 lkshGIKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 171 EVGEVlrKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK14246 195 LITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-203 |
4.92e-21 |
|
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: 93.89 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFPNmNVYENIKVGIR 101
Cdd:TIGR02857 349 ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD------ADADSwrDQIAWVPQHPFLFAG-TIAENIRLARP 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGEnfDKLIMEKLEEMRISHL-------KDKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLkwkiEL 170
Cdd:TIGR02857 422 DAS--DAEIREALERAGLDEFvaalpqgLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EA 495
|
170 180 190
....*....|....*....|....*....|....*
gi 2646445281 171 EVGEVLRKYKT--PTILVSHsREEVYRLCKEICVM 203
Cdd:TIGR02857 496 EVLEALRALAQgrTVLLVTH-RLALAALADRIVVL 529
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-214 |
7.35e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYaLFPnmnvyENIKVgi 100
Cdd:PRK11231 28 GKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM------LSSRQlaRRLALLPQHH-LTP-----EGITV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 RE----------------GENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyL 164
Cdd:PRK11231 94 RElvaygrspwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD--I 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 165 KWKIELE--VGEVLRKYKTpTILVSHSREEVYRLCKEICVMSKGK-----------SEELMKK 214
Cdd:PRK11231 172 NHQVELMrlMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHvmaqgtpeevmTPGLLRT 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-161 |
8.38e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.17 E-value: 8.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYAL-FPnMNVYENIKVG- 99
Cdd:COG4559 28 ELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA------WSPWElaRRRAVLPQHSSLaFP-FTVEEVVALGr 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 100 ---IREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLI-------NKPEIILLDEPFSALD 161
Cdd:COG4559 101 aphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-207 |
9.38e-21 |
|
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: 92.94 E-value: 9.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRI-ILNGRVLFDSEKK--INISPKDRKIGYLFQDYALFPNMNVYENI- 96
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPgpDGRGRAKRYIGILHQEYDLYPHRTVLDNLt 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 -KVGIREGENFDK------LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIE 169
Cdd:TIGR03269 388 eAIGLELPDELARmkavitLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVT 467
|
170 180 190
....*....|....*....|....*....|....*...
gi 2646445281 170 LEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR03269 468 HSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-219 |
1.79e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.91 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispKDRK-IGYLFQ--DYALFpNMNVYENIKVGI 100
Cdd:PRK13636 33 EVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM---KLREsVGMVFQdpDNQLF-SASVYQDVSFGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGENFDKLIMEK----LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:PRK13636 109 VNLKLPEDEVRKRvdnaLKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2646445281 177 RKYKTPTILVSHSREEVYRLCKEICVMSKGKS------EELMKKKELFK 219
Cdd:PRK13636 189 KELGLTIIIATHDIDIVPLYCDNVFVMKEGRVilqgnpKEVFAEKEMLR 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-222 |
1.85e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGI-----EKPDKGRIILNGRVLFdsekKINISPKDRKIGYLFQDYALFPNMNVYENI 96
Cdd:PRK14247 28 DNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF----KMDVIELRRRVQMVFQIPNPIPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGIRegenFDKLIMEKLE-EMRISH-LKDKKIYE------------ISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:PRK14247 104 ALGLK----LNRLVKSKKElQERVRWaLEKAQLWDevkdrldapagkLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 163 YLKWKIELEVGEvLRKYKTpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK14247 180 ENTAKIESLFLE-LKKDMT-IVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-221 |
2.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.69 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQdyalFPNMNVYEN----------IK 97
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ----FPEHQLFEEtvekdicfgpMN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREgENFDKLIMEKLEEMRISH-LKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVL 176
Cdd:PRK13634 114 FGVSE-EDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM-MEMFYKL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 177 RKYKTPT-ILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:PRK13634 192 HKEKGLTtVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-161 |
2.40e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYAL-FPnMNVYENIKVGI 100
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD------WSPAElaRRRAVLPQHSSLsFP-FTVEEVVAMGR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 101 ----REGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLI------NKPEIILLDEPFSALD 161
Cdd:PRK13548 102 aphgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-190 |
5.41e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.95 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 27 GLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdsekkiniSPkDRKIGYLFQDYALFPNMNVYENIKVGIRE---- 102
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP--------------AP-GIKVGYLPQEPQLDPEKTVRENVEEGVAEvkaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 --------------GENFDKLI--MEKLEEmRISHL--------------------KDKKIYEISGGEKQRVALARLLIN 146
Cdd:PRK11819 102 ldrfneiyaayaepDADFDALAaeQGELQE-IIDAAdawdldsqleiamdalrcppWDAKVTKLSGGERRRVALCRLLLE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2646445281 147 KPEIILLDEPFSALD-DYLKWkieLEvgEVLRKYKTPTILVSHSR 190
Cdd:PRK11819 181 KPDMLLLDEPTNHLDaESVAW---LE--QFLHDYPGTVVAVTHDR 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-206 |
5.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.64 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTKFEFDNEI-----MGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQdyalF 87
Cdd:PRK13643 17 FASRALFDIDLEVkkgsyTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 88 PNMNVYENI----------KVGIREgENFDKLIMEKLEEMRIS-HLKDKKIYEISGGEKQRVALARLLINKPEIILLDEP 156
Cdd:PRK13643 93 PESQLFEETvlkdvafgpqNFGIPK-EKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 157 FSALDDylKWKIE-LEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:PRK13643 172 TAGLDP--KARIEmMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-220 |
1.14e-19 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 87.10 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSlTL-KCIAGIEKPDKGRIILNGRVLFDSEKKINISpkdRKIGYLFQ-------------DYALF 87
Cdd:TIGR04520 27 KGEFVAIIGHNGSGKS-TLaKLLNGLLLPTSGKVTVDGLDTLDEENLWEIR---KKVGMVFQnpdnqfvgatvedDVAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 88 PnmnvyENIKVgirEGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKwk 167
Cdd:TIGR04520 103 L-----ENLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGR-- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 168 ieLEVGEVLRK----YKTPTILVSHSREEVyRLCKEICVMSKGKSEELMKKKELFKN 220
Cdd:TIGR04520 173 --KEVLETIRKlnkeEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-195 |
1.18e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKC-------IAGIEKpdKGRIILNGRVLFDSEkkINISPKDRKIGYLFQDYALFPNmNVYEN 95
Cdd:PRK14243 36 NQITAFIGPSGCGKSTILRCfnrlndlIPGFRV--EGKVTFHGKNLYAPD--VDPVEVRRRIGMVFQKPNPFPK-SIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 96 IKVGIR----EGeNFDKLIMEKLEEMRI-SHLKDK---KIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWK 167
Cdd:PRK14243 111 IAYGARingyKG-DMDELVERSLRQAALwDEVKDKlkqSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLR 189
|
170 180
....*....|....*....|....*...
gi 2646445281 168 IELEVGEVLRKYKtpTILVSHSREEVYR 195
Cdd:PRK14243 190 IEELMHELKEQYT--IIIVTHNMQQAAR 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-207 |
1.28e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINI-SPKD---RKIGYLFQD---YALFPNMNVYENI 96
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGADPADSGEIRLDG-------KPVRIrSPRDairAGIAYVPEDrkgEGLVLDLSIRENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 ---------KVGI----REGENFDKLImeklEEMRI--SHLkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG1129 352 tlasldrlsRGGLldrrRERALAEEYI----KRLRIktPSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 162 dylkwkieleVG------EVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG1129 427 ----------VGakaeiyRLIRELAaegKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-207 |
1.65e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.66 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVL--FDSEKKinispKD--RKIGYLFQDY--ALFPNMNVYENIK 97
Cdd:PRK10419 39 ETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakLNRAQR-----KAfrRDIQMVFQDSisAVNPRKTVREIIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREGENFDK-------LIMEKLEEMRISHLkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIEL 170
Cdd:PRK10419 114 EPLRHLLSLDKaerlaraSEMLRAVDLDDSVL-DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR 192
|
170 180 190
....*....|....*....|....*....|....*..
gi 2646445281 171 EVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10419 193 LLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-223 |
2.32e-19 |
|
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: 88.97 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSlTLkciagiekpdkGRIILN-----GRVLFDSEKKINISPKD-----RKIGYLFQD-YA-LFPNMN 91
Cdd:COG4172 313 ETLGLVGESGSGKS-TL-----------GLALLRlipseGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 92 VyENIkvgIREG----------ENFDKLIMEKLEEMRISH-LKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:COG4172 381 V-GQI---IAEGlrvhgpglsaAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 161 D--------DYLKwkiELEvgevlRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:COG4172 457 DvsvqaqilDLLR---DLQ-----REHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-193 |
2.77e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.15 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 30 GASGSGKSLTLKCIAGIEKPDKGRIilngrvLFDSEKKINISPKD--RKIGYLFQDYALFPNmNVYENIKV--GIREGEN 105
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPTSGTL------LFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNLIFpwQIRNQQP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 106 FDKLIMEKLEEMRI-SHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKYKTPTI 184
Cdd:PRK10247 113 DPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
....*....
gi 2646445281 185 LVSHSREEV 193
Cdd:PRK10247 193 WVTHDKDEI 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-222 |
3.23e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.07 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFD-SEKKINISPKDrkIGYLFQD--YALFPNMNVYENIK 97
Cdd:PRK15079 45 YEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSD--IQMIFQDplASLNPRMTIGEIIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREgeNFDKL----IMEKLEEMR-----ISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD------- 161
Cdd:PRK15079 123 EPLRT--YHPKLsrqeVKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqaqv 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 162 -DYLKwKIELEVGEVLrkyktptILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK15079 201 vNLLQ-QLQREMGLSL-------IFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-217 |
4.91e-19 |
|
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: 84.85 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFpNMNVYENIKVGiREG 103
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL----ALADPAWLRRQVGVVLQENVLF-NRSIRDNIALA-DPG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 ENFDKLIM--------EKLEEMRISHlkDKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELE 171
Cdd:cd03252 103 MSMERVIEaaklagahDFISELPEGY--DTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 172 VGEVLrkyKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKEL 217
Cdd:cd03252 181 MHDIC---AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-221 |
5.54e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.32 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTkfefdNEIMGLLGASGSGKSLTLKCIAGIEKPDkGRI----ILNGR-VLFDSEKKINispKDR--KIGYLFQD-- 83
Cdd:PRK09473 37 FSLRA-----GETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGReILNLPEKELN---KLRaeQISMIFQDpm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 84 YALFPNMNVYENI-KV-----GIREGENFDK----LIMEKLEEMRishlKDKKIY--EISGGEKQRVALARLLINKPEII 151
Cdd:PRK09473 108 TSLNPYMRVGEQLmEVlmlhkGMSKAEAFEEsvrmLDAVKMPEAR----KRMKMYphEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 152 LLDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-207 |
8.52e-19 |
|
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: 87.11 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkiNISPKD--RKIGYLFQDYALFPNmNVYENIKvgiR 101
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS------QWDREElgRHIGYLPQDVELFDG-TIAENIA---R 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 EGE-NFDKLI----MEKLEEMrISHLKDKkiYE---------ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwk 167
Cdd:COG4618 429 FGDaDPEKVVaaakLAGVHEM-ILRLPDG--YDtrigeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----- 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2646445281 168 ieleVGEV--------LRKYKTPTILVSHsREEVYRLCKEICVMSKGK 207
Cdd:COG4618 501 ----EGEAalaaairaLKARGATVVVITH-RPSLLAAVDKLLVLRDGR 543
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-222 |
1.07e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQ--DYALFPNmNVYENIKVG 99
Cdd:PRK13641 32 EGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IRE-GENFDKLIMEKLEEMRISHLKD----KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEVGE 174
Cdd:PRK13641 111 PKNfGFSEDEAKEKALKWLKKVGLSEdlisKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP----EGRKEMMQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 175 VLRKYKTP---TILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK13641 187 LFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-218 |
1.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdSEKkiNISPKDRKIGYLFQDY-ALFPNMNVYENIKVGIR- 101
Cdd:PRK13650 34 EWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL--TEE--NVWDIRHKIGMVFQNPdNQFVGATVEDDVAFGLEn 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 ---EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylKWKIEL--EVGEVL 176
Cdd:PRK13650 110 kgiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP--EGRLELikTIKGIR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 177 RKYKTPTILVSHSREEVyRLCKEICVMSKGKSEELMKKKELF 218
Cdd:PRK13650 188 DDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELF 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-161 |
1.80e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINISPKDRKIGYLFQDYALFPNMNVYENIKV--GI 100
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-------GDIDDPDVAEACHYLGHRNAMKPALTVAENLEFwaAF 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 101 REGENFDklIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK13539 101 LGGEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-161 |
1.86e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.66 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNG--------RVLFDSEKKINIspkdrkigyLFQDYALFPNMNVYEN 95
Cdd:PRK11831 34 KITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrSRLYTVRKRMSM---------LFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 96 IKVGIREGENFDK-----LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK11831 105 VAYPLREHTQLPApllhsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-220 |
2.30e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 82.66 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkINISPKDRKIGYLFQDYALFpNMNVYENIKVGIREG 103
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD----YTLASLRRQIGLVSQDVFLF-NDTVAENIAYGRPGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 E-----------NFDKLIMEKLEEMrishlkDKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKI 168
Cdd:cd03251 104 TreeveeaaraaNAHEFIMELPEGY------DTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDT----ES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 169 ELEVGEVLRK-YKTPTILVSHSREEVYRLCKEICVMSKGK------SEELMKKKELFKN 220
Cdd:cd03251 174 ERLVQAALERlMKNRTTFVIAHRLSTIENADRIVVLEDGKivergtHEELLAQGGVYAK 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-161 |
2.45e-18 |
|
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: 82.02 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKdRKIGYLFQDYALFPNMNVYENIKVGIREG 103
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPH-ENILYLGHLPGLKPELSALENLHFWAAIH 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 104 ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:TIGR01189 102 GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
28-193 |
4.04e-18 |
|
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: 82.44 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIIlngrVLFDsEKKINISPKD--RKIGY----LFQDYAlfPNMNVYENI----- 96
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFG-ERRGGEDVWElrKRIGLvspaLQLRFP--RDETVLDVVlsgff 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 -KVGI-REGENFDK-LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVG 173
Cdd:COG1119 107 dSIGLyREPTDEQReRARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELL-LALL 185
|
170 180
....*....|....*....|.
gi 2646445281 174 EVLRKYKTPT-ILVSHSREEV 193
Cdd:COG1119 186 DKLAAEGAPTlVLVTHHVEEI 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-206 |
5.31e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDK---GRIILNGRVLfDSEKKI--NISPKDRKIGYLFQDYALFPNMNVYENIKV 98
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTV-QREGRLarDIRKSRANTGYIFQQFNLVNRLSVLENVLI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIREGENF------------DKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYlKW 166
Cdd:PRK09984 110 GALGSTPFwrtcfswftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPE-SA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 167 KIELEVGEVLRKYKTPTILVS-HSREEVYRLCKEICVMSKG 206
Cdd:PRK09984 189 RIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQG 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-206 |
5.44e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkiNISP-KDRKIG-YLF-QDYALFPNMNVYENIKVGI 100
Cdd:PRK15439 38 EVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA------RLTPaKAHQLGiYLVpQEPLLFPNLSVKENILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGENFDKLIMEKLEEMRiSHLK-DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD----DYLKWKIelevgEV 175
Cdd:PRK15439 112 PKRQASMQKMKQLLAALG-CQLDlDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpaetERLFSRI-----RE 185
|
170 180 190
....*....|....*....|....*....|.
gi 2646445281 176 LRKYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:PRK15439 186 LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
5.71e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGI-----EKPDKGRIILNGRVLFDSEkkINISPKDRKIGYLFQDYALFPNMNVYENIK 97
Cdd:PRK14267 30 NGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPD--VDPIEVRREVGMVFQYPNPFPHLTIYDNVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIRegenFDKLIMEK--LEEMRISHLKDKKIYE------------ISGGEKQRVALARLLINKPEIILLDEPFSALDDY 163
Cdd:PRK14267 108 IGVK----LNGLVKSKkeLDERVEWALKKAALWDevkdrlndypsnLSGGQRQRLVIARALAMKPKILLMDEPTANIDPV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 164 LKWKIELEVGEVLRKYKtpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK14267 184 GTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-161 |
1.20e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 30 GASGSGKSLTLKCIAGIEKPDKGRIiLNGRVLFDSEKKinispkdrKIGYLFQDYALFPNMNVYENIKVGIREgeNFDKL 109
Cdd:PRK11247 45 GRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARE--------DTRLMFQDARLLPWKKVIDNVGLGLKG--QWRDA 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 110 IMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK11247 114 ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-222 |
1.22e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 18 KFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfDSEKKINISPKDRKIGYLFQD-YA-LFPNMNV 92
Cdd:PRK10261 342 KVSFDlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-DTLSPGKLQALRRDIQFIFQDpYAsLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 ----YENIKV-GIREGENFDKLIMEKLEemRISHLKD---KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYL 164
Cdd:PRK10261 421 gdsiMEPLRVhGLLPGKAAAARVAWLLE--RVGLLPEhawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 165 KWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-207 |
1.25e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.26 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinispkdrKIGYLF 81
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTinpGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QdyalfpnmnvyenikvgiregenfdklimekleemrishlkdkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03221 70 Q-----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 162 dyLKWKIELEvgEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03221 103 --LESIEALE--EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-219 |
1.39e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTKFEFDNEIM-----GLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQdyalF 87
Cdd:PRK13649 18 FEGRALFDVNLTIEdgsytAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 88 PNMNVYE------------NIKVGIREGEnfdKLIMEKLEEMRISH-LKDKKIYEISGGEKQRVALARLLINKPEIILLD 154
Cdd:PRK13649 94 PESQLFEetvlkdvafgpqNFGVSQEEAE---ALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 155 EPFSALDDylKWKIEL-EVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFK 219
Cdd:PRK13649 171 EPTAGLDP--KGRKELmTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-222 |
1.60e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.30 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEkpDK-------GRIILNGRVLFDSEKKINISpkdRKIGYLFQDYALFPnMNVYENIK 97
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMN--DKvsgyrysGDVLLGGRSIFNYRDVLEFR---RRVGMLFQRPNPFP-MSIMDNVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREGE-----NFDKLIMEKLEEMRI-SHLKDK---KIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI 168
Cdd:PRK14271 123 AGVRAHKlvprkEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 169 ElevgEVLRKY--KTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK14271 203 E----EFIRSLadRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-226 |
1.91e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.62 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSltlKCIAGIE---KPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFpNMNVYENIKVGI 100
Cdd:TIGR00958 508 EVVALVGPSGSGKS---TVAALLQnlyQPTGGQVLLDGVPL----VQYDHHYLHRQVALVGQEPVLF-SGSVRENIAYGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGE-----------NFDKLIMEklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIE 169
Cdd:TIGR00958 580 TDTPdeeimaaakaaNAHDFIME--FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 170 LEVGEVLRKYKTPTILVSHsREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSS 226
Cdd:TIGR00958 654 QLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-220 |
1.95e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.81 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDY-ALFPNMNVYENIKVG 99
Cdd:PRK13632 33 NEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENLKEIRKKIGIIFQNPdNQFIGATVEDDIAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IrEGENFD-----KLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGE 174
Cdd:PRK13632 109 L-ENKKVPpkkmkDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI-KKIMV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646445281 175 VLRKYKTPTIL-VSHSREEVYrLCKEICVMSKGKSEELMKKKELFKN 220
Cdd:PRK13632 187 DLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-161 |
2.49e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsekkinispkDRKIGYLFQDYAL---FPnMNVYENIKVG----- 99
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVpdsLP-LTVRDLVAMGrwarr 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 100 --IREGENFDKLIMEK-LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:NF040873 87 glWRRLTRDDRAAVDDaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-207 |
7.42e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPD---KGRIILNGRVLfDSEKKINISpkdrkiGYLFQDYALFPNMNVYE--NIKV 98
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEMRAIS------AYVQQDDLFIPTLTVREhlMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIREGENFDK-----LIMEKLEEMRISHLKDKKI------YEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWk 167
Cdd:TIGR00955 125 HLRMPRRVTKkekreRVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY- 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2646445281 168 ielEVGEVLR----KYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR00955 204 ---SVVQVLKglaqKGKTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-162 |
8.15e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 30 GASGSGKSLTLKCIAGIEKPDKGRIIL--NGRVLFDSEKkinisPkdrkigYLFQ----DYALFPNmnvyenikvgirEG 103
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQR-----P------YLPLgtlrEALLYPA------------TA 452
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 104 ENF-DKLIMEKLEEMRISHLKDK--------KIyeISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:COG4178 453 EAFsDAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-207 |
1.33e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.69 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPD--KGRIILNGRVLfdsekkinISPKDRKIGYLFQDYALFPNMNVYENIKVG-- 99
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP--------TKQILKRTGFVTQDDILYPHLTVRETLVFCsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IREGENFDKLIMEKLEEMRISHLKDKK----------IYEISGGEKQRVALA-RLLINkPEIILLDEPFSALDDYLKWKI 168
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELGLTKcentiignsfIRGISGGERKRVSIAhEMLIN-PSLLILDEPTSGLDATAAYRL 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646445281 169 ELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-161 |
1.37e-16 |
|
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: 77.15 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLFQDYALFPNMNVYENIKVGIREG 103
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-----RGLLYLGHAPGIKTTLSVLENLRFWHADH 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 104 EnfDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03231 102 S--DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-207 |
2.70e-16 |
|
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: 76.35 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 19 FEFD-NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsekkinispkdrkIGYLFQdYALFPNMNVYENIk 97
Cdd:cd03250 26 LEVPkGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQ-EPWIQNGTIRENI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 vgiREGENFDKlimEKLEE-MRISHL-KDKKI------YEI-------SGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:cd03250 87 ---LFGKPFDE---ERYEKvIKACALePDLEIlpdgdlTEIgekginlSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 163 YL-KWKIELEVGEVLRKYKTpTILVSHsREEVYRLCKEICVMSKGK 207
Cdd:cd03250 161 HVgRHIFENCILGLLLNNKT-RILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-210 |
2.79e-16 |
|
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: 75.81 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLFQDYALFpNMNVYENIkvgireG 103
Cdd:cd03247 29 EKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS-----SLISVLNQRPYLF-DTTLRNNL------G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 ENFdklimekleemrishlkdkkiyeiSGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKyKTpT 183
Cdd:cd03247 97 RRF------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KT-L 150
|
170 180
....*....|....*....|....*..
gi 2646445281 184 ILVSHSREEVYRLcKEICVMSKGKSEE 210
Cdd:cd03247 151 IWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-188 |
4.35e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 79.06 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 3 YVDIEKNFGKFNLRTK--FEFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIilngrvlfdsEKKINISPKDRkigYL 80
Cdd:COG1245 344 YPDLTKSYGGFSLEVEggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKISYKPQ---YI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYalfpNMNVYENIKVGIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:COG1245 411 SPDY----DGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190
....*....|....*....|....*....|....
gi 2646445281 161 DdylkwkIE--LEVGEVLRKY----KTPTILVSH 188
Cdd:COG1245 487 D------VEqrLAVAKAIRRFaenrGKTAMVVDH 514
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-223 |
4.86e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.04 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVL-FDSEKKINISpkdRKIGYLFQ--DYALFPNmNVYENI-- 96
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYDKKSLLEVR---KTVGIVFQnpDDQLFAP-TVEEDVaf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 ---KVGIREgENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVG 173
Cdd:PRK13639 103 gplNLGLSK-EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLY 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 174 EVLRKYKTpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKT 223
Cdd:PRK13639 182 DLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-215 |
5.59e-16 |
|
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: 76.11 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFPNmNVYENIKVGirEGENFD 107
Cdd:cd03254 34 IVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI----RDISRKSLRSMIGVVLQDTFLFSG-TIMENIRLG--RPNATD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 108 KLIMEKLEEMRISHLKDK--KIYE---------ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIElEVGEVL 176
Cdd:cd03254 107 EEVIEAAKEAGAHDFIMKlpNGYDtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQ-EALEKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2646445281 177 RKYKTpTILVSHsREEVYRLCKEICVMSKGK------SEELMKKK 215
Cdd:cd03254 186 MKGRT-SIIIAH-RLSTIKNADKILVLDDGKiieegtHDELLAKK 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-207 |
6.72e-16 |
|
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: 75.65 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRV--LFDsekkinispkdrkIGYLFQdyalfPNMNVYENIKVGI 100
Cdd:cd03220 48 GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssLLG-------------LGGGFN-----PELTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGENFDKLIMEKLEEM-RISHLK---DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:cd03220 110 RLLGLSRKEIDEKIDEIiEFSELGdfiDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL 189
|
170 180 190
....*....|....*....|....*....|.
gi 2646445281 177 RKYKTpTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03220 190 KQGKT-VILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-222 |
9.47e-16 |
|
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: 78.19 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEkPDkGRIILNGRVLFDSEKKINISPKD------RKIGYLFQD--YALFPNMNV--- 92
Cdd:COG4172 37 ETLALVGESGSGKSVTALSILRLL-PD-PAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmTSLNPLHTIgkq 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 -YENIKV--GIReGENFDKLIMEKLEEMRISHLKDK-KIY--EISGGEKQRVALARLLINKPEIILLDEPFSALD----- 161
Cdd:COG4172 115 iAEVLRLhrGLS-GAAARARALELLERVGIPDPERRlDAYphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqa 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 162 ---DYLKwkiELEvgevlRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:COG4172 194 qilDLLK---DLQ-----RELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-243 |
9.86e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 16 RTKFEF-----------DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKIN-ISPKDRKIGYLFQ- 82
Cdd:PRK13645 19 KTPFEFkalnntsltfkKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKeVKRLRKEIGLVFQf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 83 -DYALFPNmNVYENIKVG-IREGENFDKLIMEKLEEMRISHLKDKKI----YEISGGEKQRVALARLLINKPEIILLDEP 156
Cdd:PRK13645 99 pEYQLFQE-TIEKDIAFGpVNLGENKQEAYKKVPELLKLVQLPEDYVkrspFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 157 FSALD-----DYLKWKIELEvgevlRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSSCLISG 231
Cdd:PRK13645 178 TGGLDpkgeeDFINLFERLN-----KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEIDP 252
|
250
....*....|..
gi 2646445281 232 CKNFSEIEKISD 243
Cdd:PRK13645 253 PKLYQLMYKLKN 264
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-207 |
1.40e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRV--LFDsekkinispkdrkIGYLFQdyalfPNMNVYENIKV--- 98
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsaLLE-------------LGAGFH-----PELTGRENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 --GIREGEnfdklIMEKLEEmrI---SHLKDK-----KIYeiSGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI 168
Cdd:COG1134 115 llGLSRKE-----IDEKFDE--IvefAELGDFidqpvKTY--SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKC 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646445281 169 ELEVGEVLRKYKTpTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG1134 186 LARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-161 |
1.77e-15 |
|
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: 77.40 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkINISPKDRKIGYLFQDYALFpNMNVYENIKVGirEGENFD 107
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS----LDQDEVRRRVSVCAQDAHLF-DTTVRENLRLA--RPDATD 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 108 KLIMEKLEEMRI-SHLK------DKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:TIGR02868 439 EELWAALERVGLaDWLRalpdglDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-207 |
1.86e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIeKPD---KGRIILNGRVLfdseKKINISPKDRK-IGYLFQDYALFPNMNVYENIKVG 99
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL----QASNIRDTERAgIAIIHQELALVKELSVLENIFLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 --IREGE--NFDKLIMEK---LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYlKWKIELEV 172
Cdd:PRK13549 107 neITPGGimDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTES-ETAVLLDI 185
|
170 180 190
....*....|....*....|....*....|....*
gi 2646445281 173 GEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK13549 186 IRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-226 |
2.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQ---DYALFPNMN---VYENI 96
Cdd:PRK13652 30 NSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI----TKENIREVRKFVGLVFQnpdDQIFSPTVEqdiAFGPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGIREgENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:PRK13652 106 NLGLDE-ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 177 RKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSS 226
Cdd:PRK13652 185 ETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-219 |
2.27e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.05 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdSEKkiNISPKDRKIGYLFQD---------------YALf 87
Cdd:PRK13635 33 GEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEE--TVWDVRRQVGMVFQNpdnqfvgatvqddvaFGL- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 88 pnmnvyENIKVgirEGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylKWK 167
Cdd:PRK13635 108 ------ENIGV---PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP--RGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 168 IE-LEVGEVLRKYKTPTIL-VSHSREEVYRlCKEICVMSKGKSEELMKKKELFK 219
Cdd:PRK13635 177 REvLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-207 |
2.74e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 74.04 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKInispKDRKIGYLFQDYALFPNmNVYENIKVGIR-- 101
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY----LHSKVSLVGQEPVLFAR-SLQDNIAYGLQsc 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 ---------EGENFDKLIMEKleEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEV 172
Cdd:cd03248 116 sfecvkeaaQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
170 180 190
....*....|....*....|....*....|....*
gi 2646445281 173 GEVLRkyKTPTILVSHSREEVYRlCKEICVMSKGK 207
Cdd:cd03248 194 YDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-221 |
2.94e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.71 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 12 KFNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDkgRIILNGRVLFDSEKKINISPKDRK------IGYLFQD-- 83
Cdd:COG4170 25 RVSLTLN---EGEIRGLVGESGSGKSLIAKAICGITKDN--WHVTADRFRWNGIDLLKLSPRERRkiigreIAMIFQEps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 84 YALFPNMNVYENIKVGI----REGENFDKLIMEKLEEMRISH---LKD-KKI-----YEISGGEKQRVALARLLINKPEI 150
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIpswtFKGKWWQRFKWRKKRAIELLHrvgIKDhKDImnsypHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 151 ILLDEPFSALDDYLKWKIeLEVGEVLRKYKTPTIL-VSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:COG4170 180 LIADEPTNAMESTTQAQI-FRLLARLNQLQGTSILlISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-206 |
4.00e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDSEKKINispkdRKIGYLFQDYALFPNMNVYENIKVG- 99
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdVEALSARAAS-----RRVASVPQDTSLSFEFDVRQVVEMGr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 -------IREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIE-LE 171
Cdd:PRK09536 103 tphrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--INHQVRtLE 180
|
170 180 190
....*....|....*....|....*....|....*
gi 2646445281 172 VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:PRK09536 181 LVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-207 |
4.08e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispkdRKIGYLF-QDYALFPNMNVYENIKV---- 98
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFA-----RRIGVVFgQRSQLWWDLPAIDSFRLlkai 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 -GIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLR 177
Cdd:COG4586 124 yRIPDAE-YKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNR 202
|
170 180 190
....*....|....*....|....*....|
gi 2646445281 178 KYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG4586 203 ERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-161 |
4.97e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinispkdrKIGYLFQDYALFPNMNV----YENIKVGI 100
Cdd:PRK09544 32 ILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------------RIGYVPQKLYLDTTLPLtvnrFLRLRPGT 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 101 REGEnfdklIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK09544 97 KKED-----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-222 |
6.70e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.05 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQdyalFPNMNVYE-NIKVGIREG-EN 105
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESQLFEdTVEREIIFGpKN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 106 FdKLIMEKLEEMRISHLKD---------KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVL 176
Cdd:PRK13646 114 F-KMNLDEVKNYAHRLLMDlgfsrdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 177 RKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK13646 193 TDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-161 |
7.25e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 3 YVDIEKNFGKFNLRTK--FEFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIilngrvlfdsEKKINISPKDRkigYL 80
Cdd:PRK13409 343 YPDLTKKLGDFSLEVEggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPELKISYKPQ---YI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYalfpNMNVYENI-KVGIREGENFDKLimEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PRK13409 410 KPDY----DGTVEDLLrSITDDLGSSYYKS--EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
..
gi 2646445281 160 LD 161
Cdd:PRK13409 484 LD 485
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-207 |
7.33e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.38 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 19 FEFDN---------------EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQD 83
Cdd:PRK13657 342 FSYDNsrqgvedvsfeakpgQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI----RTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 84 YALFpNMNVYENIKVGiREGENfDKLIMEKLEE-------MRISHLKDKKIYE----ISGGEKQRVALARLLINKPEIIL 152
Cdd:PRK13657 418 AGLF-NRSIEDNIRVG-RPDAT-DEEMRAAAERaqahdfiERKPDGYDTVVGErgrqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 153 LDEPFSALDDYLKWKIELEVGEVlRKYKTpTILVSHsREEVYRLCKEICVMSKGK 207
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDEL-MKGRT-TFIIAH-RLSTVRNADRILVFDNGR 546
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-207 |
7.44e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 21 FDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRvlfdsEKKINISPKDRKIGYLFQDYALFPNMNVYENIKVGI 100
Cdd:TIGR01257 954 YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK-----DIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 R-EGENFD--KLIMEK-LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIelevGEVL 176
Cdd:TIGR01257 1029 QlKGRSWEeaQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI----WDLL 1104
|
170 180 190
....*....|....*....|....*....|...
gi 2646445281 177 RKYKT--PTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR01257 1105 LKYRSgrTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-161 |
7.47e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDSEKKINispkdRKIGYLFQDYAL--FPNMNVYENIKVGIREGE 104
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYKRA-----KYIGRVFQDPMMgtAPSMTIEENLALAYRRGK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 105 NFD----------KLIMEKLEEMRIS---HLKDkKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG1101 112 RRGlrrgltkkrrELFRELLATLGLGlenRLDT-KVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-229 |
7.81e-15 |
|
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: 75.22 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEF---DNEIMGLLGASGSGKSLTLKCIAGIE--KPDKGRIILN-------GRV------------ 60
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFtieEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcGYVerpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 61 ---LFDSEKKINISPKD-------RKIGYLFQ-DYALFPNMNVYENIKVGIRE----GENFDKLIMEKLEEMRISHLKDK 125
Cdd:TIGR03269 85 cggTLEPEEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEigyeGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 126 KIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLC-KEI---- 200
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSdKAIwlen 244
|
250 260 270
....*....|....*....|....*....|.
gi 2646445281 201 -CVMSKGKSEELMKK-KELFKNPKTFSSCLI 229
Cdd:TIGR03269 245 gEIKEEGTPDEVVAVfMEGVSEVEKECEVEV 275
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-208 |
9.16e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 6 IEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINispKDRKIGYLFQ 82
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTvypGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA---AQLGIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 83 DYALFPNMNVYENIKVGIREGENFDKLIMEKLEEMRISH--------LK---DKKIYEISGGEKQRVALARLLINKPEII 151
Cdd:PRK09700 88 ELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAammllrvgLKvdlDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 152 LLDEPFSALD----DYLkwkieLEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKS 208
Cdd:PRK09700 168 IMDEPTSSLTnkevDYL-----FLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSS 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-219 |
1.02e-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: 75.16 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFPNmNVYENIKVGIRE 102
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL----KDIDRHTLRQFINYLPQEPYIFSG-SILENLLLGAKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 GENFDKLImeklEEMRISHLKD--KKI------------YEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI 168
Cdd:TIGR01193 575 NVSQDEIW----AACEIAEIKDdiENMplgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 169 eleVGEVLRKYKTPTILVSHsREEVYRLCKEICVMSKGKSEELMKKKELFK 219
Cdd:TIGR01193 651 ---VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-207 |
1.12e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDSEKkiniSPKDRKIGYLFQDYALFPNMNVYENI------ 96
Cdd:PRK11288 31 QVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASTT----AALAAGVAIIYQELHLVPEMTVAENLylgqlp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 -KVGIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYlkwkiELE---- 171
Cdd:PRK11288 107 hKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR-----EIEqlfr 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 2646445281 172 VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK11288 182 VIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-220 |
1.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.81 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlFDSEKKINISPKDRKIGYLFQ-------------DYALFPnm 90
Cdd:PRK13633 37 EFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG---LDTSDEENLWDIRNKAGMVFQnpdnqivativeeDVAFGP-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 91 nvyENIKVgirEGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIEL 170
Cdd:PRK13633 112 ---ENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVN 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 171 EVGEVLRKYKTPTILVSHSREEVYRlCKEICVMSKGKSEELMKKKELFKN 220
Cdd:PRK13633 186 TIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-207 |
1.46e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDsekkiniSPKDRK---IGYLFQDYALFPNMNVYENIKVGi 100
Cdd:PRK10762 32 VMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKeVTFN-------GPKSSQeagIGIIHQELNLIPQLTIAENIFLG- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 RE------GENFDKLIMEK---LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwkIELE 171
Cdd:PRK10762 104 REfvnrfgRIDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD-----TETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2646445281 172 ----VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10762 179 slfrVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
3-161 |
1.94e-14 |
|
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: 72.06 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 3 YVDIEKNFGKFNLR-TKFEF-DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINISPKdrkigYL 80
Cdd:cd03237 3 YPTMKKTLGEFTLEvEGGSIsESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-------DTVSYKPQ-----YI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 FQDYalfpNMNVYENIKVGIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:cd03237 71 KADY----EGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
.
gi 2646445281 161 D 161
Cdd:cd03237 147 D 147
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-235 |
2.02e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKpDKGRIILNgRVLFDSEKKINISPKDRK------IGYLFQD--YALFPNMNVYEN 95
Cdd:PRK15093 34 EIRGLVGESGSGKSLIAKAICGVTK-DNWRVTAD-RMRFDDIDLLRLSPRERRklvghnVSMIFQEpqSCLDPSERVGRQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 96 IKVGI----REGENFDKLIMEKLEEMRISH---LKDKK------IYEISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:PRK15093 112 LMQNIpgwtYKGRWWQRFGWRKRRAIELLHrvgIKDHKdamrsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 163 YLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP-KTFSSCLISGCKNF 235
Cdd:PRK15093 192 TTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPhHPYTQALIRAIPDF 265
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-207 |
2.14e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 74.09 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 30 GASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFpNMNVYENIKVGiREGENFD 107
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD------VTQASlrAAIGIVPQDTVLF-NDTIAYNIAYG-RPDASEE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 108 KLI----MEKLEEMrISHLKDKkiYE---------ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEVGE 174
Cdd:COG5265 463 EVEaaarAAQIHDF-IESLPDG--YDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDS----RTERAIQA 535
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 175 VLR---KYKTpTILVSHsreevyRL-----CKEICVMSKGK 207
Cdd:COG5265 536 ALRevaRGRT-TLVIAH------RLstivdADEILVLEAGR 569
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-207 |
3.03e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKgriiLNGRVLFDSE--KKINISPKDRK-IGYLFQDYALFPNMNVYENIKVG- 99
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGVYPHGT----WDGEIYWSGSplKASNIRDTERAgIVIIHQELTLVPELSVAENIFLGn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 --IREGENFDKLIM-----EKLEEMRISHLKD-KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYlKWKIELE 171
Cdd:TIGR02633 104 eiTLPGGRMAYNAMylrakNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK-ETEILLD 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 2646445281 172 VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR02633 183 IIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-207 |
3.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDS-EKKINispkdRKIGYLFQDY--ALFpNMNVYENIKVGIR--- 101
Cdd:PRK13647 36 LLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnEKWVR-----SKVGLVFQDPddQVF-SSTVWDDVAFGPVnmg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 -EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVLRKYK 180
Cdd:PRK13647 110 lDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL-MEILDRLHNQG 188
|
170 180
....*....|....*....|....*..
gi 2646445281 181 TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK13647 189 KTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-200 |
1.42e-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: 71.50 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFD---NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinispkdrKIGYLF 81
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKlppGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDY-ALFPNMNVYENIKVGIregenfDKLIMEKLEEMRISHL---------KDKKIYEISGGEKQRVALARLLINKPEII 151
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGL------DIIKLGKREIPSRAYVgrfnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 152 LLDEPFSALDdylkwkIE----LEvgEVLRKYKTPTILVSHSREEVYRLCKEI 200
Cdd:TIGR03719 466 LLDEPTNDLD------VEtlraLE--EALLNFAGCAVVISHDRWFLDRIATHI 510
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-219 |
1.66e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.78 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSekkiNISPKDRKIGYLFQDyalfP-NMNVYENIKVGIREG--- 103
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD----NFEKLRKHIGIVFQN----PdNQFVGSIVKYDVAFGlen 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 -----ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRK 178
Cdd:PRK13648 112 havpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 179 YKTPTILVSHSREEVYRlCKEICVMSKGKSEELMKKKELFK 219
Cdd:PRK13648 192 HNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-206 |
2.24e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKK--INISPKDRKIGYLF----QDYALfpnMNVYENIKV 98
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVDWSFpvlvEDVVM---MGRYGHMGW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 GIREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKIELEVGEVLRK 178
Cdd:PRK15056 112 LRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD----VKTEARIISLLRE 187
|
170 180 190
....*....|....*....|....*....|.
gi 2646445281 179 YKTP--TILVS-HSREEVYRLCkEICVMSKG 206
Cdd:PRK15056 188 LRDEgkTMLVStHNLGSVTEFC-DYTVMVKG 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-201 |
3.27e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.52 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSlTLKCIAG-IEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQDYALFPNMNVYENIKV---- 98
Cdd:PRK10535 35 EMVAIVGASGSGKS-TLMNILGcLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQNVEVpavy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 -GIREGENFDKLImEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkwkielevgevlr 177
Cdd:PRK10535 114 aGLERKQRLLRAQ-ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD---------------- 176
|
170 180
....*....|....*....|....
gi 2646445281 178 kyktptilvSHSREEVYRLCKEIC 201
Cdd:PRK10535 177 ---------SHSGEEVMAILHQLR 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-191 |
4.07e-13 |
|
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: 66.41 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdsekkinisPKDRKIGYLFQDyALFPNMNvyenikvgiregenfd 107
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQR-PYLPLGT---------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 108 klimekleemrishLKDKKIY----EISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEVGEVLRKYKTPT 183
Cdd:cd03223 80 --------------LREQLIYpwddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKELGITV 141
|
....*...
gi 2646445281 184 ILVSHSRE 191
Cdd:cd03223 142 ISVGHRPS 149
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-218 |
4.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfDSEKKINISpkdRKIGYLFQDY-ALFPNMNVYENIKVGIRE 102
Cdd:PRK13642 34 EWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-TAENVWNLR---RKIGMVFQNPdNQFVGATVEDDVAFGMEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 G----ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRK 178
Cdd:PRK13642 110 QgiprEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2646445281 179 YKTPTILVSHSREEVYRlCKEICVMSKGKSEELMKKKELF 218
Cdd:PRK13642 190 YQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-161 |
5.01e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEkPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFPNMNVYENIKVGIR 101
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSD------WSAAElaRHRAYLSQQQSPPFAMPVFQYLALHQP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 102 EG---ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLL------INkPE--IILLDEPFSALD 161
Cdd:COG4138 96 AGassEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptIN-PEgqLLLLDEPMNSLD 165
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-229 |
6.30e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRI----ILNG-------RVLFDSEKKINISPKDRK-IGYLFQ--DYALFP 88
Cdd:PRK13631 52 NKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGdkknnheLITNPYSKKIKNFKELRRrVSMVFQfpEYQLFK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 89 NMN----VYENIKVGIREGENfDKLIMEKLEEMRI-SHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDy 163
Cdd:PRK13631 132 DTIekdiMFGPVALGVKKSEA-KKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP- 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 164 lkwKIELEVGEVLRKYKT---PTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSSCLI 229
Cdd:PRK13631 210 ---KGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSI 275
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-222 |
6.35e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAG-IEKPdkGRIILNgRVLFDSEKKINISPKDRK------IGYLFQD--YALFPNMNV-- 92
Cdd:PRK11022 34 EVVGIVGESGSGKSVSSLAIMGlIDYP--GRVMAE-KLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPCYTVgf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 --YENIKV--GIREGENFDKLImEKLEEMRI----SHLkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYL 164
Cdd:PRK11022 111 qiMEAIKVhqGGNKKTRRQRAI-DLLNQVGIpdpaSRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 165 KWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK11022 189 QAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-207 |
7.16e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 12 KFNLRTKfefdnEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINISPkDRKIGYL-----FQDYAL 86
Cdd:PRK11300 25 NLEVREQ-----EIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG-------QHIEGLP-GHQIARMgvvrtFQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 87 FPNMNVYEN--------IKVGI------------REGENFDKlIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLIN 146
Cdd:PRK11300 92 FREMTVIENllvaqhqqLKTGLfsgllktpafrrAESEALDR-AATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 147 KPEIILLDEPFSALDDylKWKIELE--VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK11300 171 QPEILMLDEPAAGLNP--KETKELDelIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-206 |
7.91e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFdsekkINISPKDRKIGYLFQDYALFPNMNVYENIKVGIR-- 101
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-----TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARlr 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 --EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKY 179
Cdd:TIGR01257 2041 gvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG 2120
|
170 180
....*....|....*....|....*..
gi 2646445281 180 KTpTILVSHSREEVYRLCKEICVMSKG 206
Cdd:TIGR01257 2121 RA-VVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-217 |
8.36e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdseKKINI-SPKD---RKIGYLFQ---DYALFPNMNVYENI 96
Cdd:PRK09700 290 EILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG-------KDISPrSPLDavkKGMAYITEsrrDNGFFPNFSIAQNM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KV-------------GIREGENFDKLIMEKLEEMRIS-HLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:PRK09700 363 AIsrslkdggykgamGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 163 YLKwkieLEVGEVLRKYKTP---TILVSHSREEVYRLCKEICVMSKGK-SEELMKKKEL 217
Cdd:PRK09700 443 GAK----AEIYKVMRQLADDgkvILMVSSELPEIITVCDRIAVFCEGRlTQILTNRDDM 497
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-207 |
8.89e-13 |
|
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: 68.97 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDsekkINISPKDRKIGYLFQDYALFpNMNVYENIKVGIREG 103
Cdd:TIGR02203 359 ETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD----YTLASLRRQVALVSQDVVLF-NDTIANNIAYGRTEQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 enfdkLIMEKLEE-MRISHLKD--------------KKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI 168
Cdd:TIGR02203 434 -----ADRAEIERaLAAAYAQDfvdklplgldtpigENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV 508
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646445281 169 ELEVgEVLRKYKTpTILVSHsREEVYRLCKEICVMSKGK 207
Cdd:TIGR02203 509 QAAL-ERLMQGRT-TLVIAH-RLSTIEKADRIVVMDDGR 544
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-207 |
9.77e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.32 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINIspkdRKI-GYLFQD-YALFPNMNVYENIKVGir 101
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI----RKLvGIVFQNpETQFVGRTVEEDLAFG-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 eGENF-------DKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGE 174
Cdd:PRK13644 103 -PENLclppieiRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
|
170 180 190
....*....|....*....|....*....|...
gi 2646445281 175 VLRKYKTpTILVSHSREEVYrLCKEICVMSKGK 207
Cdd:PRK13644 182 LHEKGKT-IVYITHNLEELH-DADRIIVMDRGK 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-207 |
1.03e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKDR---KIGYLFQD---YALFPNMNVYENIK 97
Cdd:COG3845 285 EILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI------TGLSPRERrrlGVAYIPEDrlgRGLVPDMSVAENLI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREGENFDKLIMEKLEEMRiSHLKDK-KIYEI------------SGGEKQRVALARLLINKPEIILLDEPFSALDdyl 164
Cdd:COG3845 359 LGRYRRPPFSRGGFLDRKAIR-AFAEELiEEFDVrtpgpdtparslSGGNQQKVILARELSRDPKLLIAAQPTRGLD--- 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 165 kwkieleVG------EVLRKYK---TPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:COG3845 435 -------VGaiefihQRLLELRdagAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-222 |
1.09e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.03 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTlkCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQD--YALFP--NM--NVYENIK 97
Cdd:PRK10418 30 RVLALVGGSGSGKSLT--CAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPlhTMhtHARETCL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREGEnfDKLIMEKLEEM------RISHLKDkkiYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELE 171
Cdd:PRK10418 108 ALGKPAD--DATLTAALEAVglenaaRVLKLYP---FEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 172 VGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK10418 183 LESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-161 |
1.16e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINIspkdRKIGYLFQDYALFPNMNVYENIKVGI--- 100
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTVRELVAIGRypw 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 101 -----REGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK10575 114 hgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-221 |
2.09e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTKfefdnEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEkkinISPKDRKIGYLFQD--YALFPNM 90
Cdd:PRK15112 34 FTLREG-----QTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 91 NVYENIKVGIR-----EGENFDKLIMEKLEEMRIshLKDKKIY---EISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:PRK15112 105 RISQILDFPLRlntdlEPEQREKQIIETLRQVGL--LPDHASYyphMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 163 YLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-207 |
2.34e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSE------KKINISPKDRKIgylfqdyalFPNMNVYENIK 97
Cdd:PRK11614 32 EIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtakimrEAVAIVPEGRRV---------FSRMTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VG--IREGENFDKLImEKLEEM--RISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVG 173
Cdd:PRK11614 103 MGgfFAERDQFQERI-KWVYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI-FDTI 180
|
170 180 190
....*....|....*....|....*....|....
gi 2646445281 174 EVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK11614 181 EQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-207 |
2.39e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.86 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSlTL-KCIAGIEK--PDKGRIILNGRVLFDsekkinISPKDRK---IGYLFQDYALFPNMNVYEN 95
Cdd:COG0396 25 PGEVHAIMGPNGSGKS-TLaKVLMGHPKyeVTSGSILLDGEDILE------LSPDERAragIFLAFQYPVEIPGVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 96 IK--VGIREGEN-----FDKLIMEKLEEMRISH-LKDKKIYE-ISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLK 165
Cdd:COG0396 98 LRtaLNARRGEElsareFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDiDALR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646445281 166 WkieleVGEVLRKYKTP---TILVSHSReevyRLCKEIC-----VMSKGK 207
Cdd:COG0396 178 I-----VAEGVNKLRSPdrgILIITHYQ----RILDYIKpdfvhVLVDGR 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-190 |
2.39e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekKINISPKDRKIGYLFQDYALFPNMNVYENIKVGIrege 104
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDI---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 105 NFDKLIMEKLEEMRI---SHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVgEVLRKYKT 181
Cdd:PRK13540 100 HFSPGAVGITELCRLfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI-QEHRAKGG 178
|
....*....
gi 2646445281 182 PTILVSHSR 190
Cdd:PRK13540 179 AVLLTSHQD 187
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-222 |
3.37e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 30 GASGSGKS-----LTLkciagIEKPDKGRIILNGRVLFDSEKkINISPKDRKIGYLFQD-YA-LFPNMnvyeniKVGIRE 102
Cdd:PRK11308 48 GESGCGKStlarlLTM-----IETPTGGELYYQGQDLLKADP-EAQKLLRQKIQIVFQNpYGsLNPRK------KVGQIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 GE----NFDKLIMEK----LEEMRISHLK----DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKIEL 170
Cdd:PRK11308 116 EEplliNTSLSAAERrekaLAMMAKVGLRpehyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD----VSVQA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 171 EVGEVL----RKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK11308 192 QVLNLMmdlqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-207 |
3.73e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGI-EKPDKGRIILNGRVL-----FDS-EKKINISPKDRKigylfqDYALFPNMNVYENI 96
Cdd:TIGR02633 287 EILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnpAQAiRAGIAMVPEDRK------RHGIVPILGVGKNI 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGIREGENFDKLIMEKLEEMRIS------HLK----DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKW 166
Cdd:TIGR02633 361 TLSVLKSFCFKMRIDAAAELQIIGsaiqrlKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 167 KIELEVGEVLRKyKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR02633 441 EIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-214 |
8.46e-12 |
|
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: 63.31 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPdkgrIILNGRVLFDSEKKINISPKDRK---IGYLFQDYALFP---NMNVYENI 96
Cdd:cd03217 26 GEVHALMGPNGSGKSTLAKTIMGHPKY----EVTEGEILFKGEDITDLPPEERArlgIFLAFQYPPEIPgvkNADFLRYV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGiregenfdklimekleemrishlkdkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLKwkielEVGEV 175
Cdd:cd03217 102 NEG------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDiDALR-----LVAEV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 176 LRKYKTPT---ILVSHSRE--------EVYRLCKEICVMSKGKS--EELMKK 214
Cdd:cd03217 147 INKLREEGksvLIITHYQRlldyikpdRVHVLYDGRIVKSGDKElaLEIEKK 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-220 |
1.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.44 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPD---KGRII-----LNGRVLFDSEKKINI---SPKDRKIGYLFQDYALFPnmnvYENI 96
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLLLPDdnpNSKITvdgitLTAKTVWDIREKVGIvfqNPDNQFVGATVGDDVAFG----LENR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 KVGIREgenFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEVGEVL 176
Cdd:PRK13640 114 AVPRPE---MIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI-LKLIRKL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 177 RKYKTPTIL-VSHSREEVyRLCKEICVMSKGK------SEELMKKKELFKN 220
Cdd:PRK13640 190 KKKNNLTVIsITHDIDEA-NMADQVLVLDDGKllaqgsPVEIFSKVEMLKE 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-161 |
1.05e-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: 63.61 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNgrvlfDSEKKINI---SPKD----RK--IGYLFQdyalF------- 87
Cdd:COG4778 38 ECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-----HDGGWVDLaqaSPREilalRRrtIGYVSQ----Flrviprv 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 88 PNMNVYEN--IKVGIREGENFDKlIMEKLEEMRI-SHLKDkkIYEI--SGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:COG4778 109 SALDVVAEplLERGVDREEARAR-ARELLARLNLpERLWD--LPPAtfSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-218 |
1.38e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfDSEKKINISPKdRKIGYLFQDyalfPNMNV-YENI------- 96
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALR-QQVATVFQD----PEQQIfYTDIdsdiafs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 --KVGIREGEnFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGE 174
Cdd:PRK13638 103 lrNLGVPEAE-ITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2646445281 175 VLRKyKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELF 218
Cdd:PRK13638 182 IVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-221 |
2.41e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLT-LKCIAGIEKPD----KGRIILNGRVLFDSEKKINISPKDRKIGYLFQD--YALFPNMNV---- 92
Cdd:PRK15134 36 ETLALVGESGSGKSVTaLSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVSLNPLHTLekql 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 YENIKV--GIRE----GEnfdklIMEKLEEMRISH----LKDKKiYEISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:PRK15134 116 YEVLSLhrGMRReaarGE-----ILNCLDRVGIRQaakrLTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 163 YLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNP 221
Cdd:PRK15134 190 SVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-220 |
2.57e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVL--FDSEKKIN-----ISPKDRKIG-YLFQDY---ALFPNMNV 92
Cdd:PRK10982 275 EILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINhgfalVTEERRSTGiYAYLDIgfnSLISNIRN 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 YENiKVGIREGENFDKLIMEKLEEMRI---SHlkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIE 169
Cdd:PRK10982 355 YKN-KVGLLDNSRMKSDTQWVIDSMRVktpGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIY 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 170 LEVGEVLRKYKTpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKN 220
Cdd:PRK10982 432 QLIAELAKKDKG-IIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQN 481
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
24-188 |
3.70e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 62.28 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGiekpDKGRIILNGRVLFDSEKKINISPKDR-KIG-YL-FQDYALFPNMNVYENIKVGI 100
Cdd:TIGR01978 27 EIHAIMGPNGSGKSTLSKTIAG----HPSYEVTSGTILFKGQDLLELEPDERaRAGlFLaFQYPEEIPGVSNLEFLRSAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 ---REGEN--------FDKLIMEKLEEMRIS-HLKDKKIYE-ISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLKw 166
Cdd:TIGR01978 103 narRSARGeepldlldFEKLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDiDALK- 181
|
170 180
....*....|....*....|....*
gi 2646445281 167 kielEVGEVLRKYKTPT---ILVSH 188
Cdd:TIGR01978 182 ----IVAEGINRLREPDrsfLIITH 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-193 |
4.67e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 5 DIEKNFGKFNLRTKFEFDNEI---MGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdSEKKinispkdrKIGYLF 81
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAgerLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-------SENA--------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 82 QDYAL-FPN-MNVYENIKVGIREGENfDKLIMEKLEEMRIShlKD---KKIYEISGGEKQRVALARLLINKPEIILLDEP 156
Cdd:PRK15064 389 QDHAYdFENdLTLFDWMSQWRQEGDD-EQAVRGTLGRLLFS--QDdikKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 157 FSALDdylkwkieLEVGE----VLRKYKTPTILVSHSREEV 193
Cdd:PRK15064 466 TNHMD--------MESIEslnmALEKYEGTLIFVSHDREFV 498
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-207 |
4.71e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKciagiekpdkgriILNGRVLFDsEKKINISpKDRKIGYLFQDYALFPNMNVYENIKVGIR 101
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMK-------------ILNGEVLLD-DGRIIYE-QDLIVARLQQDPPRNVEGTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 E-GE-------------------NFDKL--IMEKLE-------EMRISH-LK------DKKIYEISGGEKQRVALARLLI 145
Cdd:PRK11147 93 EqAEylkryhdishlvetdpsekNLNELakLQEQLDhhnlwqlENRINEvLAqlgldpDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 146 NKPEIILLDEPFSALD-DYLKWkieLEvgEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDiETIEW---LE--GFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-207 |
5.86e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNG-RVLFDSEKK-----INISPKDRKigylfQDyALFPNMNVYENIK 97
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDairagIMLCPEDRK-----AE-GIIPVHSVADNIN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 VGIREGENFDKLIM-----EKLEEMRISHLK------DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKW 166
Cdd:PRK11288 354 ISARRHHLRAGCLInnrweAENADRFIRSLNiktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646445281 167 KIeLEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK11288 434 EI-YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-207 |
6.34e-11 |
|
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: 61.12 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 2 IYVDIEKNFGKFNLRTKFEF---DNEIMGLLGASGSGKSLTLKCIAGIEkpdKGRIILNGRVLFDS-EKKINISPKDRKI 77
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGvvkPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGiPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 78 GYLFQDYALFPNMNVYENIKVGIR-EGENFdklimekleemrishlkdkkIYEISGGEKQRVALARLLINKPEIILLDEP 156
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRcKGNEF--------------------VRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 157 FSALDDylkwKIELEVGEVLR----KYKTPTIL-VSHSREEVYRLCKEICVMSKGK 207
Cdd:cd03233 146 TRGLDS----STALEILKCIRtmadVLKTTTFVsLYQASDEIYDLFDKVLVLYEGR 197
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-210 |
7.18e-11 |
|
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: 60.89 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFPNmNVYENIKvgiRE 102
Cdd:cd03369 34 GEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLEDLRSSLTIIPQDPTLFSG-TIRSNLD---PF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 GENFDKLIMEKLeemRISHLKDKkiyeISGGEKQRVALARLLINKPEIILLDEPFSALDdylkWKIELEVGEVLRK-YKT 181
Cdd:cd03369 106 DEYSDEEIYGAL---RVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALIQKTIREeFTN 174
|
170 180
....*....|....*....|....*....
gi 2646445281 182 PTILVSHSREEVYRLCKEICVMSKGKSEE 210
Cdd:cd03369 175 STILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-161 |
8.19e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.66 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTKFeFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdseKKINISPKDRK-IGYLFQDYALFPNMN 91
Cdd:PRK13541 17 FDLSITF-LPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY---------KNCNINNIAKPyCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 92 VYENIKVGiREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK13541 87 VFENLKFW-SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-207 |
1.28e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 13 FNLRTkfefdNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkINISPKD---RKIGYLFQDY---AL 86
Cdd:PRK10762 273 FTLRK-----GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV------VTRSPQDglaNGIVYISEDRkrdGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 87 FPNMNVYENIKV-GIREGENFDKLIMEKLEEMRISHL----------KDKKIYEISGGEKQRVALARLLINKPEIILLDE 155
Cdd:PRK10762 342 VLGMSVKENMSLtALRYFSRAGGSLKHADEQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646445281 156 PFSALDDYLKwkieLEVGEVLRKYKT---PTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10762 422 PTRGVDVGAK----KEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-220 |
1.82e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIeKPDKGRIILNGRVLFDsekkinISPKD--RKIGYLFQDYALFPNmNVYENIKVGI 100
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRE------LDPESwrKHLSWVGQNPQLPHG-TLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 REGEnfDKLIMEKLEEMRIS----HLKDKKIYEI-------SGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIE 169
Cdd:PRK11174 448 PDAS--DEQLQQALENAWVSeflpLLPQGLDTPIgdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDA----HSE 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 170 LEVGEVLRKY---KTpTILVSHSREEVYRlCKEICVMSKGK------SEELMKKKELFKN 220
Cdd:PRK11174 522 QLVMQALNAAsrrQT-TLMVTHQLEDLAQ-WDQIWVMQDGQivqqgdYAELSQAGGLFAT 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-216 |
3.32e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 57 NGRVLFDSEKKINISPKDRK--IGYLFQDYALFpNMNVYENIKVGIREGENFD-------KLIMEKLEEMRISHLKDKKI 127
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRnlFSIVSQEPMLF-NMSIYENIKFGKEDATREDvkrackfAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 128 Y--EISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHSREEVYRLCKEIC---- 201
Cdd:PTZ00265 1355 YgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVfnnp 1434
|
170 180
....*....|....*....|.
gi 2646445281 202 ------VMSKGKSEELMKKKE 216
Cdd:PTZ00265 1435 drtgsfVQAHGTHEELLSVQD 1455
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-207 |
3.65e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDK-GRIILNGrvlfdseKKINIS-------------PKDRKigylfqDYALFPN 89
Cdd:PRK13549 289 EILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDG-------KPVKIRnpqqaiaqgiamvPEDRK------RDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 90 MNVYENIKVGIREGENFDKLIMEKLEEMRI----SHLKDK------KIYEISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PRK13549 356 MGVGKNITLAALDRFTGGSRIDDAAELKTIlesiQRLKVKtaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2646445281 160 LDDYLKWKIELEVGEvLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK13549 436 IDVGAKYEIYKLINQ-LVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-161 |
4.50e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGR---------IILNGR---------VLFDSEKKINISPkdrkigylfQD 83
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILDEFRgselqnyftKLLEGDVKVIVKP---------QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 84 YALFPNM---NVYENIKvGIREGENFDKLImeklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:cd03236 96 VDLIPKAvkgKVGELLK-KKDERGKLDELV----DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
.
gi 2646445281 161 D 161
Cdd:cd03236 171 D 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-207 |
5.59e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 8 KNFGKFNLRTKfefDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR-VLFDSEKKinisPKDRKIGYLFQDYAL 86
Cdd:PRK10982 12 KALDNVNLKVR---PHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFKSSKE----ALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 87 FPNMNVYENIKVG--IREGENFDKLIMEK-----LEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PRK10982 85 VLQRSVMDNMWLGryPTKGMFVDQDKMYRdtkaiFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 160 LDdylkwkiELEVG---EVLRKYKTP---TILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10982 165 LT-------EKEVNhlfTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-161 |
6.52e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinispkdrKIGYLFQDY-ALFPNMNVYENI------- 96
Cdd:PRK11819 352 IVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------------KLAYVDQSRdALDPNKTVWEEIsggldii 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 97 KVGIRE--------GENF---DklimekleemrishlKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK11819 417 KVGNREipsrayvgRFNFkggD---------------QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-260 |
6.95e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 25 IMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVlfdsekkinispkdrkiGYLFQDyALFPNMNVYENIKVGIREGE 104
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------------AYVPQQ-AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 105 NFDKLIMEK---LEEMRISHLKDK-----KIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI-ELEVG-E 174
Cdd:TIGR00957 728 KYYQQVLEAcalLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfEHVIGpE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 175 VLRKYKTpTILVSHSREEVYRLcKEICVMSKGKSEELMKKKELFKNPKTFSSCLisgcKNFSEIEKISDTKlfaKDWDVE 254
Cdd:TIGR00957 808 GVLKNKT-RILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAFAEFL----RTYAPDEQQGHLE---DSWTAL 878
|
....*.
gi 2646445281 255 LETSDK 260
Cdd:TIGR00957 879 VSGEGK 884
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-161 |
7.96e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 30 GASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKinispkdRKIGYLFQDYALFPNMNVYENIK-VGIREGENFDK 108
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-------RFMAYLGHLPGLKADLSTLENLHfLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 109 LIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK13543 117 MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-207 |
1.05e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGieKPDKGRIILNGRVLFDSEKKINISPKDR-KIGYLFQDYALFPNMNVYENIKVGIR- 101
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAARc 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 102 -----EGENFDKLI-MEKLEE--MRI---SHLKDKK-----IYEISGGEKQRVALARLLINKPEIILLDEPFSALDDylk 165
Cdd:TIGR00956 166 ktpqnRPDGVSREEyAKHIADvyMATyglSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS--- 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646445281 166 wKIELEVGEVLRKY-----KTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:TIGR00956 243 -ATALEFIRALKTSanildTTPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-188 |
1.23e-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: 59.41 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRI--------ILN---GRVLFD-----SEKKINISpkdRKIGYLfqDYAlf 87
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDyfkklANGEIKVA---HKPQYV--DLI-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 88 PNM---NVYENIKvGIREGENFDKLImeklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYL 164
Cdd:COG1245 173 PKVfkgTVRELLE-KVDERGKLDELA----EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....*..
gi 2646445281 165 KwkieLEVGEVLRKY---KTPTILVSH 188
Cdd:COG1245 248 R----LNVARLIRELaeeGKYVLVVEH 270
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-222 |
1.27e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLT-LKCIAGIEKP----DKGRIILNGRvlfdSEKKINISPKDRK---------IGYLFQD--YALF 87
Cdd:PRK10261 43 ETLAIVGESGSGKSVTaLALMRLLEQAgglvQCDKMLLRRR----SRQVIELSEQSAAqmrhvrgadMAMIFQEpmTSLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 88 PNMNVYENIKVGIR--EGENFDKLIMEK---LEEMRISHLK---DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PRK10261 119 PVFTVGEQIAESIRlhQGASREEAMVEAkrmLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 160 LDDYLKWKIeLEVGEVLRK-YKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPK 222
Cdd:PRK10261 199 LDVTIQAQI-LQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-168 |
1.27e-09 |
|
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: 56.87 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAG------IEkpdkGRIILNGRvlfdsEKKINISpkdRKIGYLFQDYALFPNMNVYENikvgir 101
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGrktagvIT----GEILINGR-----PLDKNFQ---RSTGYVEQQDVHSPNLTVREA------ 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 102 egenfdklimekleeMRIShlkdKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI 168
Cdd:cd03232 100 ---------------LRFS----ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-217 |
2.98e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINIS------PKDRKIGYLFQDYALFPNMN--VYEN 95
Cdd:PRK15439 290 EILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvylPEDRQSSGLYLDAPLAWNVCalTHNR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 96 IKVGIREGEnfDKLIMEKLEE---MRISHLkDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIeLEV 172
Cdd:PRK15439 370 RGFWIKPAR--ENAVLERYRRalnIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI-YQL 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2646445281 173 GEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKEL 217
Cdd:PRK15439 446 IRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-162 |
3.13e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdsekkinispkdRKIGYLFQDYALF--------PNMNVYEN 95
Cdd:PRK13538 28 ELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------------RRQRDEYHQDLLYlghqpgikTELTALEN 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 96 IKVGIR-EGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDD 162
Cdd:PRK13538 95 LRFYQRlHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-207 |
3.77e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGIEKPdkgriiLNGRVLFDSEKKINISPKD--RKIGYLFQDYALFPNMNVYENIKVG 99
Cdd:PRK10253 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTP------AHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 --------IREGENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIE-L 170
Cdd:PRK10253 106 ryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--ISHQIDlL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 2646445281 171 EVGEVLRKYKTPTI-LVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK10253 184 ELLSELNREKGYTLaAVLHDLNQACRYASHLIALREGK 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-207 |
4.71e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 14 NLRTKFEFDNEImGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEKKINISPKDRKIGYLFQDYALFPnmnvy 93
Cdd:PLN03073 527 NLNFGIDLDSRI-AMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFP----- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 94 enikvGIREgenfdKLIMEKLEEMRIS-HLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLKWKIEle 171
Cdd:PLN03073 601 -----GVPE-----QKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQ-- 668
|
170 180 190
....*....|....*....|....*....|....*.
gi 2646445281 172 vGEVLrkYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PLN03073 669 -GLVL--FQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-204 |
5.45e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNgrvlfDSE--KKINISPKDRKIGYLFQDYALFPNmNVYENIKVGI----- 100
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIIIN-----DSHnlKDINLKWWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkd 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 ---------------REGENFDKLIMEK----------------LEEMR-----------------------ISHLKDKk 126
Cdd:PTZ00265 490 lealsnyynedgndsQENKNKRNSCRAKcagdlndmsnttdsneLIEMRknyqtikdsevvdvskkvlihdfVSALPDK- 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 127 iYE---------ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKYKTPTILVSHsREEVYRLC 197
Cdd:PTZ00265 569 -YEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-RLSTIRYA 646
|
....*..
gi 2646445281 198 KEICVMS 204
Cdd:PTZ00265 647 NTIFVLS 653
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-161 |
7.52e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 22 DNEIMGLLGASGSGKSLTLKCIAGI---------EKPDKGRII--LNGRVLFD-----SEKKINISpkdRKIGYLfqDYA 85
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVLkrFRGTELQNyfkklYNGEIKVV---HKPQYV--DLI 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 86 lfPNM---NVYENIKvGIREGENFDKLImeklEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK13409 173 --PKVfkgKVRELLK-KVDERGKLDEVV----ERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-161 |
8.36e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIeKPDKGRIILNGRVLFDsekkINISPKDRKIGYLFQDYALFPNMNVYE----NIKVG 99
Cdd:PRK03695 23 EILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEA----WSAAELARHRAYLSQQQTPPFAMPVFQyltlHQPDK 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 100 IREGENFDKL--------IMEKLEEMrISHLkdkkiyeiSGGEKQRVALARLL------INkPE--IILLDEPFSALD 161
Cdd:PRK03695 98 TRTEAVASALnevaealgLDDKLGRS-VNQL--------SGGEWQRVRLAAVVlqvwpdIN-PAgqLLLLDEPMNSLD 165
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-161 |
1.01e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGR--VLFDSekkINISPKDRKI------GYLFQDYALFPNMNVYE- 94
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDL---YALSEAERRRllrtewGFVHQHPRDGLRMQVSAg 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 95 -NI-----KVGIREGENFDKLIMEKLEEMRISHLK-DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK11701 110 gNIgerlmAVGARHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-188 |
1.91e-08 |
|
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: 54.26 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGrVLFDSEKKINISPKDR-KIGYLFQDYALFpNMNVYENIKVGIREGENF 106
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSN-KNESEPSFEATRSRNRySVAYAAQKPWLL-NATVEENITFGSPFNKQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 107 DKLIMEKLE---EMRISHLKDK-KIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELE-VGEVLR 177
Cdd:cd03290 110 YKAVTDACSlqpDIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQ 189
|
170
....*....|.
gi 2646445281 178 KYKTPTILVSH 188
Cdd:cd03290 190 DDKRTLVLVTH 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-220 |
2.12e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 19 FEFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRV-----LFDSEKKINISPKDRkigYLFQDYALFpNMNVY 93
Cdd:PLN03232 1258 FVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfgLTDLRRVLSIIPQSP---VLFSGTVRF-NIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 94 EnikvgiregENFDKLIMEKLEEmriSHLKD----------KKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSA 159
Cdd:PLN03232 1334 S---------EHNDADLWEALER---AHIKDvidrnpfgldAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 160 LDDYLKWKIELEVGEvlrKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKN 220
Cdd:PLN03232 1402 VDVRTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-193 |
3.32e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNG----------RVLFDSEK-----------KINISPKDRKI-GYLfQDYa 85
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCGTklevayfdqhRAELDPEKtvmdnlaegkqEVMVNGRPRHVlGYL-QDF- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 86 LFPNMNVYENIKVgiregenfdklimekleemrishlkdkkiyeISGGEKQRVALARLLINKPEIILLDEPFSALDdylk 165
Cdd:PRK11147 428 LFHPKRAMTPVKA-------------------------------LSGGERNRLLLARLFLKPSNLLILDEPTNDLD---- 472
|
170 180 190
....*....|....*....|....*....|..
gi 2646445281 166 wkIE----LEvgEVLRKYKTPTILVSHSREEV 193
Cdd:PRK11147 473 --VEtlelLE--ELLDSYQGTVLLVSHDRQFV 500
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-207 |
4.00e-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: 53.27 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 27 GLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsekkINIS---PKD--RKIGYLFQDYALFPnmnvyenikvG-I 100
Cdd:cd03244 34 GIVGRTGSGKSSLLLALFRLVELSSGSILIDG---------VDISkigLHDlrSRISIIPQDPVLFS----------GtI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 101 RE-----GENFDKLIMEKLEEmriSHLK----------DKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:cd03244 95 RSnldpfGEYSDEELWQALER---VGLKefveslpgglDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 162 DYLkwkiELEVGEVLR-KYKTPTIL-VSHsreevyRL-----CKEICVMSKGK 207
Cdd:cd03244 172 PET----DALIQKTIReAFKDCTVLtIAH------RLdtiidSDRILVLDKGR 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-217 |
5.32e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.25 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSEkkinISPKDRKIGYLFQDYALFpNMNVYENIKVGirEGENFD 107
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT----LASLRNQVALVSQNVHLF-NDTIANNIAYA--RTEQYS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 108 KLIMEKLEEMR-----ISHLK---DKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEv 175
Cdd:PRK11176 447 REQIEEAARMAyamdfINKMDnglDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE- 525
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 176 LRKYKtpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKEL 217
Cdd:PRK11176 526 LQKNR--TSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
8-205 |
5.42e-08 |
|
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: 52.61 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 8 KNFGKFNLRTKFEFDNEIMGLLGASGSGKSLTLKCIAGIEKPDKgriILNGRVLFDSEKKINISPKDRKIGYLFQ----- 82
Cdd:cd03240 7 RNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGEL---PPNSKGGAHDPKLIREGEVRAQVKLAFEnangk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 83 DYALFPNMNVYENIkVGIREGEnFDKLIMEKLEEMrishlkdkkiyeiSGGEKQ------RVALARLLINKPEIILLDEP 156
Cdd:cd03240 84 KYTITRSLAILENV-IFCHQGE-SNWPLLDMRGRC-------------SGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 157 FSALD-DYLKWKIELEVGEVLRKYKTPTILVSHSRE------EVYRLCKEICVMSK 205
Cdd:cd03240 149 TTNLDeENIEESLAEIIEERKSQKNFQLIVITHDEElvdaadHIYRVEKDGRQKSR 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-207 |
6.61e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.06 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFD-SEKKI--NISPKDRKIgYLFqdyalfpNMNVYENIKVG 99
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALrqAISVVSQRV-HLF-------SATLRDNLLLA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 100 IrEGENFDKLImEKLEEMRIS-HLKDKK-----IYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIE 169
Cdd:PRK11160 438 A-PNASDEALI-EVLQQVGLEkLLEDDKglnawLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA----ETE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 170 LEVGEVLRKY---KTpTILVSHsreevyRLC-----KEICVMSKGK 207
Cdd:PRK11160 512 RQILELLAEHaqnKT-VLMITH------RLTgleqfDRICVMDNGQ 550
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-190 |
1.35e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 27 GLLGASGSGKSLTLKCIAGIEKPDKGriilngrvlfdsekKINISPKDRkIGYLFQDYALFPNMNVYENIKVGIRE---- 102
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAG--------------NVSLDPNER-LGKLRQDQFAFEEFTVLDTVIMGHTElwev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 GENFDKLIM--EKLEE--MRISHLKDK-----------------------------KIYEISGGEKQRVALARLLINKPE 149
Cdd:PRK15064 96 KQERDRIYAlpEMSEEdgMKVADLEVKfaemdgytaearagelllgvgipeeqhygLMSEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646445281 150 IILLDEPFSALD-DYLKWkieLEvgEVLRKYKTPTILVSHSR 190
Cdd:PRK15064 176 ILLLDEPTNNLDiNTIRW---LE--DVLNERNSTMIIISHDR 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-194 |
3.88e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 4 VDIEKNFGKFNLRTKFEFD-NEIMGLLGASGSGKSLTLKCIAGIEK--PDKGRIILngrvlfdsekkinispkdrkigyl 80
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEpGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV------------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 fQDYALFPNMNVYENIkvgireGENFDKLimEKLEEMRISHLKDKKIY-----EISGGEKQRVALARLLINKPEIILLDE 155
Cdd:COG2401 92 -PDNQFGREASLIDAI------GRKGDFK--DAVELLNAVGLSDAVLWlrrfkELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646445281 156 PFSALDDYLKWKIELEVGEVLRKYKTPTILVSHsREEVY 194
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATH-HYDVI 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-207 |
5.27e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.47 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrVLFDSEKK------------INIS-PKDRKI----------GY 79
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKNKkktkekekvlekLVIQkTRFKKIkkikeirrrvGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 80 LFQ--DYALFPNmNVYENIKVGIR-------EGENFDKLIMEkLEEMRISHLKdKKIYEISGGEKQRVALARLLINKPEI 150
Cdd:PRK13651 110 VFQfaEYQLFEQ-TIEKDIIFGPVsmgvskeEAKKRAAKYIE-LVGLDESYLQ-RSPFELSGGQKRRVALAGILAMEPDF 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 151 ILLDEPFSALDDYLKWKIeLEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGK 207
Cdd:PRK13651 187 LVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-238 |
5.71e-07 |
|
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: 50.24 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSekkinispkdrkigylfQDYALFPNmNVYENIKVGIREG 103
Cdd:cd03291 64 EMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS-----------------QFSWIMPG-TIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 ENFDKLIME--KLEEmRISHL--KDKKIY-----EISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGE 174
Cdd:cd03291 126 EYRYKSVVKacQLEE-DITKFpeKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVC 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646445281 175 VLRKYKTpTILVShSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSSCLIsGCKNFSEI 238
Cdd:cd03291 205 KLMANKT-RILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLM-GYDTFDQF 265
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
23-195 |
5.88e-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: 48.52 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdsekkINISPkdrkigylfqdyalfpnmnvyenikvgire 102
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------IDGED------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 genfdklIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDY----LKWKIELEVGEVLRK 178
Cdd:smart00382 41 -------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqealLLLLEELRLLLLLKS 113
|
170
....*....|....*..
gi 2646445281 179 YKTPTILVSHSREEVYR 195
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-238 |
8.65e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSekkinispkdrkigylfQDYALFPNmNVYENIKVGIREG 103
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSP-----------------QTSWIMPG-TIKDNIIFGLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 104 E-NFDKLIMEKLEEMRISHL--KDKKIY-----EISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEV 175
Cdd:TIGR01271 515 EyRYTSVIKACQLEEDIALFpeKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646445281 176 LRKYKTpTILVSHSREEVYRLCKeICVMSKGKSEELMKKKELFKNPKTFSSCLIsGCKNFSEI 238
Cdd:TIGR01271 595 LMSNKT-RILVTSKLEHLKKADK-ILLLHEGVCYFYGTFSELQAKRPDFSSLLL-GLEAFDNF 654
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-155 |
9.21e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLFDSekkiNISPKDRKIGYLFQDYALFPnmnvyeniKVGIREG 103
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE----QPEDYRKLFSAVFTDFHLFD--------QLLGPEG 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 104 ENFDKLIMEK-LEEMRISH---LKDKKIYEI--SGGEKQRVALARLLINKPEIILLDE 155
Cdd:PRK10522 418 KPANPALVEKwLERLKMAHkleLEDGRISNLklSKGQKKRLALLLALAEERDILLLDE 475
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-207 |
1.04e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 112 EKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVGEVLRKYKTpTILVSHSRE 191
Cdd:NF000106 127 ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYME 205
|
90
....*....|....*.
gi 2646445281 192 EVYRLCKEICVMSKGK 207
Cdd:NF000106 206 EAEQLAHELTVIDRGR 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-207 |
1.19e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSLTLKCIAGIEKPDkgriILNGRVLFDSEKKINISPKDRK---IGYLFQDYALFPNMN-------V 92
Cdd:CHL00131 33 GEIHAIMGPNGSGKSTLSKVIAGHPAYK----ILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEIPGVSnadflrlA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 YEN--IKVGIREGE--NFDKLIMEKLE--EMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLK 165
Cdd:CHL00131 109 YNSkrKFQGLPELDplEFLEIINEKLKlvGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDiDALK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646445281 166 wkielEVGEVLRKYKTPT---ILVSH-SREEVYRLCKEICVMSKGK 207
Cdd:CHL00131 189 -----IIAEGINKLMTSEnsiILITHyQRLLDYIKPDYVHVMQNGK 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-190 |
1.27e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 26 MGLLGASGSGKSLTLKCIAGIEKPDKGRIILngrvlfdsekkinisPKDRKIGYLFQDYALFpnmnvyenikvgIREGEN 105
Cdd:PRK10636 341 IGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------------AKGIKLGYFAQHQLEF------------LRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 106 ----FDKLIMEKLEEMRISHL-----KDKKIYEI----SGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIELEv 172
Cdd:PRK10636 394 plqhLARLAPQELEQKLRDYLggfgfQGDKVTEEtrrfSGGEKARLVLALIVWQRPNLLLLDEPTNHLD--LDMRQALT- 470
|
170
....*....|....*...
gi 2646445281 173 gEVLRKYKTPTILVSHSR 190
Cdd:PRK10636 471 -EALIDFEGALVVVSHDR 487
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-188 |
1.59e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.75 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKpdkgriILNGRVLFDSEKKINISPKDRKIGY-LFQDYALFPnMNVYENIKVGIRegenf 106
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWP------VYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSSEDMKRRGLS----- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 107 DKLIMEKLEEMRISHLKDKKIY---------EISGGEKQRVALARLLINKPEIILLDEPFSALddylkwKIELE--VGEV 175
Cdd:TIGR00954 551 DKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV------SVDVEgyMYRL 624
|
170
....*....|...
gi 2646445281 176 LRKYKTPTILVSH 188
Cdd:TIGR00954 625 CREFGITLFSVSH 637
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-226 |
2.69e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGRV-----LFDSEKKINISPKDRkigYLFQDyALFPNMNVYenikv 98
Cdd:TIGR00957 1313 EKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakigLHDLRFKITIIPQDP---VLFSG-SLRMNLDPF----- 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 gireGENFDKLIMEKLEemrISHLK-------DKKIYE-------ISGGEKQRVALARLLINKPEIILLDEPFSALDdyl 164
Cdd:TIGR00957 1384 ----SQYSDEEVWWALE---LAHLKtfvsalpDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD--- 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 165 kwkieLEVGEVLR-----KYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTFSS 226
Cdd:TIGR00957 1454 -----LETDNLIQstirtQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
130-219 |
3.48e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 130 ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI-ELEVGEVLRKyKTpTILVS---HSREEVYR--LCKEICVM 203
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRG-KT-RVLVTnqlHFLSQVDRiiLVHEGMIK 818
|
90
....*....|....*.
gi 2646445281 204 SKGKSEELMKKKELFK 219
Cdd:PLN03130 819 EEGTYEELSNNGPLFQ 834
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
120-191 |
3.75e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 3.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 120 SHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDdyLKWKIELEVgeVLRKYKTPTILVSHSRE 191
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLET--YLLKWPKTFIVVSHARE 402
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-220 |
5.12e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNG-----RVLFDSEKKINISPKDRkigYLFQDYALFpNMNVYenikv 98
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskFGLMDLRKVLGIIPQAP---VLFSGTVRF-NLDPF----- 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 99 gireGENFDKLIMEKLEEmriSHLKD----------KKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALD--- 161
Cdd:PLN03130 1337 ----NEHNDADLWESLER---AHLKDvirrnslgldAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrt 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 162 DYLKWKIELEvgevlrKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKN 220
Cdd:PLN03130 1410 DALIQKTIRE------EFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
130-219 |
5.21e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 130 ISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKI-ELEVGEVLRKyKTPTILVS--HSREEVYR--LCKEICVMS 204
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKG-KTRVLVTNqlHFLPLMDRiiLVSEGMIKE 819
|
90
....*....|....*
gi 2646445281 205 KGKSEELMKKKELFK 219
Cdd:PLN03232 820 EGTFAELSKSGSLFK 834
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
3-161 |
8.19e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 3 YVDIEKNFGKFNLRTKF-EF-DNEIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdsekkINISPKDRKIgyl 80
Cdd:cd03222 3 YPDCVKRYGVFFLLVELgVVkEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG---------ITPVYKPQYI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 81 fqdyalfpnmnvyenikvgiregenfdklimekleemrishlkdkkiyEISGGEKQRVALARLLINKPEIILLDEPFSAL 160
Cdd:cd03222 71 ------------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYL 102
|
.
gi 2646445281 161 D 161
Cdd:cd03222 103 D 103
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-161 |
9.80e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIIlngrvlfdsekkinispKDRKIGYLFQDyALFPNMNVYENIKVgiregenFD 107
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVW-----------------AERSIAYVPQQ-AWIMNATVRGNILF-------FD 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646445281 108 KLIMEKLEE-MRISHLK----------DKKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PTZ00243 746 EEDAARLADaVRVSQLEadlaqlggglETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
130-206 |
1.34e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.63 E-value: 1.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646445281 130 ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEVGEVLRKY-KTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDG----RTEHQILHNLRQWgEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-186 |
1.39e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.63 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGIEKPDKGRIILNGRVLfdseKKINISPKDRKIGYLFQDYALFPNmNVYENIKVG--IREGEN 105
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----SSLSHSVLRQGVAMVQQDPVVLAD-TFLANVTLGrdISEEQV 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 106 FDKLIMEKLEEMrISHLKD---KKIYE----ISGGEKQRVALARLLINKPEIILLDEPFSALDDylkwKIELEVGEVLRK 178
Cdd:PRK10790 447 WQALETVQLAEL-ARSLPDglyTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDS----GTEQAIQQALAA 521
|
....*...
gi 2646445281 179 YKTPTILV 186
Cdd:PRK10790 522 VREHTTLV 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-168 |
1.70e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAgiEKPDKGrIILNGRVLfdsekkINISPKD----RKIGYLFQDYALFPNMNVYENI--- 96
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRL------VNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLrfs 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 -------KVGIREGENF-DKLImeKLEEMRisHLKDKKIYEISGG----EKQRVALARLLINKPEIIL-LDEPFSALDDY 163
Cdd:TIGR00956 861 aylrqpkSVSKSEKMEYvEEVI--KLLEME--SYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
....*
gi 2646445281 164 LKWKI 168
Cdd:TIGR00956 937 TAWSI 941
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
115-161 |
2.67e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 2.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2646445281 115 EEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PRK10938 121 QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-191 |
6.34e-05 |
|
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: 43.08 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 23 NEIMGLLGASGSGKSlTLkCIAGIEKPDKGRIIlNGRVLFDSEKKINISpkdrKIGYLfqdyalfpnmnvyenIKVGire 102
Cdd:cd03238 21 NVLVVVTGVSGSGKS-TL-VNEGLYASGKARLI-SFLPKFSRNKLIFID----QLQFL---------------IDVG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 103 genfdklimekLEEMRIshlkDKKIYEISGGEKQRVALARLLINKPE--IILLDEPFSALDDYLKWKIeLEVGEVLRKYK 180
Cdd:cd03238 76 -----------LGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL-LEVIKGLIDLG 139
|
170
....*....|.
gi 2646445281 181 TPTILVSHSRE 191
Cdd:cd03238 140 NTVILIEHNLD 150
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
128-219 |
1.02e-04 |
|
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: 43.30 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 128 YEISGGEKQRVALARLLINKPEIILLDEPfSALDDYLKWKIeleVGEVLRK-YKTPTILVSHSREEVYRLCKEICVMSKG 206
Cdd:cd03289 137 CVLSHGHKQLMCLARSVLSKAKILLLDEP-SAHLDPITYQV---IRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEEN 212
|
90
....*....|....*....
gi 2646445281 207 KS------EELMKKKELFK 219
Cdd:cd03289 213 KVrqydsiQKLLNEKSHFK 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-224 |
1.55e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 19 FEFDN-EIMGLLGASGSGKSLTLKCIAGIEKPDKGRIILNGrvlfdSEKKINISPkdrkigylfqdyALFPNMNVYENIK 97
Cdd:PRK13545 45 FEVPEgEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----SAALIAISS------------GLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 98 V-GIREG---ENFDKLIMEKLEEMRISHLKDKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLKWKIELEVG 173
Cdd:PRK13545 108 LkGLMMGltkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 174 EVLRKYKTpTILVSHSREEVYRLCKEICVMSKGKSEELMKKKELFKNPKTF 224
Cdd:PRK13545 188 EFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-188 |
1.98e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGIEKPDkgriILNGRVLFDSEKKINISPKDRK---IGYLFQDYALFPN------MNVYE 94
Cdd:PRK09580 28 EVHAIMGPNGSGKSTLSATLAGREDYE----VTGGTVEFKGKDLLELSPEDRAgegIFMAFQYPVEIPGvsnqffLQTAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 95 NIKVGIREGENFDKLIMEKLEEMRISHLK------DKKIYE-ISGGEKQRVALARLLINKPEIILLDEPFSALD-DYLkw 166
Cdd:PRK09580 104 NAVRSYRGQEPLDRFDFQDLMEEKIALLKmpedllTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDiDAL-- 181
|
170 180
....*....|....*....|..
gi 2646445281 167 KIELEVGEVLRKYKTPTILVSH 188
Cdd:PRK09580 182 KIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
131-191 |
2.74e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 2.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646445281 131 SGGEKQRVALARLLINKPEIILLDEPFSALD-DYLKWkieLEvgEVLRKYKTPTILVSHSRE 191
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDlDAVIW---LE--KWLKSYQGTLILISHDRD 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-219 |
3.72e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.59 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 26 MGLLGASGSGKSLTLKCIAGIEKPDkGRIILNGrVLFDSekkINISPKDRKIGYLFQDYALFP-----NMNVYENI---- 96
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG-VSWNS---VTLQTWRKAFGVIPQKVFIFSgtfrkNLDPYEQWsdee 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 97 ------KVGIREgenfdklIMEKLEEMRISHLKDKKiYEISGGEKQRVALARLLINKPEIILLDEPFSALDdylkwKIEL 170
Cdd:TIGR01271 1323 iwkvaeEVGLKS-------VIEQFPDKLDFVLVDGG-YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-----PVTL 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 171 evgEVLRK-----YKTPTILVSHSREEVYRLCKEICVMSKGKS------EELMKKKELFK 219
Cdd:TIGR01271 1390 ---QIIRKtlkqsFSNCTVILSEHRVEALLECQQFLVIEGSSVkqydsiQKLLNETSLFK 1446
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-161 |
3.75e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 28 LLGASGSGKSLTLKCIAGieKPDKGRIilngrvlfdsEKKINIS--PKD-----RKIGYLFQDYALFPNMNVYENI---- 96
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAG--RKTGGYI----------EGDIRISgfPKKqetfaRISGYCEQNDIHSPQVTVRESLiysa 978
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646445281 97 ------KVGIREGENFDKLIMEKLEemrISHLKDK-----KIYEISGGEKQRVALARLLINKPEIILLDEPFSALD 161
Cdd:PLN03140 979 flrlpkEVSKEEKMMFVDEVMELVE---LDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
8-162 |
2.19e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 8 KNFGKFNLRTKFEFDNEIMGLLGASGSGKS---------LTLKCIAGIEKPD--------KGRIIL----NGRVL----F 62
Cdd:COG0419 8 ENFRSYRDTETIDFDDGLNLIVGPNGAGKStileairyaLYGKARSRSKLRSdlinvgseEASVELefehGGKRYrierR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 63 DSE--KKINISPKDRK--IGYLFQDYALFPNMNVYENIKVGIREGENfDKLIMEKLEEMRISHLKDKKIYE-ISGGEKQR 137
Cdd:COG0419 88 QGEfaEFLEAKPSERKeaLKRLLGLEIYEELKERLKELEEALESALE-ELAELQKLKQEILAQLSGLDPIEtLSGGERLR 166
|
170 180
....*....|....*....|....*
gi 2646445281 138 VALARLLinkpeIILLDepFSALDD 162
Cdd:COG0419 167 LALADLL-----SLILD--FGSLDE 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-216 |
2.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 24 EIMGLLGASGSGKSLTLKCIAGI------EkpdkGRIILNGRV-----LFDSEKkinispkdRKIGYLFQDYALFPNMNV 92
Cdd:NF040905 28 EIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVcrfkdIRDSEA--------LGIVIIHQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646445281 93 YENIKVGIREGE----NFDKLIMEKLEEMRISHLK---DKKIYEISGGEKQRVALARLLINKPEIILLDEPFSALDDYLK 165
Cdd:NF040905 96 AENIFLGNERAKrgviDWNETNRRARELLAKVGLDespDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646445281 166 WKIeLEVGEVLRKYKTPTILVSHSREEVYRLCKEICVMSKGKSEELMKKKE 216
Cdd:NF040905 176 AAL-LDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
130-188 |
7.99e-03 |
|
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: 36.57 E-value: 7.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646445281 130 ISGGEKQRVALARLLIN---KPE-IILLDEPFSALDDY----LKWKIELevgevLRKYKTPTILVSH 188
Cdd:cd03227 78 LSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRdgqaLAEAILE-----HLVKGAQVIVITH 139
|
|
| |
