|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-245 |
7.64e-125 |
|
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: 364.22 E-value: 7.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT---RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGF 77
Cdd:COG1123 260 LLEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVFQDPMGSLDPRMRVRDIISEPL---GRRDPA----RVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLrlhGLLSRAerreRVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHE 230
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
250
....*....|....*
gi 1039688293 231 YTRELLAAAPNLRAE 245
Cdd:COG1123 500 YTRALLAAVPSLDPA 514
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-251 |
1.12e-123 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 354.81 E-value: 1.12e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY---------TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPE 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 RELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPL---------GRRDpaRVSELLEAVGLPADAAGRYPHQFSGGQRQR 143
Cdd:COG4608 88 RELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLrihglaskaERRE--RVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
250 260 270
....*....|....*....|....*....|..
gi 1039688293 224 YDAPEHEYTRELLAAAP----NLRAELARLRG 251
Cdd:COG4608 246 YARPLHPYTQALLSAVPvpdpERRRERIVLEG 277
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-250 |
3.67e-122 |
|
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: 350.51 E-value: 3.67e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT--RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKP---TAGSVSFQGKRIDTLPEREL 75
Cdd:COG0444 1 LLEVRNLKVYFPtrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLR-SELQIVFQDPMGSLDPRMRVRDIISEPL------GRRDP-ARVSELLEAVGL--PADAAGRYPHQFSGGQRQRIS 145
Cdd:COG0444 81 RKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLrihgglSKAEArERAIELLERVGLpdPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260
....*....|....*....|....*
gi 1039688293 226 APEHEYTRELLAAAPNLRAELARLR 250
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLI 265
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-243 |
1.21e-118 |
|
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: 348.98 E-value: 1.21e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY---------TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDkPTAGSVSFQGKRIDTLPE 72
Cdd:COG4172 276 LEARDLKVWFpikrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 RELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPLG----------RRdpARVSELLEAVGLPADAAGRYPHQFSGGQRQ 142
Cdd:COG4172 355 RALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRvhgpglsaaeRR--ARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDR 222
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
250 260
....*....|....*....|.
gi 1039688293 223 VYDAPEHEYTRELLAAAPNLR 243
Cdd:COG4172 513 VFDAPQHPYTRALLAAAPLLE 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-245 |
4.00e-113 |
|
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: 324.83 E-value: 4.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY--TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKridTLPERELGFL 78
Cdd:COG1124 1 MLEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDPMGSLDPRMRVRDIISEPL---GRRD-PARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:COG1124 78 RRRVQMVFQDPYASLHPRHTVDRILAEPLrihGLPDrEERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRE 234
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRE 237
|
250
....*....|.
gi 1039688293 235 LLAAAPNLRAE 245
Cdd:COG1124 238 LLAASLAFERA 248
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
9.09e-108 |
|
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: 310.59 E-value: 9.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDPMGSLDPRMRVRDIISEPL---GRRDPA-----RVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLrihGKLSKKearkeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-250 |
2.25e-97 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 288.02 E-value: 2.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYT--------RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPER 73
Cdd:PRK11308 6 LQAIDLKKHYPvkrglfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 74 ELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPLG---------RRdpARVSELLEAVGLPADAAGRYPHQFSGGQRQRI 144
Cdd:PRK11308 86 AQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLintslsaaeRR--EKALAMMAKVGLRPEHYDRYPHMFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
250 260
....*....|....*....|....*.
gi 1039688293 225 DAPEHEYTRELLAAAPNLRAELARLR 250
Cdd:PRK11308 244 NNPRHPYTQALLSATPRLNPDDRRER 269
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-244 |
3.04e-92 |
|
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: 281.57 E-value: 3.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKS----TLVRLLAALDKPTAGSVSFQGKRIDTLPERE 74
Cdd:COG4172 6 LLSVEDLSVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 75 LGFLR-SELQIVFQDPMGSLDPRMRVRDIISEPL-------GRRDPARVSELLEAVGLPADA--AGRYPHQFSGGQRQRI 144
Cdd:COG4172 86 LRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLrlhrglsGAAARARALELLERVGIPDPErrLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250 260
....*....|....*....|
gi 1039688293 225 DAPEHEYTRELLAAAPNLRA 244
Cdd:COG4172 246 AAPQHPYTRKLLAAEPRGDP 265
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-240 |
4.52e-84 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 254.25 E-value: 4.52e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD-----------VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDT 69
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 70 LPERELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPLGRRDPA--------RVSELLEAVGLPADAAGRYPHQFSGGQR 141
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlsrqevkdRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVD 221
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250
....*....|....*....
gi 1039688293 222 RVYDAPEHEYTRELLAAAP 240
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVP 266
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-255 |
2.05e-83 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 252.69 E-value: 2.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT--RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:COG1135 1 MIELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDPmgSLDPRMRVRDIISEPL-------GRRDpARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA 151
Cdd:COG1135 81 RRKIGMIFQHF--NLLSSRTVAENVALPLeiagvpkAEIR-KRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEY 231
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSEL 236
|
250 260
....*....|....*....|....*..
gi 1039688293 232 TRELLAAAPNLR---AELARLRGGDDG 255
Cdd:COG1135 237 TRRFLPTVLNDElpeELLARLREAAGG 263
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-238 |
9.71e-80 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 240.89 E-value: 9.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYT-------RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTlpeRE 74
Cdd:COG4167 5 LEVRNLSKTFKyrtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY---GD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 75 LGFLRSELQIVFQDPMGSLDPRMRVRDIISEPL---------GRRDpaRVSELLEAVGLPADAAGRYPHQFSGGQRQRIS 145
Cdd:COG4167 82 YKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLrlntdltaeEREE--RIFATLRLVGLLPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|...
gi 1039688293 226 APEHEYTRELLAA 238
Cdd:COG4167 240 NPQHEVTKRLIES 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
1.63e-78 |
|
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: 236.71 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY--TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:cd03258 1 MIELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDpMGSLDPRmRVRDIISEPL------GRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSR-TVFENVALPLeiagvpKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-240 |
1.86e-77 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 245.54 E-value: 1.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY---------TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP 71
Cdd:PRK10261 313 ILQVRNLVTRFplrsgllnrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 72 ERELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPL-------GRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRI 144
Cdd:PRK10261 393 PGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLrvhgllpGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
250
....*....|....*.
gi 1039688293 225 DAPEHEYTRELLAAAP 240
Cdd:PRK10261 553 ENPQHPYTRKLMAAVP 568
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-250 |
3.04e-75 |
|
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: 237.11 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTA---GSVSFQGKRIDTLPERELGf 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 lrSELQIVFQDPMGSLDPrMRVRDIISEPLGRRD------PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA 151
Cdd:COG1123 83 --RRIGMVFQDPMTQLNP-VTVGDQIAEALENLGlsraeaRARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPehey 231
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP---- 234
|
250
....*....|....*....
gi 1039688293 232 trELLAAAPNLRAELARLR 250
Cdd:COG1123 235 --QALAAVPRLGAARGRAA 251
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-249 |
4.13e-72 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 223.45 E-value: 4.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKS----TLVRLLAAlDKPTAGSVSFQGKRIDTLPERE 74
Cdd:PRK09473 12 LLDVKDLRVTFSTPDgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 75 LGFLRSElQI--VFQDPMGSLDPRMRVRDIISEPL------GRRDPARVS-ELLEAVGLPaDAAGR---YPHQFSGGQRQ 142
Cdd:PRK09473 91 LNKLRAE-QIsmIFQDPMTSLNPYMRVGEQLMEVLmlhkgmSKAEAFEESvRMLDAVKMP-EARKRmkmYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDR 222
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260
....*....|....*....|....*..
gi 1039688293 223 VYDAPEHEYTRELLAAAPNLRAELARL 249
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEGESL 275
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-239 |
6.92e-72 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 228.82 E-value: 6.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLE------RRYTRRDV---HALRGVSFDVEAGQRFGIVGESGSGKST----LVRLLAAldkptAGSVSFQGKRI 67
Cdd:PRK15134 275 LLDVEQLQvafpirKGILKRTVdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 68 DTLPERELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPLGRRDP--------ARVSELLEAVGLPADAAGRYPHQFSGG 139
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtlsaaqreQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 140 QRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGD 219
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250 260
....*....|....*....|
gi 1039688293 220 VDRVYDAPEHEYTRELLAAA 239
Cdd:PRK15134 510 CERVFAAPQQEYTRQLLALS 529
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-239 |
1.05e-70 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 220.44 E-value: 1.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT--RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:PRK11153 1 MIELKNISKVFPqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDpMGSLDPRMrVRDIISEPL-----GRRD-PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:PRK11153 81 RRQIGMIFQH-FNLLSSRT-VFDNVALPLelagtPKAEiKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYT 232
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
....*..
gi 1039688293 233 RELLAAA 239
Cdd:PRK11153 238 REFIQST 244
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
1.60e-70 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 216.06 E-value: 1.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:COG1136 4 LLELRNLTKSYGTGEgeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSE-LQIVFQDPmgSLDPRMRVRDIISEPL------GRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA 151
Cdd:COG1136 84 RRRhIGFVFQFF--NLLPELTALENVALPLllagvsRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVE 216
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
7.90e-68 |
|
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: 208.88 E-value: 7.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLR 79
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 SE-LQIVFQDPmgSLDPRMRVRD------IISEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:cd03255 81 RRhIGFVFQSF--NLLPDLTALEnvelplLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEI 214
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
3.79e-66 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 208.85 E-value: 3.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDT-LP--ERELGFl 78
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPprERRVGF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselqiVFQDPMgsLDPRMRVRDIISEPLGRRDP------ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:COG1118 80 ------VFQHYA--LFPHMTVAENIAFGLRVRPPskaeirARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYT 232
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
....
gi 1039688293 233 RELL 236
Cdd:COG1118 231 ARFL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-237 |
2.80e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 200.61 E-value: 2.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdTLPERELGFLRS 80
Cdd:COG1126 1 MIEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPmgSLDPRMRVRDIISEPL---GRRDPA----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:COG1126 78 KVGMVFQQF--NLFPHLTVLENVTLAPikvKKMSKAeaeeRAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTR 233
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTR 233
|
....
gi 1039688293 234 ELLA 237
Cdd:COG1126 234 AFLS 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
2.21e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 201.87 E-value: 2.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGfl 78
Cdd:COG3842 5 ALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpeKRNVG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselqIVFQDPmgSLDPRMRVRDIISEPLGRRDP------ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:COG3842 81 -----MVFQDY--ALFPHLTVAENVAFGLRMRGVpkaeirARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHD----LGvvrhVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPEEIYERPA 228
|
...
gi 1039688293 229 HEY 231
Cdd:COG3842 229 TRF 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-238 |
1.33e-62 |
|
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: 197.34 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY-------TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPER 73
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 74 ELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPL-------GRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISI 146
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLrhltsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVyDA 226
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL-LS 240
|
250
....*....|..
gi 1039688293 227 PEHEYTRELLAA 238
Cdd:TIGR02769 241 FKHPAGRNLQSA 252
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
2.87e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 195.28 E-value: 2.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgfLRSE 81
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPmgSLDPRMRVRDIISE-----PLGRRD-PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:COG1131 75 IGYVPQEP--ALYPDLTVRENLRFfarlyGLPRKEaRERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVD 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-254 |
1.37e-61 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 194.52 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHA-------LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPER 73
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 74 ELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPL-------GRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISI 146
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLrhllsldKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE---LGDVDRV 223
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKLTF 242
|
250 260 270
....*....|....*....|....*....|.
gi 1039688293 224 ydapEHEYTRELLAAApnLRAELARLRGGDD 254
Cdd:PRK10419 243 ----SSPAGRVLQNAV--LPAFPVRRRTTEK 267
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-248 |
1.19e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 191.84 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRR--DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdTLPERELGFl 78
Cdd:COG1116 7 ALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-TGPGPDRGV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselqiVFQDPmgSLDPRMRVRDIISEPLGRRD------PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:COG1116 85 ------VFQEP--ALLPWLTVLDNVALGLELRGvpkaerRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLG-VVRhVCDRVAVMRR--GEIVELGDVD-------R 222
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSArpGRIVEEIDVDlprprdrE 234
|
250 260
....*....|....*....|....*..
gi 1039688293 223 VYDAPE-HEYTRELLAAapnLRAELAR 248
Cdd:COG1116 235 LRTSPEfAALRAEILDL---LREEAER 258
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
1.21e-60 |
|
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: 190.42 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGFlr 79
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpeRRNIGM-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqiVFQDPmgSLDPRMRVRDIISEPLGRRDP------ARVSELLEAVGLPADAaGRYPHQFSGGQRQRISIARALAPN 153
Cdd:cd03259 77 -----VFQDY--ALFPHLTVAENIAFGLKLRGVpkaeirARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-238 |
3.95e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 190.27 E-value: 3.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:COG3638 2 MLELRNLSKRY-PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPmgSLDPRMRVRD-IISEPLGRR-------------DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISI 146
Cdd:COG3638 81 RIGMIFQQF--NLVPRLSVLTnVLAGRLGRTstwrsllglfppeDRERALEALERVGL-ADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIvelgdvdrVYDA 226
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDG 229
|
250
....*....|..
gi 1039688293 227 PEHEYTRELLAA 238
Cdd:COG3638 230 PPAELTDAVLRE 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
7.96e-60 |
|
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: 189.03 E-value: 7.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHalRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDpmGSLDPRMRVRDIISEPL---GRRDPA----RVSELLEAVGLPaDAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:COG1127 83 RIGMLFQG--GALFDSLTVFENVAFPLrehTDLSEAeireLVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALD-VSVRKqILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDApEHEYT 232
Cdd:COG1127 160 PEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS-DDPWV 237
|
....
gi 1039688293 233 RELL 236
Cdd:COG1127 238 RQFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-221 |
8.12e-60 |
|
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: 188.45 E-value: 8.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY--TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTlPERELGFlr 79
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqiVFQDPmgSLDPRMRVRDIISEPLGRRDP------ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:cd03293 78 -----VFQQD--ALLPWLTVLDNVALGLELQGVpkaearERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVM--RRGEIVELGDVD 221
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
1.53e-59 |
|
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: 187.92 E-value: 1.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP-----MGSldprmrVRDIIS---EPLGRRDP---ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG1122 77 VGLVFQNPddqlfAPT------VEEDVAfgpENLGLPREeirERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
3.89e-58 |
|
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: 185.25 E-value: 3.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:COG1120 1 MLEAENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 elqIVFQDPmgSLDPRMRVRDIIS----------EPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG1120 79 ---YVPQEP--PAPFGLTVRELVAlgryphlglfGRPSAEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVydapehe 230
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV------- 225
|
250
....*....|....*
gi 1039688293 231 YTRELLAAAPNLRAE 245
Cdd:COG1120 226 LTPELLEEVYGVEAR 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-216 |
1.97e-57 |
|
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: 182.63 E-value: 1.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:COG4181 8 IIELRGLTKTVGTGAgeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSE-LQIVFQDPMgsLDPRMRVRDIISEPL---GRRDP-ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:COG4181 88 RARhVGFVFQSFQ--LLPTLTALENVMLPLelaGRRDArARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVE 216
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
6.05e-57 |
|
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: 179.69 E-value: 6.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLpERELGFLRSE 81
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPmgSLDPRMRVRDIISEPLgrrdparvselleavglpadaagryphqfSGGQRQRISIARALAPNPSVLIADE 161
Cdd:cd03229 78 IGMVFQDF--ALFPHLTVLENIALGL-----------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 162 PVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGE 213
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-227 |
2.23e-56 |
|
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: 180.23 E-value: 2.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGFlr 79
Cdd:cd03296 3 IEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqERNVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqiVFQDPmgSLDPRMRVRDIIS-----EPLGRRDP-----ARVSELLEAVGLPAdAAGRYPHQFSGGQRQRISIARA 149
Cdd:cd03296 79 -----VFQHY--ALFRHMTVFDNVAfglrvKPRSERPPeaeirAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 150 LAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-238 |
2.83e-56 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 181.14 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLER--RYT-----RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRidtLPER 73
Cdd:PRK15112 4 LLEVRNLSKtfRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 74 ELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPL-------GRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISI 146
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLrlntdlePEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|..
gi 1039688293 227 PEHEYTRELLAA 238
Cdd:PRK15112 241 PLHELTKRLIAG 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-235 |
3.36e-56 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 180.51 E-value: 3.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK-----RIDTLPEREL 75
Cdd:PRK11701 6 LLSVRGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFL-RSELQIVFQDPMGSLdpRMRVR--DIISEPL---GRRDPARV----SELLEAVGLPADAAGRYPHQFSGGQRQRIS 145
Cdd:PRK11701 84 RRLlRTEWGFVHQHPRDGL--RMQVSagGNIGERLmavGARHYGDIrataGDWLERVEIDAARIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLD 241
|
250
....*....|
gi 1039688293 226 APEHEYTREL 235
Cdd:PRK11701 242 DPQHPYTQLL 251
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-221 |
5.50e-56 |
|
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: 179.23 E-value: 5.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSE 81
Cdd:cd03261 1 IELRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpmGSLDPRMRVRDIISEPL---GRRDPARVSEL----LEAVGLPaDAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:cd03261 79 MGMLFQS--GALFDSLTVFENVAFPLrehTRLSEEEIREIvlekLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVD 221
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
2.66e-54 |
|
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: 174.25 E-value: 2.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdTLPERELGFLRSE 81
Cdd:cd03262 1 IEIKNLHKSFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpmGSLDPRMRVRDIISEPL----GRRDP---ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:cd03262 78 VGMVFQQ--FNLFPHLTVLENITLAPikvkGMSKAeaeERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
4.59e-54 |
|
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: 173.42 E-value: 4.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSEL 82
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 QIVFQDP-----MgsldprMRVRDIIS---EPLGR---RDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA 151
Cdd:cd03225 78 GLVFQNPddqffG------PTVEEEVAfglENLGLpeeEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGE 213
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-228 |
6.32e-54 |
|
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: 173.96 E-value: 6.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGflr 79
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPphKRPVN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqIVFQDPmgSLDPRMRVRDIISEPLGRRD------PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:cd03300 76 ----TVFQNY--ALFPHLTVFENIAFGLRLKKlpkaeiKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
8.43e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 173.89 E-value: 8.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgfLRS 80
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMgsLDPRMRVRDII------SEPLGRRDPARVSELLEAVGLPADAAGRYpHQFSGGQRQRISIARALAPNP 154
Cdd:COG4555 75 QIGVLPDERG--LYDRLTVRENIryfaelYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-240 |
1.99e-53 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 180.67 E-value: 1.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 21 GVSFDVEAGQRFGIVGESGSGKS-TLVRLLAALDKP----TAGSVSFQGKRIDTLPERELGFLR-SELQIVFQDPMGSLD 94
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 95 PRMRVRDIISEPLG-----RRDPARVSEL--LEAVGLpADAAGR---YPHQFSGGQRQRISIARALAPNPSVLIADEPVS 164
Cdd:PRK15134 107 PLHTLEKQLYEVLSlhrgmRREAARGEILncLDRVGI-RQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 165 ALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRELLAAAP 240
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEP 261
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-238 |
2.37e-53 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 172.68 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGFlr 79
Cdd:TIGR00968 1 IEIANISKRFG--SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHarDRKIGF-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqiVFQDPmgSLDPRMRVRDIISEPLGRRDP------ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:TIGR00968 77 -----VFQHY--ALFKHLTVRDNIAFGLEIRKHpkakikARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTR 233
Cdd:TIGR00968 149 PQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVM 228
|
....*
gi 1039688293 234 ELLAA 238
Cdd:TIGR00968 229 SFLGE 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-249 |
3.22e-53 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 174.93 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKS-TLVRLLAALDKP---TAGSVSFQGKRIDTLPERE-LGFLRSELQIVFQDPMGS 92
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKErRNLVGAEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 93 LDPRMRVRDIISEPL---------GRRDpaRVSELLEAVGLPaDAAGR---YPHQFSGGQRQRISIARALAPNPSVLIAD 160
Cdd:PRK11022 102 LNPCYTVGFQIMEAIkvhqggnkkTRRQ--RAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 161 EPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRELLAAAP 240
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP 258
|
....*....
gi 1039688293 241 NLRAELARL 249
Cdd:PRK11022 259 EFAQDKARL 267
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
4.61e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.77 E-value: 4.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRSE 81
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP-MGsldpRMRVRDIISEPLGRR----DPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSV 156
Cdd:COG4619 76 VAYVPQEPaLW----GGTVRDNLPFPFQLRerkfDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
4.99e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 171.00 E-value: 4.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:COG2884 1 MIRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDpmGSLDPRMRVRDIISEPL---GRRDP---ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:COG2884 80 RIGVVFQD--FRLLPDRTVYENVALPLrvtGKSRKeirRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE 216
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-239 |
1.39e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.65 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPEReLGFL-- 78
Cdd:COG1121 6 AIELENLTVSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-IGYVpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFqdpmgsldPrMRVRDIIS----------EPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIAR 148
Cdd:COG1121 83 RAEVDWDF--------P-ITVRDVVLmgrygrrglfRRPSRADREAVDEALERVGL-EDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGeIVELGDVDRVydape 228
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEV----- 225
|
250
....*....|.
gi 1039688293 229 heYTRELLAAA 239
Cdd:COG1121 226 --LTPENLSRA 234
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-253 |
6.26e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 171.04 E-value: 6.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRs 80
Cdd:COG1125 1 MIEFENVTKRY-PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---R- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 eLQI--VFQDpmGSLDPRMRVRD---IISEPLG---RRDPARVSELLEAVGLPADA-AGRYPHQFSGGQRQRISIARALA 151
Cdd:COG1125 76 -RRIgyVIQQ--IGLFPHMTVAEniaTVPRLLGwdkERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHD------LGvvrhvcDRVAVMRRGEIVELGDVDRVYD 225
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidealkLG------DRIAVMREGRIVQYDTPEEILA 226
|
250 260
....*....|....*....|....*...
gi 1039688293 226 APEHEYTRELLAAAPNLRAeLARLRGGD 253
Cdd:COG1125 227 NPANDFVADFVGADRGLRR-LSLLRVED 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
6.49e-52 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 172.18 E-value: 6.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGFl 78
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPpkDRNIAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselqiVFQDPMgsLDPRMRVRDIISEPLG-RRDP-----ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:COG3839 80 ------VFQSYA--LYPHMTVYENIAFPLKlRKVPkaeidRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALD----VSVRKQILDLLASLvelySLTLVFVSHD------LGvvrhvcDRVAVMRRGEIVELGDVDR 222
Cdd:COG3839 151 EPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL----GTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGTPEE 220
|
....*....
gi 1039688293 223 VYDAPEHEY 231
Cdd:COG3839 221 LYDRPANLF 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
6.64e-52 |
|
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: 166.42 E-value: 6.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgfLRSE 81
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE----VKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPmgSLDPRMRVRDIIseplgrrdparvselleavglpadaagryphQFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:cd03230 75 IGYLPEEP--SLYENLTVRENL-------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 162 PVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
1.57e-51 |
|
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: 169.17 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY---TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:TIGR04521 1 IKLKNVSYIYqpgTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDPMGSLDPRMRVRDIISEP--LGRRD---PARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:TIGR04521 81 RKKVGLVFQFPEHQLFEETVYKDIAFGPknLGLSEeeaEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-234 |
1.99e-51 |
|
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: 168.59 E-value: 1.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 4 VRDLERRYTRRDVH-------ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELG 76
Cdd:cd03294 18 FKLLAKGKSKEEILkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 FLRSE-LQIVFQDpMGsLDPRMRVRDIISEPLG--------RRdpARVSELLEAVGLPADAAgRYPHQFSGGQRQRISIA 147
Cdd:cd03294 98 ELRRKkISMVFQS-FA-LLPHRTVLENVAFGLEvqgvpraeRE--ERAAEALELVGLEGWEH-KYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
....*..
gi 1039688293 228 EHEYTRE 234
Cdd:cd03294 253 ANDYVRE 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-244 |
2.14e-50 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 174.27 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 13 RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQG-------KRIDTLPERELGFLR----SE 81
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQMRhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMGSLDPRMRVRDIISEP------LGRRDP-ARVSELLEAVGLPADAA--GRYPHQFSGGQRQRISIARALAP 152
Cdd:PRK10261 106 MAMIFQEPMTSLNPVFTVGEQIAESirlhqgASREEAmVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYT 232
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265
|
250
....*....|..
gi 1039688293 233 RELLAAAPNLRA 244
Cdd:PRK10261 266 RALLAAVPQLGA 277
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-230 |
3.48e-50 |
|
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: 164.66 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSE 81
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPmgSLDPRMRV-RDIISEPLGRR-------------DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIA 147
Cdd:cd03256 80 IGMIFQQF--NLIERLSVlENVLSGRLGRRstwrslfglfpkeEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
...
gi 1039688293 228 EHE 230
Cdd:cd03256 237 LDE 239
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-216 |
1.45e-49 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 162.14 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTR--RDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:TIGR02211 1 LLKCENLGKRYQEgkLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RS-ELQIVFQdpMGSLDPRMRVRDIISEPL--GRRDPA----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA 151
Cdd:TIGR02211 81 RNkKLGFIYQ--FHHLLPDFTALENVAMPLliGKKSVKeakeRAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVE 216
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
1.69e-49 |
|
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: 163.37 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkrIDTLPERELGFLRSE 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP----MGSLdprmrVRDIIS---EPLG------RRdpaRVSELLEAVGLpADAAGRYPHQFSGGQRQRISIAR 148
Cdd:TIGR04520 79 VGMVFQNPdnqfVGAT-----VEDDVAfglENLGvpreemRK---RVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEG 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-231 |
1.88e-49 |
|
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: 172.71 E-value: 1.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIISepLGRRDP--ARVSELLEAVGLpADAAGRYPH-----------QFSGGQRQRIS 145
Cdd:COG2274 551 IGVVLQDVFlfsGT------IRENIT--LGDPDAtdEEIIEAARLAGL-HDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLveLYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLA 698
|
....*.
gi 1039688293 226 APEHEY 231
Cdd:COG2274 699 RKGLYA 704
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-247 |
4.50e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 164.31 E-value: 4.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKP----TAGSVSFQGkrIDTL---PERELGFLRSELQIVFQD 88
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNG--IDLLklsPRERRKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 89 PMGSLDPRMRVRDIISEPLGRRD------------PARVSELLEAVGL--PADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:COG4170 98 PSSCLDPSAKIGDQLIEAIPSWTfkgkwwqrfkwrKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRE 234
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257
|
250
....*....|...
gi 1039688293 235 LLAAAPNLRAELA 247
Cdd:COG4170 258 LLRSMPDFRQPLP 270
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
1.46e-48 |
|
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: 160.54 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRSE 81
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpMGsLDPRMRVRDIIS-------EPLGRRDpARVSELLEAVGL-PADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:cd03295 77 IGYVIQQ-IG-LFPHMTVEENIAlvpkllkWPKEKIR-ERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTR 233
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
....*
gi 1039688293 234 ELLAA 238
Cdd:cd03295 234 EFVGA 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
6.05e-48 |
|
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: 158.11 E-value: 6.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAL-----DKPTAGSVSFQGKRIDTLPERELG 76
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 fLRSELQIVFQDPMgsldP-RMRVRDIISEPL---GRRD----PARVSELLEAVGLPADAAGR-YPHQFSGGQRQRISIA 147
Cdd:cd03260 79 -LRRRVGMVFQKPN----PfPGSIYDNVAYGLrlhGIKLkeelDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYslTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
5.12e-47 |
|
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: 154.52 E-value: 5.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflrsel 82
Cdd:cd03214 1 EVENLSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 qivfqdpmgsldprmrvrdiiseplgRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEP 162
Cdd:cd03214 72 --------------------------ARKIAYVPQALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 163 VSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-223 |
1.68e-46 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 155.58 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERE---LGF 77
Cdd:COG0411 4 LLEVRGLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSelqivFQDPmgSLDPRMRVRD-----------------IISEPLGRRDP----ARVSELLEAVGLpADAAGRYPHQF 136
Cdd:COG0411 82 ART-----FQNP--RLFPELTVLEnvlvaaharlgrgllaaLLRLPRARREErearERAEELLERVGL-ADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 137 SGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE 216
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
....*..
gi 1039688293 217 LGDVDRV 223
Cdd:COG0411 234 EGTPAEV 240
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-239 |
2.75e-46 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 154.99 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSF-----QGKRIDTLPERELGFL-RSELQIVFQDPMG 91
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRLmRTEWGFVHQNPRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 92 SLdpRMRVR--DIISEPL---GRRDPARVSEL----LEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEP 162
Cdd:TIGR02323 98 GL--RMRVSagANIGERLmaiGARHYGNIRATaqdwLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 163 VSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRELLAAA 239
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-223 |
5.26e-46 |
|
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: 153.75 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERE---LGFL 78
Cdd:cd03219 1 LEVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSelqivFQDPmgSLDPRMRVRD-------------IISEPLGRRDPA---RVSELLEAVGLpADAAGRYPHQFSGGQRQ 142
Cdd:cd03219 79 RT-----FQIP--RLFPELTVLEnvmvaaqartgsgLLLARARREEREareRAEELLERVGL-ADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDR 222
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
.
gi 1039688293 223 V 223
Cdd:cd03219 230 V 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
7.35e-46 |
|
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: 151.00 E-value: 7.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIIseplgrrdparvselleavglpadaagryphqFSGGQRQRISIARALAPNPSVLI 158
Cdd:cd03228 78 IAYVPQDPFlfsGT------IRENI--------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 159 ADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGE 213
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-246 |
1.59e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 155.63 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTL--PERELGFlr 79
Cdd:PRK10851 3 IEIANIKKSFGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhaRDRKVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqiVFQDPmgSLDPRMRVRDIIS---EPLGRRD-------PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARA 149
Cdd:PRK10851 79 -----VFQHY--ALFRHMTVFDNIAfglTVLPRRErpnaaaiKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 150 LAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEH 229
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
250
....*....|....*..
gi 1039688293 230 EYTRELLAAAPNLRAEL 246
Cdd:PRK10851 231 RFVLEFMGEVNRLQGTI 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
1.87e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 151.83 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHAlrgvSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELgfl 78
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpaERPV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselQIVFQDpmGSLDPRMRVRDIISepLGRR--------DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG3840 74 ----SMLFQE--NNLFPHLTVAQNIG--LGLRpglkltaeQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHE 230
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
....*.
gi 1039688293 231 YTRELL 236
Cdd:COG3840 225 ALAAYL 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
6.99e-45 |
|
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: 150.91 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:TIGR02315 1 MLEVENLSKVYPN-GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDpmGSLDPRMRV-RDIISEPLG-------------RRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISI 146
Cdd:TIGR02315 80 RIGMIFQH--YNLIERLTVlENVLHGRLGykptwrsllgrfsEEDKERALSALERVGL-ADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIvelgdvdrVYDA 226
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI--------VFDG 228
|
250
....*....|
gi 1039688293 227 PEHEYTRELL 236
Cdd:TIGR02315 229 APSELDDEVL 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
1.57e-44 |
|
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: 148.94 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGflr 79
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkDRDIA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqIVFQDPmgSLDPRMRVRDIISEPLGRRD------PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:cd03301 76 ----MVFQNY--ALYPHMTVYDNIAFGLKLRKvpkdeiDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-238 |
1.65e-44 |
|
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: 149.79 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFlrse 81
Cdd:cd03299 1 LKVENLSKDW--KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 lQIVFQDPmgSLDPRMRVRDIISEPLGRR------DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:cd03299 74 -SYVPQNY--ALFPHMTVYKNIAYGLKKRkvdkkeIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTREL 235
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEF 229
|
...
gi 1039688293 236 LAA 238
Cdd:cd03299 230 LGF 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-218 |
2.08e-44 |
|
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: 148.98 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 22 VSFDVEaGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQG-------KRIDTLP-ERELGFlrselqiVFQDpmGSL 93
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPqQRKIGL-------VFQQ--YAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 94 DPRMRVRDIISEPLGRRDPA----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVS 169
Cdd:cd03297 87 FPHLNVRENLAFGLKRKRNRedriSVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039688293 170 VRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
1.72e-43 |
|
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: 144.33 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgFLRSELQIVFQDPmgSLDPRMR 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK---SLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 99 VRDIISEPL------GRRDPARVSELLEAVGLP---ADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEP 162
Cdd:pfam00005 76 VRENLRLGLllkglsKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
2.62e-43 |
|
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: 145.75 E-value: 2.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPEReLGFLRSEL 82
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 QIVFQDPMgsldprmRVRDIIS----------EPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:cd03235 78 SIDRDFPI-------SVRDVVLmglyghkglfRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRG 212
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
5.35e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 143.79 E-value: 5.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGF--- 77
Cdd:COG4598 8 ALEVRDLHKSFGDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 -------LRSELQIVFQDpmGSLDPRMRV-RDIISEP---LGR-RDPA--RVSELLEAVGLpADAAGRYPHQFSGGQRQR 143
Cdd:COG4598 86 drrqlqrIRTRLGMVFQS--FNLWSHMTVlENVIEAPvhvLGRpKAEAieRAEALLAKVGL-ADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*
gi 1039688293 224 YDAPEHEYTRELLAA 238
Cdd:COG4598 242 FGNPKSERLRQFLSS 256
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
8.49e-42 |
|
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: 140.07 E-value: 8.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRSEL 82
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 QIVFQdpmgsldprmrvrdiiseplgrrdparvselleavglpadaagryphqFSGGQRQRISIARALAPNPSVLIADEP 162
Cdd:cd00267 76 GYVPQ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 163 VSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGE 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-249 |
9.60e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.93 E-value: 9.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:COG1132 340 IEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIISepLGRRDpARVSELLEAvglpADAAG------RYPHQF-----------SGGQR 141
Cdd:COG1132 416 IGVVPQDTFlfsGT------IRENIR--YGRPD-ATDEEVEEA----AKAAQahefieALPDGYdtvvgergvnlSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGDvd 221
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT-- 557
|
250 260
....*....|....*....|....*...
gi 1039688293 222 rvydapeHEytrELLAAAPnLRAELARL 249
Cdd:COG1132 558 -------HE---ELLARGG-LYARLYRL 574
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-236 |
1.60e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.58 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTlpERELG---- 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDT--ARSLSqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 ---FLRSELQIVFQDpmGSLDP-RMRVRDIISEPL-GRRDP-----ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISI 146
Cdd:PRK11264 79 lirQLRQHVGFVFQN--FNLFPhRTVLENIIEGPViVKGEPkeeatARARELLAKVGL-AGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|
gi 1039688293 227 PEHEYTRELL 236
Cdd:PRK11264 235 PQQPRTRQFL 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-239 |
1.88e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.42 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPE--------- 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 -RELGFLRSELQIVFQDpmGSLDPRMRVRDIISEP------LGRRDP-ARVSELLEAVGLPADAAGRYPHQFSGGQRQRI 144
Cdd:PRK10619 84 kNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEApiqvlgLSKQEArERAVKYLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|....*
gi 1039688293 225 DAPEHEYTRELLAAA 239
Cdd:PRK10619 241 GNPQSPRLQQFLKGS 255
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-244 |
2.51e-41 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 144.17 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 34 IVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPErelgFLRSeLQIVFQDPmgSLDPRMRVRDIISEPLGRRD-- 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP----HLRH-INMVFQSY--ALFPHMTVEENVAFGLKMRKvp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 112 ----PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSL 187
Cdd:TIGR01187 74 raeiKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 188 TLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRELLAAAPNLRA 244
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEA 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
8.44e-41 |
|
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: 147.21 E-value: 8.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:COG4988 337 IELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIISepLGRRD--PARVSELLEAVGLpADAAGRYPH-----------QFSGGQRQRIS 145
Cdd:COG4988 413 IAWVPQNPYlfaGT------IRENLR--LGRPDasDEELEAALEAAGL-DEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGDVD 221
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHE 556
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
1.97e-40 |
|
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: 138.66 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdtlpERELGFLRSE 81
Cdd:cd03265 1 IEVENLVKKYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPmgSLDPRMRVRD-------IISEPLGRRDpARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:cd03265 75 IGIVFQDL--SVDDELTGWEnlyiharLYGVPGAERR-ERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVD 221
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
2.59e-40 |
|
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: 138.31 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSE 81
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpmGSLDPRMRVRDIISEPL------GRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:cd03292 80 IGVVFQD--FRLLPDRNVYENVAFALevtgvpPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASlVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
3.08e-40 |
|
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: 136.40 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdtlperelgflrse 81
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 lqivfqdpmgsldprmrvrdiisEPLGRRDparvselleavglpADAAG-RYPHQFSGGQRQRISIARALAPNPSVLIAD 160
Cdd:cd03216 65 -----------------------SFASPRD--------------ARRAGiAMVYQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 161 EPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-253 |
5.39e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 141.90 E-value: 5.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPErelgFLRS 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP----YQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 eLQIVFQDPmgSLDPRMRVRDIISEPLgRRD-------PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:PRK11607 93 -INMMFQSY--ALFPHMTVEQNIAFGL-KQDklpkaeiASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTR 233
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
250 260
....*....|....*....|
gi 1039688293 234 ELLAAApNLRAELARLRGGD 253
Cdd:PRK11607 248 EFIGSV-NVFEGVLKERQED 266
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-247 |
5.98e-40 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 138.68 E-value: 5.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 20 RGVSFDVEAGQRFGIVGESGSGKStlVRLLAALD------KPTAGSVSFQGKRIdtlperELGFLRSEL-QIVFQDPMGS 92
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV------APCALRGRKiATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 93 LDPRMRVRDIISEPL---GR-RDPARVSELLEAVGL--PADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSAL 166
Cdd:PRK10418 92 FNPLHTMHTHARETClalGKpADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 167 DVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTRELLAAAPNL-RAE 245
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLALyGME 251
|
..
gi 1039688293 246 LA 247
Cdd:PRK10418 252 LA 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-236 |
1.37e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.15 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGS-----VSFQGKRIDtlpEREL 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVD---ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 gflRSELQIVFQD----P-MGSLDPRM----RVRDiisepLGRRDPARVS-ELLEAVGLpADAAGRYPHQFSGGQRQRIS 145
Cdd:PRK09493 76 ---RQEAGMVFQQfylfPhLTALENVMfgplRVRG-----ASKEEAEKQArELLAKVGL-AERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
250
....*....|.
gi 1039688293 226 APEHEYTRELL 236
Cdd:PRK09493 226 NPPSQRLQEFL 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.49e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.81 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRI--DTLPErelgfL 78
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKE-----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDP----MGSldprmRVRDIISEPLGRR--DP----ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIAR 148
Cdd:PRK13632 82 RKKIGIIFQNPdnqfIGA-----TVEDDIAFGLENKkvPPkkmkDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRhVCDRVAVMRRGEIVELGD 219
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-218 |
1.79e-39 |
|
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: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgfLRSE 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA----ARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMgsLDPRMRVRDII-------SEPLGRRDpARVSELLEAVGLPaDAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:cd03263 77 LGYCPQFDA--LFDELTVREHLrfyarlkGLPKSEIK-EEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-219 |
1.91e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.07 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRID---TLPERELGFLRSELQIVFQDPmgSLD 94
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLRQKVGMVFQQY--NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 95 PRMRVRD-IISEP-----LGRRDP-ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALD 167
Cdd:COG4161 95 PHLTVMEnLIEAPckvlgLSKEQArEKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 168 VSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGD 219
Cdd:COG4161 174 PEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-224 |
3.39e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.49 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdTLPERELGFLRSELQIVFQDPMGSLDPRM 97
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEP--LGRRDPA---RVSELLEAVGLPADA-AGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVR 171
Cdd:PRK13637 101 IEKDIAFGPinLGLSEEEienRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 172 KQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-223 |
3.71e-39 |
|
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: 139.08 E-value: 3.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVrDLERRYTRRDVHalrgVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQG-------KRIDTLPE- 72
Cdd:COG4148 2 MLEV-DFRLRRGGFTLD----VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIFLPPHr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 RELGFlrselqiVFQDPmgSLDPRMRVRD-------IISEPLGRRDPARVSELLeavGLpADAAGRYPHQFSGGQRQRIS 145
Cdd:COG4148 77 RRIGY-------VFQEA--RLFPHLSVRGnllygrkRAPRAERRISFDEVVELL---GI-GHLLDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-221 |
3.95e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.91 E-value: 3.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRID---TLPERELGFLRSELQIVFQDPmgSLD 94
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRELRRNVGMVFQQY--NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 95 PRMRVRD-IISEP---LGRRDP---ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALD 167
Cdd:PRK11124 95 PHLTVQQnLIEAPcrvLGLSKDqalARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 168 VSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVD 221
Cdd:PRK11124 174 PEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-219 |
5.33e-39 |
|
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: 135.74 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPereLGFLRS 80
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPM---GSldprmrVRDIISepLGRRDpARVSELLEA----------VGLPaDA----AGRYPHQFSGGQRQR 143
Cdd:cd03249 78 QIGLVSQEPVlfdGT------IAENIR--YGKPD-ATDEEVEEAakkanihdfiMSLP-DGydtlVGERGSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGD 219
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-244 |
2.68e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 135.24 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL-- 78
Cdd:COG4152 1 MLELKGLTKRFG--DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 -RselqivfqdpmgSLDPRMRVRDIISEpLGRR-------DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG4152 79 eR------------GLYPKMKVGEQLVY-LARLkglskaeAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 151 APNPSVLIADEPVSALD-VSV---RKQILDLLASLVelyslTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:COG4152 145 LHDPELLILDEPFSGLDpVNVellKDVIRELAAKGT-----TVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
250
....*....|....*....
gi 1039688293 227 -PEHEYTRELLAAAPNLRA 244
Cdd:COG4152 220 fGRNTLRLEADGDAGWLRA 238
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-239 |
3.31e-38 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 137.05 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKP--TAGSVSFQGKRIDTLPERELGflr 79
Cdd:TIGR03258 6 IRIDHLRVAYGANTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKRG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 seLQIVFQDPmgSLDPRMRVRDIISEPL-GRRDPA-----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:TIGR03258 81 --LALLFQNY--ALFPHLKVEDNVAFGLrAQKMPKadiaeRVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASL-VELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYT 232
Cdd:TIGR03258 156 PDVLLLDEPLSALDANIRANMREEIAALhEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFA 235
|
....*..
gi 1039688293 233 RELLAAA 239
Cdd:TIGR03258 236 AEFLGAA 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
4.19e-38 |
|
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: 132.34 E-value: 4.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPE--RELGFLR 79
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 SElqivfqdpmGSLDPRMRVRD---IISEPLGRRDpARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSV 156
Cdd:cd03268 79 EA---------PGFYPNLTAREnlrLLARLLGIRK-KRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE 216
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
6.91e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.77 E-value: 6.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRS 80
Cdd:PRK13652 3 LIETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMGSLDPRMRVRDIISEP--LGRRDPA---RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:PRK13652 79 FVGLVFQNPDDQIFSPTVEQDIAFGPinLGLDEETvahRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
8.62e-38 |
|
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: 131.94 E-value: 8.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLdprmrvRDIISEPLGRRDPARVSELLEAVGLpADAAGRYPHQF-----------SGGQRQRISIA 147
Cdd:cd03245 80 IGYVPQDVTlfyGTL------RDNITLGAPLADDERILRAAELAGV-TDFVNKHPNGLdlqigergrglSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRhVCDRVAVMRRGEIV 215
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-227 |
4.77e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 4.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgflRSE 81
Cdd:PRK09452 15 VELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPmgSLDPRMRVRDIISEPLG-RRDPA-----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:PRK09452 88 VNTVFQSY--ALFPHMTVFENVAFGLRmQKTPAaeitpRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-214 |
6.84e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 129.94 E-value: 6.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHA--LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RS-ELQIVFQdpMGSLDPRMRVRDIISEPL--GRRDPA----RVSELLEAVGLPADAAGRyPHQFSGGQRQRISIARALA 151
Cdd:PRK11629 85 RNqKLGFIYQ--FHHLLPDFTALENVAMPLliGKKKPAeinsRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEI 214
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-226 |
1.65e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 136.53 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRSE 81
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---RRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLdprmrvRDIISepLGRR--DPARVSELLEAVGLpADAAGRYPHQF-----------SGGQRQRIS 145
Cdd:TIGR03375 541 IGYVPQDPRlfyGTL------RDNIA--LGAPyaDDEEILRAAELAGV-TEFVRRHPDGLdmqigergrslSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRhVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688
|
.
gi 1039688293 226 A 226
Cdd:TIGR03375 689 A 689
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-219 |
1.81e-36 |
|
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: 135.28 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP---MGSldprmrVRDIISepLGRRD--PARVSELLEAVGLpADAAGRYPH-----------QFSGGQRQRIS 145
Cdd:COG4987 411 IAVVPQRPhlfDTT------LRENLR--LARPDatDEELWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGD 219
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGT 552
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-218 |
2.88e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.75 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKridTLPERELGFLRSE 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP----MGSldprmRVRDIIS---EPLG-RRDP--ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA 151
Cdd:PRK13635 83 VGMVFQNPdnqfVGA-----TVQDDVAfglENIGvPREEmvERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEG 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
4.49e-36 |
|
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: 127.01 E-value: 4.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSE 81
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LqivfqdpmgSLDPRMRVRDIIS-----EPLGRRDPAR-VSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:cd03269 79 R---------GLYPKMKVIDQLVylaqlKGLKKEEARRrIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 156 VLIADEPVSALD-VSVR--KQILDLLASlvelYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03269 149 LLILDEPFSGLDpVNVEllKDVIRELAR----AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
4.49e-36 |
|
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: 127.21 E-value: 4.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgfLRS 80
Cdd:COG4133 2 MLEAENLSCRRGERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMgsLDPRMRVRDII---SEPLGRR-DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSV 156
Cdd:COG4133 76 RLAYLGHADG--LKPELTVRENLrfwAALYGLRaDREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHD 195
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
4.82e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.37 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYT------RRdvhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFqGKRIDT--LPER 73
Cdd:PRK13634 3 ITFQKVEHRYQyktpfeRR---ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 74 ELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPLG---RRDPA--RVSELLEAVGLPADAAGRYPHQFSGGQRQRISIAR 148
Cdd:PRK13634 79 KLKPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNfgvSEEDAkqKAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
6.27e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.89 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY--------------------TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSV 60
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 61 SFQGkRIDTL--------PE---RE--------LGFLRSElqivfqdpmgsldPRMRVRDIISeplgrrdparVSELLEA 121
Cdd:COG1134 84 EVNG-RVSALlelgagfhPEltgREniylngrlLGLSRKE-------------IDEKFDEIVE----------FAELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 122 VGLPAdaaGRYphqfSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSlTLVFVSHDLGVVRH 201
Cdd:COG1134 140 IDQPV---KTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....*
gi 1039688293 202 VCDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-195 |
9.45e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 127.67 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT--RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdTLPERELGfl 78
Cdd:COG4525 3 MLTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselqIVFQDpmGSLDPRMRVRDIISEPL--------GRRdpARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG4525 80 -----VVFQK--DALLPWLNVLDNVAFGLrlrgvpkaERR--ARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHD 195
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
1.41e-35 |
|
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: 125.77 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRdvHALRGVSFDVEAGQrFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkrIDTLPERElgFLRSE 81
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQ--KLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMgsLDPRMRVRD------IISEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:cd03264 74 IGYLPQEFG--VYPNFTVREfldyiaWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.68e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.56 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRS 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDP----MGS---------LDPRMRVRDIISEplgrrdpaRVSELLEAVGLpADAAGRYPHQFSGGQRQRISIA 147
Cdd:PRK13648 84 HIGIVFQNPdnqfVGSivkydvafgLENHAVPYDEMHR--------RVSEALKQVDM-LERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-216 |
1.76e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.97 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRI-DTLPERELGFLRSELQIVFQDPMGSLDPR 96
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIISEPLGRRDP-----ARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVR 171
Cdd:PRK13646 102 TVEREIIFGPKNFKMNldevkNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039688293 172 KQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE 216
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-233 |
3.20e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.77 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLR-SELQIVFQDpmGSLDPR 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIIS---EPLGRRDPARVSELLEA---VGLPADAAGrYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSV 170
Cdd:PRK10070 121 MTVLDNTAfgmELAGINAEERREKALDAlrqVGLENYAHS-YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 171 RKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTR 233
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-223 |
3.28e-35 |
|
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: 125.97 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAG-SVSFQGKRID--TLPE--REL 75
Cdd:COG1119 3 LLELRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGgeDVWElrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLRSELQIVFQdpmgsldPRMRVRDII----------SEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRIS 145
Cdd:COG1119 81 GLVSPALQLRFP-------RDETVLDVVlsgffdsiglYREPTDEQRERARELLELLGL-AHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-227 |
5.17e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.65 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQivfQDPmgSLDPRMRVRDIISepLGR--------RDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA- 151
Cdd:PRK13548 80 VLP---QHS--SLSFPFTVEEVVA--MGRaphglsraEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 -----PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG---DV--- 220
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGtpaEVltp 231
|
250
....*....|
gi 1039688293 221 ---DRVYDAP 227
Cdd:PRK13548 232 etlRRVYGAD 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
5.98e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 124.40 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY--TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP---EREL 75
Cdd:cd03266 1 MITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaeaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLrselqivfQDPMGsLDPRMRVRDIIsEPLGR-----RDP--ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIAR 148
Cdd:cd03266 81 GFV--------SDSTG-LYDRLTARENL-EYFAGlyglkGDEltARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
8.41e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.58 E-value: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtLPERELGFLRS 80
Cdd:PRK13639 1 ILETRDLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMGSL-DPRMRvRDIISEPLGRRDP-----ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:PRK13639 79 TVGIVFQNPDDQLfAPTVE-EDVAFGPLNLGLSkeeveKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-223 |
8.96e-35 |
|
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: 130.31 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD---VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQ--GKRIDTLPEREL 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLRSELQIVFQDPMGSLDPRMRVRDIISEPLGRRDPARVSEL-----LEAVGLPADAA----GRYPHQFSGGQRQRISI 146
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMkavitLKMVGFDEEKAeeilDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
9.15e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 125.18 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 4 VRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgkRIDTLPereLGFLRSELQ 83
Cdd:PRK11247 15 LNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-----LAGTAP---LAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 84 IVFQDpmGSLDPRMRVRDIISEPLGR--RDPARvsELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:PRK11247 85 LMFQD--ARLLPWKKVIDNVGLGLKGqwRDAAL--QALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 162 PVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
1.52e-34 |
|
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: 123.73 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTL-PERelgflrselQIVFQDPmgSLDPRM 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDR---------MVVFQNY--SLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEPLGRRDPAR--------VSELLEAVGLPAdAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVS 169
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLskserraiVEEHIALVGLTE-AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 170 VRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV-YDAPEH 229
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-218 |
2.03e-34 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 130.45 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRSE 81
Cdd:TIGR03796 478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVL---ANS 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSL-------DPRMRVRDI--------ISEPLGRRDPARVSELLEAvglpadaaGRyphQFSGGQRQR 143
Cdd:TIGR03796 555 VAMVDQDIFlfeGTVrdnltlwDPTIPDADLvrackdaaIHDVITSRPGGYDAELAEG--------GA---NLSGGQRQR 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASlvelYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:TIGR03796 624 LEIARALVRNPSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-234 |
2.21e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.99 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLL---------AALDkptaGSVSFQGKRIDTlPE 72
Cdd:COG1117 12 IEVRNLNVYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgARVE----GEILLDGEDIYD-PD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 RELGFLRSELQIVFQDP------------MGsldPRMRvrdiiseplGRRDPA----RVSELLEAVGLPADAAGR---YP 133
Cdd:COG1117 85 VDVVELRRRVGMVFQKPnpfpksiydnvaYG---LRLH---------GIKSKSeldeIVEESLRKAALWDEVKDRlkkSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 134 HQFSGGQRQRISIARALAPNPSVLIADEPVSALD-VSVRKqILDLLASLVELYslTLVFVSHDLGVVRHVCDRVAVMRRG 212
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLG 229
|
250 260
....*....|....*....|..
gi 1039688293 213 EIVELGDVDRVYDAPEHEYTRE 234
Cdd:COG1117 230 ELVEFGPTEQIFTNPKDKRTED 251
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
3.31e-34 |
|
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: 122.93 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT-----RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSF--QGKRID--TLP 71
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 72 ERE-LGFLRSELQIVFQdpmgSLD--PRMRVRDIISEPLGRR--DP----ARVSELLEAVGLPADAAGRYPHQFSGGQRQ 142
Cdd:COG4778 84 PREiLALRRRTIGYVSQ----FLRviPRVSALDVVAEPLLERgvDReearARARELLARLNLPERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRG 212
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
3.61e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 122.54 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgfLRSE 81
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMgsLDPRMRVRD-------IISEPLGRRDPARVSELLEAVglpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:cd03224 77 IGYVPEGRR--IFPELTVEEnlllgayARRRAKRKARLERVYELFPRL---KERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-241 |
8.76e-34 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 124.53 E-value: 8.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKP----TAGSVSFQGkrIDTL---P 71
Cdd:PRK15093 3 LLDIRNLTIEFKTSDgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDD--IDLLrlsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 72 ERELGFLRSELQIVFQDPMGSLDPRMRV-RDIISEPLG-----------RRDPARVSELLEAVGL--PADAAGRYPHQFS 137
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVgRQLMQNIPGwtykgrwwqrfGWRKRRAIELLHRVGIkdHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 138 GGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVEL 217
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260
....*....|....*....|....
gi 1039688293 218 GDVDRVYDAPEHEYTRELLAAAPN 241
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPD 264
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-227 |
1.66e-33 |
|
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: 124.07 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 22 VSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQG-------KRIDTLPERElgflrsELQIVFQDpmGSLD 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEKR------RIGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 95 PRMRVRDIISEPLGRRDP-------ARVSELLEAVGLpadaAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALD 167
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPserrisfERVIELLGIGHL----LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 168 VSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-215 |
1.68e-33 |
|
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: 120.44 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdtlPERELgflRSEL 82
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKER---RKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 QIVFQDP-----MGSldprmrVRD--IISEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:cd03226 74 GYVMQDVdyqlfTDS------VREelLLGLKELDAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELYSLTLVfVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-215 |
1.85e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 120.75 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 17 HALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSELQIVFQDPMGSLDpr 96
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIISEPL------GRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSV 170
Cdd:PRK10908 94 RTVYDNVAIPLiiagasGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039688293 171 RKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:PRK10908 173 SEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-226 |
1.96e-33 |
|
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: 121.18 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRSE 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIISepLGRRDPARvSELLEAvglpADAAgrYPHQF-------------------SGG 139
Cdd:cd03251 78 IGLVSQDVFlfnDT------VAENIA--YGRPGATR-EEVEEA----ARAA--NAHEFimelpegydtvigergvklSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 140 QRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGD 219
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
....*..
gi 1039688293 220 VDRVYDA 226
Cdd:cd03251 220 HEELLAQ 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
3.56e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.88 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtLPERELGFLRS 80
Cdd:PRK13636 5 ILKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMGSLDPRMRVRDIISEPLGRRDPA-----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEdevrkRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPE 228
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
1.65e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.59 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRrdVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRI---DTLPERELGf 77
Cdd:COG1129 4 LLEMRGISKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 lrseLQIVFQDPmgSLDPRMRVRDII---SEPL--GRRDP----ARVSELLEAVGL---PADAAGRYphqfSGGQRQRIS 145
Cdd:COG1129 81 ----IAIIHQEL--NLVPNLSVAENIflgREPRrgGLIDWramrRRARELLARLGLdidPDTPVGDL----SVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-227 |
2.25e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 124.83 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdtlPERELGFLRS 80
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPM---GSldprmrVRDIISEPLGRRDPARVSELLEAVGLpADAAGRYPH-----------QFSGGQRQRISI 146
Cdd:TIGR00958 556 QVALVGQEPVlfsGS------VRENIAYGLTDTPDEEIMAAAKAANA-HDFIMEFPNgydtevgekgsQLSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVsvrkQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
.
gi 1039688293 227 P 227
Cdd:TIGR00958 704 Q 704
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-218 |
3.79e-32 |
|
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: 117.71 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIISepLGRRDP--ARVSELLEAVG-------LPAD---AAGRYPHQFSGGQRQRISI 146
Cdd:cd03254 79 IGVVLQDTFlfsGT------IMENIR--LGRPNAtdEEVIEAAKEAGahdfimkLPNGydtVLGENGGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEG 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-214 |
4.35e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.68 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkriDTLPERELGFLR 79
Cdd:PRK13650 4 IIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 SELQIVFQDP----MGSldprmRVRDIISEPLGRRDPA------RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARA 149
Cdd:PRK13650 81 HKIGMVFQNPdnqfVGA-----TVEDDVAFGLENKGIPheemkeRVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 150 LAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRhVCDRVAVMRRGEI 214
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-218 |
6.63e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.27 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD----VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkrIDTLPERELG 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 FLRSELQIVFQDPMGSLdprmrVRDIISE------------PLGRRdpARVSELLEAVGLpADAAGRYPHQFSGGQRQRI 144
Cdd:PRK13633 82 DIRNKAGMVFQNPDNQI-----VATIVEEdvafgpenlgipPEEIR--ERVDESLKKVGM-YEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.12e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 116.72 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGflrS 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPmgSLDPRMRVRDIISepLGR----------RDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG4604 76 RLAILRQEN--HINSRLTVRELVA--FGRfpyskgrltaEDREIIDEAIAYLDL-EDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-218 |
1.17e-31 |
|
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: 116.56 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRS 80
Cdd:cd03253 1 IEFENVTFAYdPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQD-PMGSLDPRMRVRdiisepLGRRDpARVSELLEAvglpADAAG------RYPHQF-----------SGGQRQ 142
Cdd:cd03253 76 AIGVVPQDtVLFNDTIGYNIR------YGRPD-ATDEEVIEA----AKAAQihdkimRFPDGYdtivgerglklSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-218 |
1.69e-31 |
|
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: 115.71 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 4 VRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkRIDTLPERELGFlRSEL- 82
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGLGGGF-NPELt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 ---QIVFqdpMGSL------DPRMRVRDIISeplgrrdparVSELLEAVGLPadaAGRYphqfSGGQRQRISIARALAPN 153
Cdd:cd03220 101 greNIYL---NGRLlglsrkEIDEKIDEIIE----------FSELGDFIDLP---VKTY----SSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSlTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-234 |
5.59e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.14 E-value: 5.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYTRRDVHA-LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK---------RIDTLPe 72
Cdd:PRK14246 9 DVFNISRLYLYINDKAiLKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 relgfLRSELQIVFQDPmgSLDPRMRVRDIISEPL---GRRDPARVSELLE----AVGLPADAAGRY---PHQFSGGQRQ 142
Cdd:PRK14246 88 -----LRKEVGMVFQQP--NPFPHLSIYDNIAYPLkshGIKEKREIKKIVEeclrKVGLWKEVYDRLnspASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDR 222
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
250
....*....|..
gi 1039688293 223 VYDAPEHEYTRE 234
Cdd:PRK14246 239 IFTSPKNELTEK 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-218 |
6.02e-31 |
|
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: 114.13 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 26 VEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGFLRSELQI-----VFQDPMGSLDPRMR 98
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpaDRPVSMLFQENNLfahltVEQNVGLGLSPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 99 VRDIiseplgrrDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLL 178
Cdd:cd03298 101 LTAE--------DRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039688293 179 ASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-215 |
7.01e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.21 E-value: 7.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD--VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFL 78
Cdd:PRK10535 4 LLELKDIRRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSE-LQIVFQD----PMGSLDPRMRVRDIISEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:PRK10535 84 RREhFGFIFQRyhllSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIV 215
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQA-ERVIEIRDGEIV 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-247 |
8.27e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:PRK13647 5 IEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMGSLDPRMRVRDIISEPLGRR-DPA----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSV 156
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGlDKDeverRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVydapeheyTRELL 236
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL--------TDEDI 230
|
250
....*....|.
gi 1039688293 237 AAAPNLRAELA 247
Cdd:PRK13647 231 VEQAGLRLPLV 241
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-218 |
8.60e-31 |
|
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: 119.82 E-value: 8.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkriDTLPERELGFLRSE 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG---HDLADYTLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLDPRM---RVRDIISEPLgrRDPARVSELLEAV-GLP-------ADAAGRyphqFSGGQRQRISIA 147
Cdd:TIGR02203 408 VALVSQDVVlfnDTIANNIaygRTEQADRAEI--ERALAAAYAQDFVdKLPlgldtpiGENGVL----LSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKA-DRIVVMDDGRIVERG 549
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
1.34e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.63 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFqGKRIdtlperELGFLRS 80
Cdd:COG0488 315 VLELEGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQivfqdpmgSLDPRMRVRDIISEPLGRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIAD 160
Cdd:COG0488 386 HQE--------ELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 161 EPVSALDVSVRKQILDLLASlvelYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE-LGDVD 221
Cdd:COG0488 458 EPTNHLDIETLEALEEALDD----FPGTVLLVSHDRYFLDRVATRILEFEDGGVREyPGGYD 515
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-218 |
1.91e-30 |
|
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: 112.97 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLdpRMRVrdiisEPLGRRDPARVSELLEAVGL-------------PADAAGRyphQFSGGQRQRIS 145
Cdd:cd03244 80 ISIIPQDPVlfsGTI--RSNL-----DPFGEYSDEELWQALERVGLkefveslpggldtVVEEGGE---NLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASlvELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
1-206 |
1.98e-30 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 112.87 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD-----VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQ--GKRID--TLP 71
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQqggvrLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRheGAWVDlaQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 72 ERELGFLR-SELQIVFQdpmgSLD--PRMRVRDIISEPLGRRD------PARVSELLEAVGLPADAAGRYPHQFSGGQRQ 142
Cdd:TIGR02324 81 PREVLEVRrKTIGYVSQ----FLRviPRVSALEVVAEPLLERGvpreaaRARARELLARLNIPERLWHLPPATFSGGEQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLvELYSLTLVFVSHDLGVVRHVCDRV 206
Cdd:TIGR02324 157 RVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRV 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
2.32e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtlperelgfLRS 80
Cdd:COG3845 5 ALELRGITKRFG--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---------IRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 -----ELQI--VFQDPMgsLDPRMRVRD-II--SEPLGRRDP------ARVSELLEAVGLPADAAgRYPHQFSGGQRQRI 144
Cdd:COG3845 74 prdaiALGIgmVHQHFM--LVPNLTVAEnIVlgLEPTKGGRLdrkaarARIRELSERYGLDVDPD-AKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
2.75e-30 |
|
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: 111.15 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGflrSE 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---DH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSldprmrVRDIIseplgrrdparvselleavglpadaagryphqFSGGQRQRISIARALAPNPSVLI 158
Cdd:cd03246 78 VGYLPQDDElfsGS------IAENI--------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 159 ADEPVSALDVSVRKQILDLLASLvELYSLTLVFVSHDLGVVRhVCDRVAVMRRGEI 214
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-248 |
2.96e-30 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 118.52 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRSE 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpmGSLDPRMRVRDII-SEPLGrrdPARVSELLEAVGLPADAAgRYPHQF-----------SGGQRQRISIARA 149
Cdd:TIGR03797 529 LGVVLQN--GRLMSGSIFENIAgGAPLT---LDEAWEAARMAGLAEDIR-AMPMGMhtvisegggtlSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 150 LAPNPSVLIADEPVSALDVSVRKQILDLLASLvelySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGdvdrvydapeh 229
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG----------- 666
|
250
....*....|....*....
gi 1039688293 230 eyTRELLAAAPNLRAELAR 248
Cdd:TIGR03797 667 --TYDELMAREGLFAQLAR 683
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-227 |
3.48e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.20 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 29 GQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRI--DTLPERELGflrselqIVFQDPmgSLDPRMRVRDIIS-- 104
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDIC-------MVFQSY--ALFPHMSLGENVGyg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 105 -EPLGRRDP---ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLAS 180
Cdd:PRK11432 103 lKMLGVPKEerkQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039688293 181 LVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PRK11432 182 LQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-222 |
4.29e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.80 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLerRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLA-ALDKP--TAGSVSFQGKRIDTLP--EREL 75
Cdd:COG4136 1 MLSLENL--TITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALPaeQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GflrselqIVFQDPMgsLDPRMRVRDIIS----EPLGRRD-PARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:COG4136 79 G-------ILFQDDL--LFPHLSVGENLAfalpPTIGRAQrRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGvvrhvcDRVAVmrrGEIVELGDVDR 222
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE------DAPAA---GRVLDLGNWQH 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-216 |
4.38e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.18 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSE-LQIVFQDPMgsLDPRM 97
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSFM--LIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEPL------GRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVR 171
Cdd:PRK10584 104 NALENVELPAllrgesSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039688293 172 KQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVE 216
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-219 |
7.21e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 111.11 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 23 SFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFlrselQIVFQDpmGSLDPRMRVRDI 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPV-----SMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 103 I------SEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILD 176
Cdd:TIGR01277 91 IglglhpGLKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039688293 177 LLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGD 219
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
8.54e-30 |
|
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: 111.61 E-value: 8.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgflRS 80
Cdd:COG0410 3 MLEVENLHAGYG--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR----IA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQI--------VFqdpmgsldPRMRVRD-IISEPLGRRDPARVSELLEAVglpadaAGRYP------HQF----SGGQR 141
Cdd:COG0410 77 RLGIgyvpegrrIF--------PSLTVEEnLLLGAYARRDRAEVRADLERV------YELFPrlkerrRQRagtlSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVD 221
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
....*..
gi 1039688293 222 RVYDAPE 228
Cdd:COG0410 222 ELLADPE 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-218 |
1.08e-29 |
|
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: 110.58 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPereLGFLRSE 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP---MGS----LDPRMRVRDI-ISEPLgrrdpaRVSElleaVGLpadaagryphQFSGGQRQRISIARALAPN 153
Cdd:cd03369 84 LTIIPQDPtlfSGTirsnLDPFDEYSDEeIYGAL------RVSE----GGL----------NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASlvELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-237 |
1.14e-29 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 111.08 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP-----ERELGF 77
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpheraRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVfqdpmgsldPRMRVRDIIS---EPLGRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:TIGR03410 80 VPQGREIF---------PRLTVEENLLtglAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVydapEHEYTRE 234
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRR 226
|
...
gi 1039688293 235 LLA 237
Cdd:TIGR03410 227 YLA 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
3.10e-29 |
|
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: 108.55 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgfLRSE 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMgsldprmRVRDIISEPLGRRdparvselleavglpadaagryphqFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:cd03247 77 ISVLNQRPY-------LFDTTLRNNLGRR-------------------------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 162 PVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-221 |
3.13e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRSELQIVFQDPMgsLDPRm 97
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRRNIAVVFQDAG--LFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISepLGRRDpARVSELLEAVGLPADA-------------AGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVS 164
Cdd:PRK13657 424 SIEDNIR--VGRPD-ATDEEMRAAAERAQAHdfierkpdgydtvVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 165 ALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVD 221
Cdd:PRK13657 501 ALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNA-DRILVFDNGRVVESGSFD 554
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
7.21e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.55 E-value: 7.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAL-----DKPTAGSVSFQGKRIDTlPERELG 76
Cdd:PRK14267 5 IETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 FLRSELQIVFQDPmgSLDPRMRVRDIISEPL-------GRRD-PARVSELLEAVGLPADAAGR---YPHQFSGGQRQRIS 145
Cdd:PRK14267 82 EVRREVGMVFQYP--NPFPHLTIYDNVAIGVklnglvkSKKElDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYslTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....
gi 1039688293 226 APEHEYTRELLAAA 239
Cdd:PRK14267 238 NPEHELTEKYVTGA 251
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-232 |
7.93e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.62 E-value: 7.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAL-----DKPTAGSVSFQGKRIDTLPERELg 76
Cdd:PRK14247 4 IEIRDLKVSFG--QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 flRSELQIVFQDPmgSLDPRMRVRDIISepLG----------RRDPARVSELLEAVGLPADAAGRY---PHQFSGGQRQR 143
Cdd:PRK14247 81 --RRRVQMVFQIP--NPIPNLSIFENVA--LGlklnrlvkskKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
....*....
gi 1039688293 224 YDAPEHEYT 232
Cdd:PRK14247 233 FTNPRHELT 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-216 |
1.56e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.41 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRR-DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRidtLPERELGFLR 79
Cdd:PRK13642 4 ILEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 SELQIVFQDPMGSLDPRMRVRDII----SEPLGRRDP-ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGATVEDDVAfgmeNQGIPREEMiKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVE 216
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-228 |
1.86e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDT-LPERELGFLRSELQIVFQDPMGSLDPRM 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEPLG---RRDPARVSEL--LEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRK 172
Cdd:PRK13641 103 VLKDVEFGPKNfgfSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 173 QILDLLASLvELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVElgdvdrvYDAPE 228
Cdd:PRK13641 183 EMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK-------HASPK 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
1.91e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSfqgkRID----TLPERELGF 77
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNS----KITvdgiTLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVFQDP----MGSldprmRVRDIISEPLGRRDPAR------VSELLEAVGLpADAAGRYPHQFSGGQRQRISIA 147
Cdd:PRK13640 82 IREKVGIVFQNPdnqfVGA-----TVGDDVAFGLENRAVPRpemikiVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMA-DQVLVLDDGKLLAQGSPVEIFSKV 234
|
.
gi 1039688293 228 E 228
Cdd:PRK13640 235 E 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-226 |
2.12e-28 |
|
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: 107.96 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRSE 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQ----------DPMGSLDPRMRVRDIISEPLGRRDPARVSELLEAVGlpaDAAGRYPHQFSGGQRQRISIARALA 151
Cdd:cd03252 78 VGVVLQenvlfnrsirDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYD---TIVGEQGAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLveLYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
2.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.41 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRR---DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVS--FQGKRIDTLPERELG 76
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 F-------------------LRSELQIVFQDPMGSLDPRMRVRDIISEPLG---RRDPA--RVSELLEAVGLPADAAGRY 132
Cdd:PRK13651 83 VleklviqktrfkkikkikeIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSmgvSKEEAkkRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 133 PHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLAslvELYSL--TLVFVSHDLGVVRHVCDRVAVMR 210
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD---NLNKQgkTIILVTHDLDNVLEWTKRTIFFK 239
|
....*....
gi 1039688293 211 RGEIVELGD 219
Cdd:PRK13651 240 DGKIIKDGD 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
4.61e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.82 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDK-----PTAGSVSFQGKRIdtlPERELG 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNI---YERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 F--LRSELQIVFQDPmgSLDPrMRVRDIIS---EPLGRRDPARVSELLEAVGLPADAAGRYPHQ-------FSGGQRQRI 144
Cdd:PRK14258 83 LnrLRRQVSMVHPKP--NLFP-MSVYDNVAygvKIVGWRPKLEIDDIVESALKDADLWDEIKHKihksaldLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVM-----RRGEIVELGD 219
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGL 239
|
250
....*....|....*....
gi 1039688293 220 VDRVYDAPEHEYTRELLAA 238
Cdd:PRK14258 240 TKKIFNSPHDSRTREYVLS 258
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-248 |
5.38e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMGsldprMRVRDIIS---EP-------LGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:PRK11231 80 LLPQHHLTPEG-----ITVRELVAygrSPwlslwgrLSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGdvdrvydAPEHE 230
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEV 225
|
250
....*....|....*...
gi 1039688293 231 YTRELLAAAPNLRAELAR 248
Cdd:PRK11231 226 MTPGLLRTVFDVEAEIHP 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-228 |
6.10e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.79 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtLPERELGFLRS 80
Cdd:PRK13638 1 MLATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPmgslDPRMRVRDIISE------PLGRRDPA---RVSELLEAVGlpadaAGRYPHQ----FSGGQRQRISIA 147
Cdd:PRK13638 78 QVATVFQDP----EQQIFYTDIDSDiafslrNLGVPEAEitrRVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
.
gi 1039688293 228 E 228
Cdd:PRK13638 228 E 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-223 |
8.99e-28 |
|
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: 110.99 E-value: 8.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPEREL----GF 77
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhiGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRselqivfQDPM---GSldprmrVRDIISEpLGRRDPARVSELLEAVG-------LPA------DAAGrypHQFSGGQR 141
Cdd:COG4618 411 LP-------QDVElfdGT------IAENIAR-FGDADPEKVVAAAKLAGvhemilrLPDgydtriGEGG---ARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQildLLASLVELYS--LTLVFVSHDLGVVRhVCDRVAVMRRGEIVELGD 219
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAA---LAAAIRALKArgATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGP 549
|
....
gi 1039688293 220 VDRV 223
Cdd:COG4618 550 RDEV 553
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
1.50e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 4 VRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQ-GKRIDTLPE---------- 72
Cdd:COG0488 1 LENLSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLPQeppldddltv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 73 --------RELGFLRSELQIVFQDpMGSLDPRMRVRDIISEPLGRRD----PARVSELLEAVGLPADAAGRYPHQFSGGQ 140
Cdd:COG0488 79 ldtvldgdAELRALEAELEELEAK-LAEPDEDLERLAELQEEFEALGgweaEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 141 RQRISIARALAPNPSVLIADEPVSALDV-SVRkqildLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-218 |
1.71e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRI-DTLPERELGFLRSELQIVFQDPMGSLDPR 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIISEP----LGRRDPARVS-ELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVR 171
Cdd:PRK13649 102 TVLKDVAFGPqnfgVSQEEAEALArEKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039688293 172 KQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:PRK13649 182 KELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-214 |
2.83e-27 |
|
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: 104.86 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdtlPERELGFLRS 80
Cdd:cd03248 12 VKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMgsLDPRmRVRDIISEPLGRRDPARVSELLEAVGL----------PADAAGRYPHQFSGGQRQRISIARAL 150
Cdd:cd03248 89 KVSLVGQEPV--LFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAhsfiselasgYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEI 214
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
2.86e-27 |
|
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: 109.30 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKridTLPERELGFLRSE 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLDPRMRvrdiisepLGRRD--PARVSELLEAVGL-PADAA---------GRYPHQFSGGQRQRISI 146
Cdd:TIGR02857 398 IAWVPQHPFlfaGTIAENIR--------LARPDasDAEIREALERAGLdEFVAAlpqgldtpiGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 147 ARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLgVVRHVCDRVAVM 209
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-214 |
4.07e-27 |
|
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: 102.90 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRytrrdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgFLRSEL 82
Cdd:cd03215 6 EVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--AIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 QIVFQDPMGS-LDPRMRVRDIISeplgrrdparvselleavglpadaagrYPHQFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:cd03215 78 AYVPEDRKREgLVLDLSVAENIA---------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 162 PVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
4.38e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.14 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQdpmgsldprmRVrDIISEPLgrRD----------PARVSELLEAVGL--------PADA----AGRyphQFSGG 139
Cdd:PRK11160 416 ISVVSQ----------RV-HLFSATL--RDnlllaapnasDEALIEVLQQVGLeklleddkGLNAwlgeGGR---QLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 140 QRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGD 219
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-234 |
4.40e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDvhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDK-----PTAGSVSFQGKRIDTlPEREL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS-PRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLRSELQIVFQDPmgslDP-RMRVRDIISEPL---GRRDPARVSELLEAVGLPA---DAAGRYPHQ----FSGGQRQRI 144
Cdd:PRK14239 82 VDLRKEIGMVFQQP----NPfPMSIYENVVYGLrlkGIKDKQVLDEAVEKSLKGAsiwDEVKDRLHDsalgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYslTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|
gi 1039688293 225 DAPEHEYTRE 234
Cdd:PRK14239 236 MNPKHKETED 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-200 |
5.33e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.08 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 10 RYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQ-GKRIDTLPERelgflrselqivfqd 88
Cdd:NF040873 1 GYGGRPV--LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAYVPQR--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 89 pmGSLDPRM--RVRDIIS----------EPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSV 156
Cdd:NF040873 64 --SEVPDSLplTVRDLVAmgrwarrglwRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVR 200
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-235 |
6.96e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.20 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRI-DTLPERELGFLRSELQIVFQDPMGSLDPR 96
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsSTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIISEP----LGRRDPARVS-ELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVR 171
Cdd:PRK13643 101 TVLKDVAFGPqnfgIPKEKAEKIAaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 172 KQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTREL 235
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-196 |
2.37e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.86 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDvhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTlPERELGflrs 80
Cdd:PRK11248 1 MLQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 elqIVFQDPmgSLDPRMRVRDIISEPL--------GRRDPARvsELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:PRK11248 74 ---VVFQNE--GLLPWRNVQDNVAFGLqlagvekmQRLEIAH--QMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039688293 153 NPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDL 196
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
2.38e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.40 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYT-------------------RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVS 61
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 62 FQG-----KRIDTLpeRELGFL---RSELqivFQD--PMGSLdpRMrVRDI--ISEPLGRRDPARVSELLEAVGL---PA 126
Cdd:COG4586 81 VLGyvpfkRRKEFA--RRIGVVfgqRSQL---WWDlpAIDSF--RL-LKAIyrIPDAEYKKRLDELVELLDLGELldtPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 127 daagrypHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRV 206
Cdd:COG4586 153 -------RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRV 225
|
250
....*....|....*.
gi 1039688293 207 AVMRRGEIVELGDVDR 222
Cdd:COG4586 226 IVIDHGRIIYDGSLEE 241
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-218 |
3.31e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 106.75 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKridTLPERELGFLRSE 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV---DLAIADPAWLRRQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSL-------DPRMRVRDIISEPLGRRDPARVSELLEAVGLPADAAGRyphQFSGGQRQRISIARALA 151
Cdd:TIGR01846 533 MGVVLQENVlfsRSIrdnialcNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGA---NLSGGQRQRIAIARALV 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-226 |
3.35e-26 |
|
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: 106.75 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRSE 81
Cdd:TIGR01193 474 IVINDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLdprmrVRDIIsepLGRRDPARVSELLEAVGLPA--DAAGRYPHQF-----------SGGQRQRIS 145
Cdd:TIGR01193 550 INYLPQEPYifsGSI-----LENLL---LGAKENVSQDEIWAACEIAEikDDIENMPLGYqtelseegssiSGGQKQRIA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDllaSLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVDRVYD 225
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVN---NLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
.
gi 1039688293 226 A 226
Cdd:TIGR01193 698 R 698
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-250 |
4.61e-26 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 106.32 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRS 80
Cdd:TIGR02204 338 IEFEQVNFAYpARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAEL---RA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDP-MGSLDPRMRVRdiisepLGRRDPARvsellEAVGLPADAA------GRYPHQF-----------SGGQRQ 142
Cdd:TIGR02204 415 RMALVPQDPvLFAASVMENIR------YGRPDATD-----EEVEAAARAAhahefiSALPEGYdtylgergvtlSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGdvdr 222
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQG---- 556
|
250 260
....*....|....*....|....*...
gi 1039688293 223 vydapeheyTRELLAAAPNLRAELARLR 250
Cdd:TIGR02204 557 ---------THAELIAKGGLYARLARLQ 575
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-222 |
5.74e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRyTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgflRSEL 82
Cdd:COG3845 259 EVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 83 QIVF--QDPMGS-LDPRMRVRD------IISEPLGRR---DPARVSELLEAV--------GLPADAAGryphQFSGGQRQ 142
Cdd:COG3845 334 GVAYipEDRLGRgLVPDMSVAEnlilgrYRRPPFSRGgflDRKAIRAFAEELieefdvrtPGPDTPAR----SLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVS----VRKQILDL----LASLVelysltlvfVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGaiefIHQRLLELrdagAAVLL---------ISEDLDEILALSDRIAVMYEGRI 480
|
....*...
gi 1039688293 215 VelGDVDR 222
Cdd:COG3845 481 V--GEVPA 486
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-239 |
1.22e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLErrYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGflrS 80
Cdd:PRK09536 3 MIDVSDLS--VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPMGSLDprMRVRDIIS----------EPLGRRDPARVSELLEAVGLPADAAgRYPHQFSGGQRQRISIARAL 150
Cdd:PRK09536 78 RVASVPQDTSLSFE--FDVRQVVEmgrtphrsrfDTWTETDRAAVERAMERTGVAQFAD-RPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGdvdrvydAPEHE 230
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG-------PPADV 226
|
....*....
gi 1039688293 231 YTRELLAAA 239
Cdd:PRK09536 227 LTADTLRAA 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-247 |
1.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkrIDTLPERELGFLRSELQIVFQDPMGSLDPRM 97
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNPETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEPLGRRDP-----ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRK 172
Cdd:PRK13644 95 VEEDLAFGPENLCLPpieirKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 173 QILDLLASLVElYSLTLVFVSHDLGVVrHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYtrelLAAAPNLRAELA 247
Cdd:PRK13644 174 AVLERIKKLHE-KGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQT----LGLTPPSLIELA 242
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-243 |
1.37e-25 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 100.31 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 24 FDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRiDTLPERELGFLRSELQIVFQDPMGSLDPRMRVRDII 103
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-PGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 104 SEPL---GRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLAS 180
Cdd:TIGR03771 80 IGWLrrpCVADFAAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 181 LVElYSLTLVFVSHDLGVVRHVCDRVaVMRRGEIVELGDVDRVYDAPEHEYTRELLAAAPNLR 243
Cdd:TIGR03771 159 LAG-AGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGVSDSSPLLR 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-222 |
1.74e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHalrgVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK-RIDTLPERElgflr 79
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPSRR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 sELQIVFQDpmGSLDPRMRVRDIIS---EP---LGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:PRK10771 72 -PVSMLFQE--NNLFSHLTVAQNIGlglNPglkLNAAQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVRE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDR 222
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-215 |
2.44e-25 |
|
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: 99.71 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTR-------------------RDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSF 62
Cdd:cd03267 1 IEVSNLSKSYRVyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 63 QGKRidtlP-ERELGFLRsELQIVFQD---------PMGSLDPRMRVRDIISEPLGRRdPARVSELLEaVGLPADAAGRy 132
Cdd:cd03267 81 AGLV----PwKRRKKFLR-RIGVVFGQktqlwwdlpVIDSFYLLAAIYDLPPARFKKR-LDELSELLD-LEELLDTPVR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 133 phQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRG 212
Cdd:cd03267 153 --QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 1039688293 213 EIV 215
Cdd:cd03267 231 RLL 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-219 |
4.53e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 12 TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVS-----------FQGKRIDTLPERELGF--L 78
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknNHELITNPYSKKIKNFkeL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDPMGSLDPRMRVRDIISEP--LGR---RDPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:PRK13631 115 RRRVSMVFQFPEYQLFKDTIEKDIMFGPvaLGVkksEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASlVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGD 219
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-222 |
4.99e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.35 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSF-QGKRIDTLPERelGFLrselqivfqdPMGSLdprm 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQR--PYL----------PLGTL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 rvRDIISEPLGRR--DPARVSELLEAVGLPA-----DAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSV 170
Cdd:COG4178 443 --REALLYPATAEafSDAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 171 RKQILDLLASlvELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELGDVDR 222
Cdd:COG4178 521 EAALYQLLRE--ELPGTTVISVGHRSTLAAF-HDRVLELTGDGSWQLLPAEA 569
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
5.95e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.39 E-value: 5.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRY---TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgf 77
Cdd:COG1101 1 MLELKNLSKTFnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 lRSELqI--VFQDPMGSLDPRMRVRDIIS------EPLG------RRDPARVSELLEAVGL-----PADAAGryphQFSG 138
Cdd:COG1101 78 -RAKY-IgrVFQDPMMGTAPSMTIEENLAlayrrgKRRGlrrgltKKRRELFRELLATLGLglenrLDTKVG----LLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 139 GQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSH------DLGvvrhvcDRVAVMRRG 212
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG------NRLIMMHEG 225
|
...
gi 1039688293 213 EIV 215
Cdd:COG1101 226 RII 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-206 |
6.55e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 6.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTL-PERelgfLRSELQIVFQDPMGSLDPrm 97
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkPEI----YRQQVSYCAQTPTLFGDT-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 rVRDIISEPLGRR----DPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQ 173
Cdd:PRK10247 97 -VYDNLIFPWQIRnqqpDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190
....*....|....*....|....*....|...
gi 1039688293 174 ILDLLASLVELYSLTLVFVSHDLGVVRHvCDRV 206
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-218 |
1.09e-24 |
|
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: 102.21 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgflRSELQIVFQDPmgsldprmr 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDT--------- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 99 V--RDIISEPL--GRRDpARVSELLEAvglpADAAgrYPHQF-------------------SGGQRQRISIARALAPNPS 155
Cdd:COG5265 442 VlfNDTIAYNIayGRPD-ASEEEVEAA----ARAA--QIHDFieslpdgydtrvgerglklSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELYSlTLVfVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRT-TLV-IAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-228 |
1.52e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.92 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGflrs 80
Cdd:PRK11650 3 GLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 eLQIVFQDPmgSLDPRMRVRDIISEPLGRRDPARvSELLEAVglpADAAG---------RYPHQFSGGQRQRISIARALA 151
Cdd:PRK11650 78 -IAMVFQNY--ALYPHMSVRENMAYGLKIRGMPK-AEIEERV---AEAARileleplldRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 PNPSVLIADEPVSALD----VSVRKQILDLLASLvelySLTLVFVSHD------LGvvrhvcDRVAVMRRGEIVELGDVD 221
Cdd:PRK11650 151 REPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRL----KTTSLYVTHDqveamtLA------DRVVVMNGGVAEQIGTPV 220
|
....*..
gi 1039688293 222 RVYDAPE 228
Cdd:PRK11650 221 EVYEKPA 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-245 |
2.04e-24 |
|
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: 101.42 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALD--KPTAGSV----------------SFQ 63
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 64 GKRI----DTLPERELGF----------LRSELQIVFQDPMgSLDPRMRVRDIISEPL------GRRDPARVSELLEAVG 123
Cdd:TIGR03269 79 GEPCpvcgGTLEPEEVDFwnlsdklrrrIRKRIAIMLQRTF-ALYGDDTVLDNVLEALeeigyeGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 124 LpadaAGRYPH---QFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVR 200
Cdd:TIGR03269 158 L----SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039688293 201 HVCDRVAVMRRGEIVELGDVDRVYD-----APEHEYTRELLAAAPNLRAE 245
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAvfmegVSEVEKECEVEVGEPIIKVR 283
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
2.08e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.82 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSfqgkridtlperelgflrse 81
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 lqivfqdpmgsLDPRMRVRdiiseplgrrdparvselleavglpadaagrYPHQFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:cd03221 59 -----------WGSTVKIG-------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 162 PVSALDVSVRKQILDLLASlvelYSLTLVFVSHDLGVVRHVCDRVAVMRRGE 213
Cdd:cd03221 97 PTNHLDLESIEALEEALKE----YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-239 |
4.26e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRytrrdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDT------------- 69
Cdd:COG1129 258 EVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiay 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 70 LPE--RELGflrselqIVFQDP------MGSLDpRMRVRDIISEplgRRDPARVSELLEAVGLPADAAGRYPHQFSGGQR 141
Cdd:COG1129 332 VPEdrKGEG-------LVLDLSirenitLASLD-RLSRGGLLDR---RRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVelGDVD 221
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV--GELD 477
|
250
....*....|....*....
gi 1039688293 222 RvydapeHEYTRE-LLAAA 239
Cdd:COG1129 478 R------EEATEEaIMAAA 490
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-218 |
5.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPER--ELGFLRSELQIVFQDPMGSLDP 95
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 RMRVRDIISEP--LGRRDP---ARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSV 170
Cdd:PRK13645 106 ETIEKDIAFGPvnLGENKQeayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039688293 171 RKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-218 |
2.89e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 96.64 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERELGflrselqIVFQDPmgS 92
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPpaERGVG-------MVFQSY--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 93 LDPRMRVRDIIS--EPLGRRDPA----RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSAL 166
Cdd:PRK11000 86 LYPHLSVAENMSfgLKLAGAKKEeinqRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 167 DVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-227 |
3.76e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 34 IVGESGSGKSTLVRLLAALDKPTAGSVSFQG-------KRIDTLPE-RELGFlrselqiVFQDpmGSLDPRMRVRDIISE 105
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEkRRIGY-------VFQD--ARLFPHYKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 106 PLGRRDPARVSELLEAVGLPAdAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELY 185
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039688293 186 SLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-238 |
8.24e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkriDTLPERElGFLRSE 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPSRA-RHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQdpMGSLDPRMRVRD---IISEPLGRRDP---ARVSELLEAVGLPADAAGRYpHQFSGGQRQRISIARALAPNPS 155
Cdd:PRK13537 82 VGVVPQ--FDNLDPDFTVREnllVFGRYFGLSAAaarALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIV-----------ELG-DVDRV 223
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIaegaphaliesEIGcDVIEI 237
|
250
....*....|....*
gi 1039688293 224 YdAPEHEYTRELLAA 238
Cdd:PRK13537 238 Y-GPDPVALRDELAP 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-219 |
8.45e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.70 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVE-------------AGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPE----RELGFLRS 80
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELqivfqdPMGSldpRMRVRDIIS-------EPLGR---RDPARVSELLEAVGLPAdAAGRYPHQFSGGQRQRISIARAL 150
Cdd:PRK10575 93 QL------PAAE---GMTVRELVAigrypwhGALGRfgaADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGD 219
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-179 |
8.96e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.24 E-value: 8.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLerRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgflrs 80
Cdd:PRK13539 2 MLEGEDL--ACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 elQIVFQDPMGSLDPRMRVRDIIS---EPLGRRDPaRVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVL 157
Cdd:PRK13539 74 --ACHYLGHRNAMKPALTVAENLEfwaAFLGGEEL-DIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180
....*....|....*....|..
gi 1039688293 158 IADEPVSALDVSVRKQILDLLA 179
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIR 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-223 |
9.51e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTL-----PERELGFLRSELQIVfqDPM 90
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhklaAQLGIGIIYQELSVI--DEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 91 GSLDP----RMRVRDIISEPL--GRRDPARVSELLEAVGLPADAAGRYPhQFSGGQRQRISIARALAPNPSVLIADEPVS 164
Cdd:PRK09700 96 TVLENlyigRHLTKKVCGVNIidWREMRVRAAMMLLRVGLKVDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 165 ALdvsVRKQILDLLASLVELYS--LTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:PRK09700 175 SL---TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
1.83e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP--ERE---L 75
Cdd:COG1137 3 TLEAENLVKSYGKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLRSELQIvFQdpmgsldpRMRVRD---IISE--PLGRRDP-ARVSELLEAVGLP--ADAAGrypHQFSGGQRQRISIA 147
Cdd:COG1137 81 GYLPQEASI-FR--------KLTVEDnilAVLElrKLSKKEReERLEELLEEFGIThlRKSKA---YSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 148 RALAPNPSVLIADEPVSALD-VSVrKQILDLLASLVElysltlvfvsHDLGV------VRH---VCDRVAVMRRGEIVEL 217
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKE----------RGIGVlitdhnVREtlgICDRAYIISEGKVLAE 217
|
250
....*....|.
gi 1039688293 218 GDVDRVYDAPE 228
Cdd:COG1137 218 GTPEEILNNPL 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-238 |
3.56e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.47 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAG-----SVSFQGKRIdtLPERELGFLRSELQIVFQDP---- 89
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPnpfp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 90 MGSLD------------PRMRVRDIISeplgrrdpARVSE--LLEAVglpADAAGRYPHQFSGGQRQRISIARALAPNPS 155
Cdd:PRK14271 115 MSIMDnvlagvrahklvPRKEFRGVAQ--------ARLTEvgLWDAV---KDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEHEYTREL 235
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARY 261
|
...
gi 1039688293 236 LAA 238
Cdd:PRK14271 262 VAG 264
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-219 |
6.89e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.90 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 14 RDVHA-------LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDK--PTAGSVSFQGKRIDTLP--ER-ELG-FLrs 80
Cdd:COG0396 4 KNLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSpdERaRAGiFL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 elqiVFQDPM---GsldprMRVRDIISEPLG-RRDPA--------RVSELLEAVGLPADAAGRYPHQ-FSGGQRQRISIA 147
Cdd:COG0396 82 ----AFQYPVeipG-----VSVSNFLRTALNaRRGEElsareflkLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 148 RALAPNPSVLIADEPVSALDV-SVRKqildlLASLVELYS---LTLVFVSHDLGVVRHV-CDRVAVMRRGEIVELGD 219
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIdALRI-----VAEGVNKLRspdRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGG 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-253 |
7.17e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLErrYTRRDVHALRG-VSFDVEAGQRFGIVGESGSGKSTLVRLLAaldkptaGSVSFQGK-RIDTLPEREL--GF 77
Cdd:PRK11174 350 IEAEDLE--ILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALL-------GFLPYQGSlKINGIELRELdpES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVFQDPM---GSLdprmrvRDIISepLGRRDP-----------ARVSELLEAV--GL---PADAAGRyphqFSG 138
Cdd:PRK11174 421 WRKHLSWVGQNPQlphGTL------RDNVL--LGNPDAsdeqlqqalenAWVSEFLPLLpqGLdtpIGDQAAG----LSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 139 GQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
250 260 270
....*....|....*....|....*....|....*
gi 1039688293 219 DVDRvydapeheytrelLAAAPNLRAELARLRGGD 253
Cdd:PRK11174 566 DYAE-------------LSQAGGLFATLLAHRQEE 587
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-213 |
7.57e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALdKPTA---GSVSFQGK--RIDTLPERElgflRSELQIVFQDP 89
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEelQASNIRDTE----RAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 90 MgsLDPRMRVRDII---SEPL--GRRD----PARVSELLEAVGLPADAAGRYPHqFSGGQRQRISIARALAPNPSVLIAD 160
Cdd:PRK13549 92 A--LVKELSVLENIflgNEITpgGIMDydamYLRAQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 161 EPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGE 213
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-215 |
7.78e-22 |
|
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: 93.74 E-value: 7.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALdKPTA---GSVSFQGKRIDTLPERELGflRSELQIVFQDPMg 91
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDTE--RAGIVIIHQELT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 92 sLDPRMRVRDII------SEPLGRRDPA----RVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:TIGR02633 89 -LVPELSVAENIflgneiTLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 162 PVSALDVSVRKQILDLLASLvELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-235 |
9.74e-22 |
|
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: 90.29 E-value: 9.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgflRSE 81
Cdd:cd03218 1 LRAENLSKRYGKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVF--QDPmgSLDPRMRVRDIISEPLGRRDPA------RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:cd03218 75 LGIGYlpQEA--SIFRKLTVEENILAVLEIRGLSkkereeKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELysltlvfvshDLGV------VRH---VCDRVAVMRRGEIVELGDVDRVY 224
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDR----------GIGVlitdhnVREtlsITDRAYIIYEGKVLAEGTPEEIA 221
|
250
....*....|.
gi 1039688293 225 dapEHEYTREL 235
Cdd:cd03218 222 ---ANELVRKV 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-223 |
1.46e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 93.18 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELG----FLRSELQIvFQdpmGSld 94
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhigYLPQDVEL-FP---GT-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 95 prmrvrdiISEPLGR-RDPARVSELLEAvglpADAAG------RYPHQF-----------SGGQRQRISIARALAPNPSV 156
Cdd:TIGR01842 408 --------VAENIARfGENADPEKIIEA----AKLAGvhelilRLPDGYdtvigpggatlSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 157 LIADEPVSALD----VSVRKQILDLLASLVelyslTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVDRV 223
Cdd:TIGR01842 476 VVLDEPNSNLDeegeQALANAIKALKARGI-----TVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-218 |
2.56e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkriDTLPERELGFLRSE 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpmgsldprmrVR---DIIS--------EPLGRRDPARVSELLEAVglpaDAAGRYPHQF-----------SGG 139
Cdd:PRK11176 419 VALVSQN----------VHlfnDTIAnniayartEQYSREQIEEAARMAYAM----DFINKMDNGLdtvigengvllSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 140 QRQRISIARALAPNPSVLIADEPVSALDVSVRKQIldlLASLVELY-SLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAI---QAALDELQkNRTSLVIAHRLSTIEKA-DEILVVEDGEIVERG 560
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-229 |
4.26e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.44 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLerRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRS 80
Cdd:PRK11831 7 LVDMRGV--SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDpmGSLDPRMRVRDIISEPLgrRDPARVSEL---------LEAVGLPAdAAGRYPHQFSGGQRQRISIARALA 151
Cdd:PRK11831 85 RMSMLFQS--GALFTDMNVFDNVAYPL--REHTQLPAPllhstvmmkLEAVGLRG-AAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 152 PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDAPEH 229
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-234 |
1.03e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.30 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 18 ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDK--PTA---GSVSFQGKRIDTlPERELGFLRSELQIVFQDP--- 89
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPnpf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 90 -----------------MGSLDprmrvrDIISEPLgrRDPA---RVSELLEAVGLpadaagryphQFSGGQRQRISIARA 149
Cdd:PRK14243 104 pksiydniaygaringyKGDMD------ELVERSL--RQAAlwdEVKDKLKQSGL----------SLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 150 LAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYslTLVFVSHDLGVVRHVCDRVAVM---------RRGEIVELGDV 220
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRT 243
|
250
....*....|....
gi 1039688293 221 DRVYDAPEHEYTRE 234
Cdd:PRK14243 244 EKIFNSPQQQATRD 257
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.10e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.50 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:TIGR02868 335 LELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDP-MGSLDPRMRVRdiisepLGRRD--PARVSELLEAVGLpADAAGRYPH-----------QFSGGQRQRISIA 147
Cdd:TIGR02868 411 VSVCAQDAhLFDTTVRENLR------LARPDatDEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDL 196
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
1.55e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTL-PER--ELGf 77
Cdd:PRK15439 11 LLCARSISKQYS--GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKahQLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 lrseLQIVFQDPMgsLDPRMRVRDII--SEPLGRRDPARVSELLEAVGLPADaagryPHQFSG----GQRQRISIARALA 151
Cdd:PRK15439 88 ----IYLVPQEPL--LFPNLSVKENIlfGLPKRQASMQKMKQLLAALGCQLD-----LDSSAGslevADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 152 PNPSVLIADEPVSALD-VSVR---KQILDLLASLVelyslTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYDA 226
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETErlfSRIRELLAQGV-----GIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-228 |
1.63e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERE---LGF 77
Cdd:PRK11300 5 LLSVSGLMMRFG--GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSelqivFQDPmgSLDPRMRV-----------------RDIISEPLGRRDPA----RVSELLEAVGLpADAAGRYPHQF 136
Cdd:PRK11300 83 VRT-----FQHV--RLFREMTVienllvaqhqqlktglfSGLLKTPAFRRAESealdRAATWLERVGL-LEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 137 SGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVE 216
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
250
....*....|..
gi 1039688293 217 LGDVDRVYDAPE 228
Cdd:PRK11300 235 NGTPEEIRNNPD 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-218 |
1.96e-20 |
|
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: 86.56 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 7 LERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALD---KPTAGSVSFQGKridtlpERELGFLRSELQ 83
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ------PRKPDQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 84 IVFQDpmGSLDPRMRVRDIIS----EPLGRRDPARVSELLEAVGLPADAA-----GRYPHQFSGGQRQRISIARALAPNP 154
Cdd:cd03234 85 YVRQD--DILLPGLTVRETLTytaiLRLPRKSSDAIRKKRVEDVLLRDLAltrigGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-231 |
2.29e-20 |
|
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: 85.66 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLerRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALD--KPTAGSVSFQGKRIDTLPERElgflR 79
Cdd:cd03217 1 LEIKDL--HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 SELQI--VFQDPMgsldprmRVRDIiseplgrrdpaRVSELLEAVGlpadaAGryphqFSGGQRQRISIARALAPNPSVL 157
Cdd:cd03217 75 ARLGIflAFQYPP-------EIPGV-----------KNADFLRYVN-----EG-----FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 158 IADEPVSALDVSVRKQILDLLASLVELYSLTLVfVSHDLGVVRHV-CDRVAVMRRGEIVELGDVDRVYDAPEHEY 231
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLI-ITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-243 |
2.42e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 22 VSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGflrSELQIVFQDPMGSLDprMRVRD 101
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQNATTPGD--ITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 102 IIS------EPLGRR----DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVR 171
Cdd:PRK10253 101 LVArgryphQPLFTRwrkeDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 172 KQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGdvdrvydAPEHEYTRELLAAAPNLR 243
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERIYGLR 244
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-223 |
4.99e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALdKPTAGSVSFQGKRIDTLPERELGFLRSEL--QivfQDPMGSldpr 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLsqQ---QSPPFA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIISepLGRRDPAR-------VSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALA-------PNPSVLIADEP 162
Cdd:COG4138 84 MPVFQYLA--LHQPAGASseaveqlLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 163 VSALDVSVRKQILDLLASLVELySLTLVFVSHDLG-VVRHvCDRVAVMRRGEIVELGDVDRV 223
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNhTLRH-ADRVWLLKQGKLVASGETAEV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
8.07e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIdtlPERELgFLRSE 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARAR-LARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQdpMGSLDPRMRVRD---IISEPLG---RRDPARVSELLEAVGLPADAAGRYPhQFSGGQRQRISIARALAPNPS 155
Cdd:PRK13536 116 IGVVPQ--FDNLDLEFTVREnllVFGRYFGmstREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRG-EIVE 216
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-234 |
9.06e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAL---DKPTAGSVSFQGKRIDTLPE--REL 75
Cdd:PRK09984 4 IIRVEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLRSELQIVFQDpmGSLDPRMRVRDII------SEPLGRR-----DPARVSELLEAvgLPADAAGRYPHQ----FSGGQ 140
Cdd:PRK09984 82 RKSRANTGYIFQQ--FNLVNRLSVLENVligalgSTPFWRTcfswfTREQKQRALQA--LTRVGMVHFAHQrvstLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 141 RQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIvelgdv 220
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV------ 231
|
250
....*....|....
gi 1039688293 221 drVYDAPEHEYTRE 234
Cdd:PRK09984 232 --FYDGSSQQFDNE 243
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
1.26e-19 |
|
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: 83.67 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHA---LRGVSFDVEAGQRFGIVGESGSGKSTLVR-LLAALDKpTAGSVSFQGKridtlpereLGF 77
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS---------IAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 lrselqiVFQDPM---GSldprmrVRDII--SEPLgrrDPARVSELLEAVGLPADAAgRYPHQ-----------FSGGQR 141
Cdd:cd03250 71 -------VSQEPWiqnGT------IRENIlfGKPF---DEERYEKVIKACALEPDLE-ILPDGdlteigekginLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQILD--LLASLveLYSLTLVFVSHDLGVVRHvCDRVAVMRRGE 213
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-214 |
1.40e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 20 RGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgflRSELQIVF--QDPMGS---LD 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpEDRQSSglyLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 95 PRMRvRDIISEPLGRR----DPARVSELLE----AVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSAL 166
Cdd:PRK15439 356 APLA-WNVCALTHNRRgfwiKPARENAVLEryrrALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039688293 167 DVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:PRK15439 435 DVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-227 |
1.48e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.46 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 10 RYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRidtLPERELGFLRSELQIVFQDP 89
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP---LTKLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 90 MGSLDprmRVRDIISepLGRrdPARVSELLEAVGLPA---DAAGRYPHQF-----------SGGQRQRISIARALAPNPS 155
Cdd:PRK10789 399 FLFSD---TVANNIA--LGR--PDATQQEIEHVARLAsvhDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 156 VLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-199 |
2.23e-19 |
|
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: 83.18 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLErrYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTL---PERELGFL 78
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrdePHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 rselqivfqdpmGSLD---PRMRVRDIIS--EPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPN 153
Cdd:TIGR01189 79 ------------GHLPglkPELSALENLHfwAAIHGGAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVV 199
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-218 |
2.74e-19 |
|
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: 82.60 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTA--GSVSFQGKRID-TLPERELGFlrselqiVFQDPMgsLDP 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDkRSFRKIIGY-------VPQDDI--LHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 RMRVRdiiseplgrrdparvsellEAVGLPADAAGryphqFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQIL 175
Cdd:cd03213 96 TLTVR-------------------ETLMFAAKLRG-----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039688293 176 DLLASLVELySLTLVFVSHDL-GVVRHVCDRVAVMRRGEIVELG 218
Cdd:cd03213 152 SLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-222 |
2.98e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERE-----LGFLRSELQIVfqdpm 90
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagVAIIYQELHLV----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 91 gsldPRMRVRD------------IISEPLGRRdpaRVSELLEAVGLPADAAGRYPHqFSGGQRQRISIARALAPNPSVLI 158
Cdd:PRK11288 92 ----PEMTVAEnlylgqlphkggIVNRRLLNY---EAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 159 ADEPVSALdvSVRkQILDLLASLVELYS--LTLVFVSHDLGVVRHVCDRVAVMRRGEIVE----LGDVDR 222
Cdd:PRK11288 164 FDEPTSSL--SAR-EIEQLFRVIRELRAegRVILYVSHRMEEIFALCDAITVFKDGRYVAtfddMAQVDR 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-223 |
3.90e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 22 VSFDVEAGQRFGIVGESGSGKSTLVRLLAALdKPTAGSVSFQGKRIDTLPERELGFLRSEL--QI-------VFQDPMGS 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLsqQQtppfampVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 93 LDPRMRVRDIISEplgrrdparVSELLEAVGLpADAAGRYPHQFSGGQRQRISIA-------RALAPNPSVLIADEPVSA 165
Cdd:PRK03695 94 QPDKTRTEAVASA---------LNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 166 LDVSvRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:PRK03695 164 LDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-217 |
1.20e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLerryTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRID-------------- 68
Cdd:PRK09700 267 EVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkkgmay 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 69 -TLPERELGF-----LRSELQIVFQDPMGSLDPRMrvrDIISEPLGRRDPARVSELLEavgLPADAAGRYPHQFSGGQRQ 142
Cdd:PRK09700 343 iTESRRDNGFfpnfsIAQNMAISRSLKDGGYKGAM---GLFHEVDEQRTAENQRELLA---LKCHSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVEL 217
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-179 |
1.36e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLErryTRRDVHAL-RGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPE---RELG 76
Cdd:PRK13538 1 MLEARNLA---CERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 FL------RSELQivfqdPMGSLDPRMRVRdiiseplGRRDPARVSELLEAVGLpadaAGR--YP-HQFSGGQRQRISIA 147
Cdd:PRK13538 78 YLghqpgiKTELT-----ALENLRFYQRLH-------GPGDDEALWEALAQVGL----AGFedVPvRQLSAGQQRRVALA 141
|
170 180 190
....*....|....*....|....*....|..
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRKQILDLLA 179
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-228 |
7.71e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.86 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSfqgkrIDTLPERELGF--LR 79
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGCDISKFGLmdLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 SELQIVFQDPM---GS----LDP--------------RMRVRDIIseplgRRDP----ARVSElleavglpadaAGRyph 134
Cdd:PLN03130 1313 KVLGIIPQAPVlfsGTvrfnLDPfnehndadlwesleRAHLKDVI-----RRNSlgldAEVSE-----------AGE--- 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 135 QFSGGQRQRISIARALAPNPSVLIADEPVSALDVS----VRKQILDllaslvELYSLTLVFVSHDLGVVRHvCDRVAVMR 210
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRtdalIQKTIRE------EFKSCTMLIIAHRLNTIID-CDRILVLD 1446
|
250
....*....|....*...
gi 1039688293 211 RGEIVElgdvdrvYDAPE 228
Cdd:PLN03130 1447 AGRVVE-------FDTPE 1457
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-234 |
1.91e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.56 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLperELGFLRS 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDP-MGSLDPRMRVrdiisEPLGRRDPARVSELLEAVGLpADAAGRYP-----------HQFSGGQRQRISIAR 148
Cdd:PLN03232 1311 VLSIIPQSPvLFSGTVRFNI-----DPFSEHNDADLWEALERAHI-KDVIDRNPfgldaevseggENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASlvELYSLTLVFVSHDLGVVRHvCDRVAVMRRGEIVElgdvdrvYDAPE 228
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQ 1454
|
....*.
gi 1039688293 229 HEYTRE 234
Cdd:PLN03232 1455 ELLSRD 1460
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-230 |
3.40e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 12 TRRDVH-ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRID-TLPERELGFLRSELQIVFQDP 89
Cdd:PRK15056 15 TWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 90 MGSLDPRMRVRDIISEPLGR---RDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSAL 166
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLRRakkRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 167 DVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDrVAVMRRGEIVELGDVDRVYDAPEHE 230
Cdd:PRK15056 174 DVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAENLE 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-218 |
3.53e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.53 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERelgFLRSE 81
Cdd:PRK10790 341 IDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPMGSLDprmRVRDIISepLGRR-DPARVSELLEAVGLpADAAGRYP-----------HQFSGGQRQRISIARA 149
Cdd:PRK10790 417 VAMVQQDPVVLAD---TFLANVT--LGRDiSEEQVWQALETVQL-AELARSLPdglytplgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 150 LAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQG 556
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-194 |
3.75e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERrytrrdvHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLL--AALDKPTAGSVSFQGKRIDtlperelgflr 79
Cdd:COG2401 36 VELRVVER-------YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 80 selqivfqdpmgsldprmRVRDIISEPLGRRDPARVSELLEAVGLpADAAG--RYPHQFSGGQRQRISIARALAPNPSVL 157
Cdd:COG2401 98 ------------------REASLIDAIGRKGDFKDAVELLNAVGL-SDAVLwlRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039688293 158 IADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSH 194
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-199 |
4.50e-17 |
|
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: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtlpERELGFLRSELQIVFQDPM-GSLDPRM 97
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD---FQRDSIARGLLYLGHAPGIkTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRdiISEPLGRRDpaRVSELLEAVGLPAdAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDL 177
Cdd:cd03231 93 NLR--FWHADHSDE--QVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180
....*....|....*....|..
gi 1039688293 178 LASLVELYSLTLVFVSHDLGVV 199
Cdd:cd03231 168 MAGHCARGGMVVLTTHQDLGLS 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-218 |
9.41e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgfLRSE 81
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM---GSLdpRMRVrdiisEPLGRRDPARVSELLEAVGLPADAAGRYP----------HQFSGGQRQRISIAR 148
Cdd:PTZ00243 1386 FSMIPQDPVlfdGTV--RQNV-----DPFLEASSAEVWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMAR 1458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 149 ALAPNPSVLI-ADEPVSALDVSVRKQILDLLASLVELYslTLVFVSHDLGVVRHvCDRVAVMRRGEIVELG 218
Cdd:PTZ00243 1459 ALLKKGSGFIlMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-227 |
1.35e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.92 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRidTLPERELGFLRS 80
Cdd:PTZ00265 383 IQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDPM---GSLDPRMR-----VRDI-------------ISEPLGRRDPARV---------------SELLEA--- 121
Cdd:PTZ00265 461 KIGVVSQDPLlfsNSIKNNIKyslysLKDLealsnyynedgndSQENKNKRNSCRAkcagdlndmsnttdsNELIEMrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 122 ----------------------VGLP---ADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILD 176
Cdd:PTZ00265 541 yqtikdsevvdvskkvlihdfvSALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 177 LLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGDVDRVYDAP 227
Cdd:PTZ00265 621 TINNLKGNENRITIIIAHRLSTIRYA-NTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-229 |
1.74e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 22 VSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPEREL---GFL-----RSELQIVfqdPMGSl 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiraGIMlcpedRKAEGII---PVHS- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 94 dprmrVRD--IISeplGRRDPARVSELLEAvGLPADAAGRY----------PHQ----FSGGQRQRISIARALAPNPSVL 157
Cdd:PRK11288 348 -----VADniNIS---ARRHHLRAGCLINN-RWEAENADRFirslniktpsREQlimnLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 158 IADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVelGDVDRVyDAPEH 229
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELARE-QATER 486
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-218 |
1.89e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 78.45 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtRRDVH-ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgkRIDTLPERELGF--L 78
Cdd:TIGR00957 1285 VEFRNYCLRY-REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-----IIDGLNIAKIGLhdL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQDPM---GSLdpRMRVrdiisEPLGRRDPARV---SELLEAVGLPADAAGRYPHQ-------FSGGQRQRIS 145
Cdd:TIGR00957 1359 RFKITIIPQDPVlfsGSL--RMNL-----DPFSQYSDEEVwwaLELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 146 IARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElySLTLVFVSHDLGVVRHVCdRVAVMRRGEIVELG 218
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-218 |
2.02e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 78.45 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVR-LLAALDKpTAGSVSFQGKrIDTLPErelgflrs 80
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-VAYVPQ-------- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 elQIVFQDPmgsldpRMRVRDIISEPLgrrDPARVSELLEAVGLPAD----------AAGRYPHQFSGGQRQRISIARAL 150
Cdd:TIGR00957 707 --QAWIQND------SLRENILFGKAL---NEKYYQQVLEACALLPDleilpsgdrtEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 151 APNPSVLIADEPVSALDVSVRKQILD-LLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-245 |
2.26e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.07 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 24 FDVEAGQRFGIVGESGSGKSTLVRLLA---ALDKptaGSVSFQG----KRIDTLPER---------------ELGFLRSE 81
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQdlivARLQQDPPRnvegtvydfvaegieEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 ----LQIVFQDPMGSLDPRM-RVRDIISEPLGRRDPARVSELLEAVGLPADAAgryPHQFSGGQRQRISIARALAPNPSV 156
Cdd:PRK11147 101 yhdiSHLVETDPSEKNLNELaKLQEQLDHHNLWQLENRINEVLAQLGLDPDAA---LSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 157 LIADEPVSALDVsvrkQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVEL-GDvdrvYDApeheYtreL 235
Cdd:PRK11147 178 LLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYpGN----YDQ----Y---L 242
|
250
....*....|
gi 1039688293 236 LAAAPNLRAE 245
Cdd:PRK11147 243 LEKEEALRVE 252
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-225 |
3.31e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.62 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 3 EVRDLERRYTRRDVH-ALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRidTLPERELGfLRSE 81
Cdd:PRK13545 23 KLKDLFFRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--ALIAISSG-LNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 L----QIVFQDPMGSLDpRMRVRDIISEplgrrdparVSELLEavglpadaAGRYPHQ----FSGGQRQRISIARALAPN 153
Cdd:PRK13545 100 LtgieNIELKGLMMGLT-KEKIKEIIPE---------IIEFAD--------IGKFIYQpvktYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 154 PSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYD 225
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-223 |
6.85e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 6 DLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLP-----ERELGFLRS 80
Cdd:PRK10895 8 NLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlharaRRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQI-----VFQDPMGSLDPRmrvRDIISEPlgRRDpaRVSELLEAVGLP--ADAAGRyphQFSGGQRQRISIARALAPN 153
Cdd:PRK10895 86 EASIfrrlsVYDNLMAVLQIR---DDLSAEQ--RED--RANELMEEFHIEhlRDSMGQ---SLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 154 PSVLIADEPVSALD-VSVR--KQILDLLASlvelYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRV 223
Cdd:PRK10895 156 PKFILLDEPFAGVDpISVIdiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-208 |
1.28e-15 |
|
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: 73.98 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 21 GVSFDVEAG-----QRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPErelgflrselQIvfqdpmgSLDP 95
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ----------YI-------KADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 RMRVRDIISEPLGRR--DPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQ 173
Cdd:cd03237 75 EGTVRDLLSSITKDFytHPYFKTEIAKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1039688293 174 ILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAV 208
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-234 |
1.58e-15 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 73.79 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTL----VRLLAALDkptaGSVSFQGKRIDTLPereLGF 77
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---LHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVFQDPM---GS----LDPRMRVRD-IISEPLgrrDPARVSELLEAVGLPADA-AGRYPHQFSGGQRQRISIAR 148
Cdd:cd03288 93 LRSRLSIILQDPIlfsGSirfnLDPECKCTDdRLWEAL---EIAQLKNMVKSLPGGLDAvVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVrKQILDLLAsLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVElgdvdrvYDAPE 228
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVSTILDA-DLVLVLSRGILVE-------CDTPE 239
|
....*.
gi 1039688293 229 HEYTRE 234
Cdd:cd03288 240 NLLAQE 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-194 |
1.87e-15 |
|
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: 71.80 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKptagsvSFQGkRIDTLPERELGFL--RSELqivfqdPMGSLdpr 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSG-RIGMPEGEDLLFLpqRPYL------PLGTL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 mrvRDIISEPLGRRdparvselleavglpadaagryphqFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILD 176
Cdd:cd03223 81 ---REQLIYPWDDV-------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*...
gi 1039688293 177 LLaslvELYSLTLVFVSH 194
Cdd:cd03223 133 LL----KELGITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-213 |
5.93e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERE-----LGFLRSELQIV----- 85
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagIGIIHQELNLIpqlti 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 86 ---------FQDPMGSLD-PRMRvrdiiseplgrrdpARVSELLEAVGLPadaagRYPHQFSG----GQRQRISIARALA 151
Cdd:PRK10762 97 aeniflgreFVNRFGRIDwKKMY--------------AEADKLLARLNLR-----FSSDKLVGelsiGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 152 PNPSVLIADEPVSAL-DV---SVRKQILDLLASlvelySLTLVFVSHDLGVVRHVCDRVAVMRRGE 213
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTeteSLFRVIRELKSQ-----GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-181 |
7.23e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 17 HALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKP---TAGSVSFQGKRIDtlpereLGFLRSELQIVFQDPMgsL 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID------AKEMRAISAYVQQDDL--F 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 94 DPRMRVRD--IISEPL--GRRDP-----ARVSELLEAVGLpADAA-------GRYpHQFSGGQRQRISIARALAPNPSVL 157
Cdd:TIGR00955 111 IPTLTVREhlMFQAHLrmPRRVTkkekrERVDEVLQALGL-RKCAntrigvpGRV-KGLSGGERKRLAFASELLTDPPLL 188
|
170 180
....*....|....*....|....
gi 1039688293 158 IADEPVSALDVSVRKQILDLLASL 181
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGL 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-239 |
7.74e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRY-TRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAL------------DKPTAGSVSFQGKRID 68
Cdd:PTZ00265 1166 IEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkNEHTNDMTNEQDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 69 TlpERELGF-----------------------------------------LRSELQIVFQDPMGSldpRMRVRDIIS--- 104
Cdd:PTZ00265 1246 E--EQNVGMknvnefsltkeggsgedstvfknsgkilldgvdicdynlkdLRNLFSIVSQEPMLF---NMSIYENIKfgk 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 105 EPLGRRDPARVS------ELLEAVGLPADA-AGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDL 177
Cdd:PTZ00265 1321 EDATREDVKRACkfaaidEFIESLPNKYDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 178 LASLVELYSLTLVFVSHdlgvvrhvcdRVAVMRRGE-IVELGDVDRVYDAPEHEYTRELLAAA 239
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAH----------RIASIKRSDkIVVFNNPDRTGSFVQAHGTHEELLSV 1453
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-206 |
1.22e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK-RIDTLPERElgFLRSELQIVFQDPMgSLDPRM 97
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKL--YLDTTLPLTVNRFL-RLRPGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIIsePLGRRDPArvSELLEAvglpadaagryPHQ-FSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILD 176
Cdd:PRK09544 97 KKEDIL--PALKRVQA--GHLIDA-----------PMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|
gi 1039688293 177 LLASLVELYSLTLVFVSHDLGVVRHVCDRV 206
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-222 |
1.47e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALdKPTA---GSVSFQGKridtlpERELGFLR-SELQ---IVFQD 88
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGE------VCRFKDIRdSEALgivIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 89 ----PMGSL-------DPRMRvRDIISEPLGRRdpaRVSELLEAVGLPADAAGRYPHQFSGGQrQRISIARALAPNPSVL 157
Cdd:NF040905 87 laliPYLSIaeniflgNERAK-RGVIDWNETNR---RARELLAKVGLDESPDTLVTDIGVGKQ-QLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039688293 158 IADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDR 222
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-221 |
1.52e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.83 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALD--KPTAGSVSFQGKRIDTLPERElgfl 78
Cdd:CHL00131 7 ILEIKNLHASVNENEI--LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQI--VFQDP------------MGSLDPRMRvrdiiSEPLGRRDPAR----VSELLEAVGLPADAAGRYPHQ-FSGG 139
Cdd:CHL00131 81 RAHLGIflAFQYPieipgvsnadflRLAYNSKRK-----FQGLPELDPLEfleiINEKLKLVGMDPSFLSRNVNEgFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 140 QRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVC-DRVAVMRRGEIVELG 218
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
...
gi 1039688293 219 DVD 221
Cdd:CHL00131 235 DAE 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-252 |
1.78e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.08 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTrrDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVrLLAALDKPTAGSVSFqgkRIDT------LPEREL 75
Cdd:NF000106 14 VEVRGLVKHFG--EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPW---RF*TwcanrrALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 76 GFLRSELQIVFQDPMGSLDPRMRVRDIisePLGRRDP-ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:NF000106 88 G*HRPVR*GRRESFSGRENLYMIGR*L---DLSRKDArARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 155 SVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVydapEHEYTRE 234
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL----KTKVGGR 238
|
250
....*....|....*...
gi 1039688293 235 LLAAAPNLRAELARLRGG 252
Cdd:NF000106 239 TLQIRPAHAAELDRMVGA 256
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-230 |
3.03e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 70.23 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 14 RDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK------------RIDTLPERE-----LG 76
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsviaisaglsgQLTGIENIEfkmlcMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 77 FLRSELQivfqdpmgSLDPRmrvrdIIseplgrrdpaRVSELLEAVGLPADaagryphQFSGGQRQRISIARALAPNPSV 156
Cdd:PRK13546 115 FKRKEIK--------AMTPK-----II----------EFSELGEFIYQPVK-------KYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVYdaPEHE 230
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYE 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-218 |
6.98e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVR-LLAALDKPTAGSVSFQGKridtlperelgflrselqiVFQDPMGSL 93
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------------VAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 94 DPRMRVRDII--SEPLgrrDPARVSELLEAVGLPADAA----------GRYPHQFSGGQRQRISIARALAPNPSVLIADE 161
Cdd:PLN03130 690 IFNATVRDNIlfGSPF---DPERYERAIDVTALQHDLDllpggdlteiGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 162 PVSALDVSVRKQILDLLASlVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-231 |
8.76e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.66 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLerRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALD--KPTAGSVSFQGKRIDTL-PERELGf 77
Cdd:PRK09580 1 MLSIKDL--HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELsPEDRAG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 lrSELQIVFQDPM------------GSLDPRMRVRDiiSEPLGRRDPAR-VSELLEAVGLPADAAGRYPHQ-FSGGQRQR 143
Cdd:PRK09580 78 --EGIFMAFQYPVeipgvsnqfflqTALNAVRSYRG--QEPLDRFDFQDlMEEKIALLKMPEDLLTRSVNVgFSGGEKKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHV-CDRVAVMRRGEIVELGDVDR 222
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRD-GKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGDFTL 232
|
....*....
gi 1039688293 223 VYDAPEHEY 231
Cdd:PRK09580 233 VKQLEEQGY 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-239 |
1.60e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRD---------VHALRG-----VSFDVEAGQRFGIVGESGSGKSTLVRLL-AALDKpTAGSVSFQGK 65
Cdd:PRK10762 236 MMVGRKLEDQYPRLDkapgevrlkVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGH 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 66 RIDTLPERE-------------------LGF----------LRSelqivFQDPMGSL---DPRMRVRDIIsEPLGRRDPA 113
Cdd:PRK10762 315 EVVTRSPQDglangivyisedrkrdglvLGMsvkenmsltaLRY-----FSRAGGSLkhaDEQQAVSDFI-RLFNIKTPS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 114 RVsellEAVGLpadaagryphqFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVS 193
Cdd:PRK10762 389 ME----QAIGL-----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVS 452
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039688293 194 HDLGVVRHVCDRVAVMRRGEIVelGDVDRvydapeHEYTRE-LLAAA 239
Cdd:PRK10762 453 SEMPEVLGMSDRILVMHEGRIS--GEFTR------EQATQEkLMAAA 491
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-212 |
2.94e-13 |
|
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: 66.97 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLvrLLAALD--KPTAGSVSFQGKRIDTlPERELGFLRSELQIVF--QDPM 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGemQTLEGKVHWSNKNESE-PSFEATRSRNRYSVAYaaQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 91 gSLDPRMRVRDIISEPLGRRdpaRVSELLEAVGLPAD----------AAGRYPHQFSGGQRQRISIARALAPNPSVLIAD 160
Cdd:cd03290 90 -LLNATVEENITFGSPFNKQ---RYKAVTDACSLQPDidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 161 EPVSALDVSVRKQILDL-LASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRG 212
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHA-DWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-209 |
4.67e-13 |
|
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: 67.01 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 26 VEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPErelgFLRSELQIVFQDPM-GSLDPRMRVR--DI 102
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDE----FRGSELQNYFTKLLeGDVKVIVKPQyvDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 103 I--------SEPLGRRDP-ARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQ 173
Cdd:cd03236 99 IpkavkgkvGELLKKKDErGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039688293 174 ILDLLASLVELYSLTLVfVSHDLGVVRHVCDRVAVM 209
Cdd:cd03236 178 AARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-242 |
4.83e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLerryTRR--DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRID-----TlpERE 74
Cdd:NF033858 267 IEARGL----TMRfgDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagdiaT--RRR 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 75 LGF------LRSELQiVFQDpmgsLDPRMRVRDIISEplgrRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIAR 148
Cdd:NF033858 341 VGYmsqafsLYGELT-VRQN----LELHARLFHLPAA----EIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 149 ALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTlVFVShdlgvvRHV------CDRVAVMRRGEIVelgdvdr 222
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIS------THFmneaerCDRISLMHAGRVL------- 476
|
250 260
....*....|....*....|..
gi 1039688293 223 VYDAPEheytrELLAA--APNL 242
Cdd:NF033858 477 ASDTPA-----ALVAArgAATL 493
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
6.14e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRrdVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELgfLRS 80
Cdd:PRK11614 5 MLSFDKVSAHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVfqdpmgsldprmrvrdiisePLGRRDPAR--VSELLEAVGLPADAA----------GRYPHQF----------SG 138
Cdd:PRK11614 81 AVAIV--------------------PEGRRVFSRmtVEENLAMGGFFAERDqfqerikwvyELFPRLHerriqragtmSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 139 GQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-218 |
6.36e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSElqiVFQD---PMG 91
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD---EWQRnntDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 92 SLDPR---MRVRDIISEplGRRDPARVSELLEAVGLPADAAGRYPHqFSGGQRQRISIARALAPNPSVLIADEPVSALDV 168
Cdd:PRK10938 92 SPGEDdtgRTTAEIIQD--EVKDPARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039688293 169 SVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELG 218
Cdd:PRK10938 169 ASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-194 |
7.05e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAlDKPTAGS--VSFQGKRI---DTLPE--RE 74
Cdd:PRK10938 261 IVLNNGVVSYNDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSndLTLFGRRRgsgETIWDikKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 75 LGFLRSELQivfqdpmgsLDPRM--RVRD-IIS---------EPLGRRDPARVSELLEAVGLPADAAGRYPHQFSGGQRQ 142
Cdd:PRK10938 338 IGYVSSSLH---------LDYRVstSVRNvILSgffdsigiyQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039688293 143 RISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSH 194
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-249 |
8.77e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 29 GQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSfqgkrIDtlPERELGFLRSElQIVFQDP-------MG---------- 91
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS-----LD--PNERLGKLRQD-QFAFEEFtvldtviMGhtelwevkqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 92 ----------SLDPRMRVRDI---ISEPLGRRDPARVSELLEAVGLPADaagryphQFSG-------GQRQRISIARALA 151
Cdd:PRK15064 99 rdriyalpemSEEDGMKVADLevkFAEMDGYTAEARAGELLLGVGIPEE-------QHYGlmsevapGWKLRVLLAQALF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 PNPSVLIADEPVSALDV-SVRkqildLLASLVELYSLTLVFVSHDlgvvRH----VCDRVAVMRRGEIvelgdvdRVYDA 226
Cdd:PRK15064 172 SNPDILLLDEPTNNLDInTIR-----WLEDVLNERNSTMIIISHD----RHflnsVCTHMADLDYGEL-------RVYPG 235
|
250 260 270
....*....|....*....|....*....|
gi 1039688293 227 PEHEY------TRE-LLAAAPNLRAELARL 249
Cdd:PRK15064 236 NYDEYmtaatqARErLLADNAKKKAQIAEL 265
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-220 |
1.57e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTlperelgflrs 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----------- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 ELQIVFQDpMGSLdPRMrvrDIISEPLGRRD-----------PARVSEL-----LEAVGLPAdAAGRYPHQFSGGQRQRI 144
Cdd:TIGR01257 2006 NISDVHQN-MGYC-PQF---DAIDDLLTGREhlylyarlrgvPAEEIEKvanwsIQSLGLSL-YADRLAGTYSGGNKRKL 2079
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 145 SIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDV 220
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-222 |
1.78e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 17 HALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQgkridtlPERELGFLRSELQivfqdpmgsLDPR 96
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIKVGYLPQEPQ---------LDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDIISEPLGRR---------------DP-----------ARVSELLEAVGL---------PADAAgRYP------HQ 135
Cdd:TIGR03719 83 KTVRENVEEGVAEIkdaldrfneisakyaEPdadfdklaaeqAELQEIIDAADAwdldsqleiAMDAL-RCPpwdadvTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 136 FSGGQRQRISIARALAPNPSVLIADEPVSALDV-SVrkqilDLLASLVELYSLTLVFVSHDlgvvRHVCDRVAvmrrGEI 214
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAeSV-----AWLERHLQEYPGTVVAVTHD----RYFLDNVA----GWI 228
|
....*...
gi 1039688293 215 VELgdvDR 222
Cdd:TIGR03719 229 LEL---DR 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-214 |
2.98e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.96 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 29 GQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSF-QGKRIDTLPERELGFLR---SELQivfqdPMGSLDPR---MRVRD 101
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEFLRadeSPLQ-----HLARLAPQeleQKLRD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 102 iiseplgrrdparvseLLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASl 181
Cdd:PRK10636 413 ----------------YLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID- 475
|
170 180 190
....*....|....*....|....*....|...
gi 1039688293 182 velYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:PRK10636 476 ---FEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-181 |
3.81e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPT--AGSVSFQGKRIDTLPERELGFlrselqiVFQDPMgsLDPR 96
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRTGF-------VTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 97 MRVRDII--------SEPLGRRDPARVSE-LLEAVGLPADAAGRYPHQF----SGGQRQRISIARALAPNPSVLIADEPV 163
Cdd:PLN03211 155 LTVRETLvfcsllrlPKSLTKQEKILVAEsVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPT 234
|
170
....*....|....*...
gi 1039688293 164 SALDVSVRKQILDLLASL 181
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-208 |
7.48e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.81 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 21 GVSFDVEAGQRF-----GIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK--------RIDTlPERELGFLRSELQIVFQ 87
Cdd:COG1245 353 GFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqyiSPDY-DGTVEEFLRSANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 88 DPMgsldprmrVRDIISEPLGrrdparVSELLEavglpadaagRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALD 167
Cdd:COG1245 432 SSY--------YKTEIIKPLG------LEKLLD----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039688293 168 VSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAV 208
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-214 |
9.22e-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: 64.46 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 22 VSFDVEAGQRFGIVGESGSGKSTLVR-LLAALDKPTAGSVSFQGKRIDT-------------LPE-RELGFLRSELQIVF 86
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIrnpaqairagiamVPEdRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 87 QDPMGSLDP---RMRVRDIISEPLGRRDPARVSELLEAVGLPAdaaGRyphqFSGGQRQRISIARALAPNPSVLIADEPV 163
Cdd:TIGR02633 359 NITLSVLKSfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLPI---GR----LSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 164 SALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-229 |
1.24e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 13 RRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAA-LDKPTA-------GSVSFQGKRIDTLPERELGFLRSELQI 84
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 85 VFQDPMGsldprMRVRDIISepLGRRDPARVS-ELLEAVGLPADAA----------GRYPHQFSGGQRQRISIARALA-- 151
Cdd:PRK13547 91 AAQPAFA-----FSAREIVL--LGRYPHARRAgALTHRDGEIAWQAlalagatalvGRDVTTLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 152 -------PNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIVELGDVDRVY 224
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
....*
gi 1039688293 225 dAPEH 229
Cdd:PRK13547 244 -TPAH 247
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-215 |
1.63e-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: 61.51 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTA---GSVSFQGKRIDTLPERELGflrselQIVFQDPMGSLDP 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPG------EIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 RMRVRdiiseplgrrdparvsELLEAVglpADAAG-RYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQI 174
Cdd:cd03233 97 TLTVR----------------ETLDFA---LRCKGnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039688293 175 LDLLASLVELYSLTLVF-VSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:cd03233 158 LKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-239 |
2.44e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 31 RFGIVGESGSGKSTLvrlLAALDKPTAGSvsfqgkRIDTlpERELGFLRSELQivfqdpmgsldpRMRVRdiISEPLgrr 110
Cdd:PRK13549 349 RDGIVPVMGVGKNIT---LAALDRFTGGS------RIDD--AAELKTILESIQ------------RLKVK--TASPE--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 111 dpARVSELleavglpadaagryphqfSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLV 190
Cdd:PRK13549 401 --LAIARL------------------SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAII 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039688293 191 FVSHDLGVVRHVCDRVAVMRRGEIVElgdvdrvyDAPEHEYTRE-LLAAA 239
Cdd:PRK13549 460 VISSELPEVLGLSDRVLVMHEGKLKG--------DLINHNLTQEqVMEAA 501
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-207 |
3.59e-11 |
|
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: 62.65 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgkridtlperELGflrSE 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-------------EIG---ET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDPM-GSLDPRMRVRDIISE-----PLGRRD-PARVseLLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNP 154
Cdd:TIGR03719 385 VKLAYVDQSrDALDPNKTVWEEISGgldiiKLGKREiPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 155 SVLIADEPVSALDVsvrkQILDLLASLVELYSLTLVFVSHDlgvvRHVCDRVA 207
Cdd:TIGR03719 463 NVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD----RWFLDRIA 507
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-215 |
4.74e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERE-----LGFLRSELQIVFQdpm 90
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEalengISMVHQELNLVLQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 91 gsldprMRVRDIISepLGR--------------RDPARVSELLEAVGLPADAAGryphQFSGGQRQRISIARALAPNPSV 156
Cdd:PRK10982 88 ------RSVMDNMW--LGRyptkgmfvdqdkmyRDTKAIFDELDIDIDPRAKVA----TLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-215 |
7.03e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhaLRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKridtlpeRELGFLRse 81
Cdd:PRK15064 320 LEVENLTKGFDNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-------ANIGYYA-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 lqivfQDPMGSLDPRMRVRDIISE-------------PLGRrdparvseLLeavgLPADAAGRYPHQFSGGQRQRISIAR 148
Cdd:PRK15064 389 -----QDHAYDFENDLTLFDWMSQwrqegddeqavrgTLGR--------LL----FSQDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 149 ALAPNPSVLIADEPVSALDVsvrkQILDLLASLVELYSLTLVFVSHDLGVVRHVCDRVAVMRRGEIV 215
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-208 |
8.23e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 23 SFDVEAGQRF-----GIVGESGSGKSTLVRLLAALDKPTAGSVSfqgkridtlperelgflrSELQIVFQDPMGSLDPRM 97
Cdd:PRK13409 354 SLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------------PELKISYKPQYIKPDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEPLGRRDPARV-SELLEAVGLPaDAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILD 176
Cdd:PRK13409 416 TVEDLLRSITDDLGSSYYkSEIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494
|
170 180 190
....*....|....*....|....*....|..
gi 1039688293 177 LLASLVELYSLTLVFVSHDLGVVRHVCDRVAV 208
Cdd:PRK13409 495 AIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-175 |
1.29e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALdKPTAGSVSFQGKRIDTLP----ERELGF 77
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTlqtwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVFQDPMGSLDPRMRVRD----IISEPLGRRD-----PARVSELLEAVGlpadaagrypHQFSGGQRQRISIAR 148
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQWSDeeiwKVAEEVGLKSvieqfPDKLDFVLVDGG----------YVLSNGHKQLMCLAR 1366
|
170 180
....*....|....*....|....*..
gi 1039688293 149 ALAPNPSVLIADEPVSALDvSVRKQIL 175
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLD-PVTLQII 1392
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-195 |
1.46e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgkRIDTlperelgflrsELQIVFQDPM-GSLDPRM 97
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----HCGT-----------KLEVAYFDQHrAELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISEplGRRDparvselLEAVGLPADAAGrYPHQF--------------SGGQRQRISIARA-LAPNpSVLIADEP 162
Cdd:PRK11147 399 TVMDNLAE--GKQE-------VMVNGRPRHVLG-YLQDFlfhpkramtpvkalSGGERNRLLLARLfLKPS-NLLILDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 1039688293 163 VSALDVsvrkQILDLLASLVELYSLTLVFVSHD 195
Cdd:PRK11147 468 TNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-206 |
1.50e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 26 VEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQG--------KRIDTLP----------ERELGFLRSELQIVFQ 87
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPqpaleyvidgDREYRQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 88 DPMGSLdprmrvrdiISEPLGRRDP-------ARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIAD 160
Cdd:PRK10636 104 RNDGHA---------IATIHGKLDAidawtirSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039688293 161 EPVSALDVSVRKQILDLLASlvelYSLTLVFVSHDLGVVRHVCDRV 206
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKWLKS----YQGTLILISHDRDFLDPIVDKI 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-167 |
1.70e-10 |
|
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: 59.87 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTL----VRLLAaldkpTAGSVSFQGKRIDTLPERElgf 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 78 LRSELQIVFQDPM---GSLdpRMRVrdiisEPLGRRDPARVSELLEAVGLPAdAAGRYPHQ-----------FSGGQRQR 143
Cdd:cd03289 75 WRKAFGVIPQKVFifsGTF--RKNL-----DPYGKWSDEEIWKVAEEVGLKS-VIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180
....*....|....*....|....
gi 1039688293 144 ISIARALAPNPSVLIADEPVSALD 167
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-219 |
1.76e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsFQGKRIDTLPEREL---GFLRSelQIVFQDPmgsldp 95
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWimnATVRG--NILFFDE------ 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 rmrvrdiiseplgrRDPARVSELLEAVGLPADAA----------GRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSA 165
Cdd:PTZ00243 747 --------------EDAARLADAVRVSQLEADLAqlgggleteiGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 166 LDVSVRKQILDLLAsLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELGD 219
Cdd:PTZ00243 813 LDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRA-DYVVALGDGRVEFSGS 864
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-214 |
2.32e-10 |
|
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: 60.41 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 30 QRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTlperELGFLRSELQIVFQDPMgsLDPRMRVRDII---SEP 106
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQHNI--LFHHLTVAEHIlfyAQL 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 107 LGRR-DPARVS--ELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLasLVE 183
Cdd:TIGR01257 1031 KGRSwEEAQLEmeAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKY 1107
|
170 180 190
....*....|....*....|....*....|.
gi 1039688293 184 LYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-194 |
4.47e-10 |
|
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: 59.38 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 23 SFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK-RIDTLPER---ELGFLRSelQIVFqdPMGSLDPRMR 98
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVPQRpymTLGTLRD--QIIY--PDSSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 99 vrdiiseplGRRDpARVSELLEAVGLPA--------DAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSV 170
Cdd:TIGR00954 548 ---------GLSD-KDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|....
gi 1039688293 171 RKQILDLLASlvelYSLTLVFVSH 194
Cdd:TIGR00954 618 EGYMYRLCRE----FGITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-176 |
4.79e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGkRIDTLPEREL---GFLRSelQIVFqdpmGSLDP 95
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RISFSPQTSWimpGTIKD--NIIF----GLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 RMRVRDIISEPLGRRDparVSELLEAVGLPADAAGRyphQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQIL 175
Cdd:TIGR01271 515 EYRYTSVIKACQLEED---IALFPEKDKTVLGEGGI---TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
.
gi 1039688293 176 D 176
Cdd:TIGR01271 589 E 589
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-218 |
4.97e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVR-LLAALDKPTAGSVSFQGKridtlperelgflrselqiVFQDPMGSLDPRM 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------------VAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRDIISepLGRR-DPARVSELLEAVGLPAD----------AAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSAL 166
Cdd:PLN03232 694 TVRENIL--FGSDfESERYWRAIDVTALQHDldllpgrdltEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039688293 167 DVSVRKQILDllaSLV--ELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVELG 218
Cdd:PLN03232 772 DAHVAHQVFD---SCMkdELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-208 |
7.44e-10 |
|
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: 56.43 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 25 DVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERElgflrselqivfqdpmgsldprmrvrdiis 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 105 eplgrrdparvselleavglpadaagryphQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVEL 184
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....
gi 1039688293 185 YSLTLVFVSHDLGVVRHVCDRVAV 208
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-167 |
1.07e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtlpeRELGFLRS 80
Cdd:PRK13540 1 MLDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 81 elQIVFQDPMGSLDPRMRVRD-------IISEPLGRRDPARVSELLEAVGLPADAagryphqFSGGQRQRISIARALAPN 153
Cdd:PRK13540 75 --QLCFVGHRSGINPYLTLREnclydihFSPGAVGITELCRLFSLEHLIDYPCGL-------LSSGQKRQVALLRLWMSK 145
|
170
....*....|....
gi 1039688293 154 PSVLIADEPVSALD 167
Cdd:PRK13540 146 AKLWLLDEPLVALD 159
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-167 |
1.20e-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: 56.10 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAldKPTAGSVS----FQGKRIDTLPERELGFLRSElqivfqdpmgsld 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLDKNFQRSTGYVEQQ------------- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039688293 95 prmrvrDIISEPLGRRDPARVSELLEAVGLpadaagryphqfsgGQRQRISIARALAPNPSVLIADEPVSALD 167
Cdd:cd03232 88 ------DVHSPNLTVREALRFSALLRGLSV--------------EQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-167 |
1.88e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 11 YTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgkRIDTLPERELGFLRselQIVFQDPM 90
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSR---FMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 91 GSLDPRMRVRD---IISEPLGRRDPARVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARA-LAPNPSVLIaDEPVSAL 166
Cdd:PRK13543 91 PGLKADLSTLEnlhFLCGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANL 168
|
.
gi 1039688293 167 D 167
Cdd:PRK13543 169 D 169
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-176 |
2.05e-09 |
|
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: 56.79 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKridtlperelgflrselqIVFQDPMGSLDPRMR 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------------ISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 99 VRDIIsepLG-RRDPARVSELLEAVGLPADAAgRYPHQ-----------FSGGQRQRISIARALAPNPSVLIADEPVSAL 166
Cdd:cd03291 115 KENII---FGvSYDEYRYKSVVKACQLEEDIT-KFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170
....*....|
gi 1039688293 167 DVSVRKQILD 176
Cdd:cd03291 191 DVFTEKEIFE 200
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-217 |
2.31e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRDVhALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtlpERELGFLRSE 81
Cdd:PRK10522 323 LELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 82 LQIVFQDpmgsldprMRVRDIISEPLGRR-DPARVSELLEAVGLPAD---AAGRYPH-QFSGGQRQRISIARALAPNPSV 156
Cdd:PRK10522 399 FSAVFTD--------FHLFDQLLGPEGKPaNPALVEKWLERLKMAHKlelEDGRISNlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039688293 157 LIADEPVSALDVSVRKQILDLLASLVELYSLTLVFVSHDLGVVRHVcDRVAVMRRGEIVEL 217
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHA-DRLLEMRNGQLSEL 530
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-200 |
3.16e-09 |
|
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: 54.64 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRllaaldkpTAGSVSFQGKRIDTLPerelgfLRSELQIVFQDPMGSLdp 95
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLP------KFSRNKLIFIDQLQFL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 rmrvrdiiseplgrrdparvsellEAVGLPADAAGRYPHQFSGGQRQRISIARALA--PNPSVLIADEPVSALDVSVRKQ 173
Cdd:cd03238 72 ------------------------IDVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQ 127
|
170 180
....*....|....*....|....*..
gi 1039688293 174 ILDLLASLVELySLTLVFVSHDLGVVR 200
Cdd:cd03238 128 LLEVIKGLIDL-GNTVILIEHNLDVLS 153
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-209 |
5.61e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 26 VEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKrIDTLPERelgFLRSELQIVFQD-PMGSLDP--------- 95
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS-WDEVLKR---FRGTELQNYFKKlYNGEIKVvhkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 96 -RMRVRDIISEPLGRRDPA-RVSELLEAVGLpADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQ 173
Cdd:PRK13409 172 iPKVFKGKVRELLKKVDERgKLDEVVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLN 250
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039688293 174 ILDLLASLVElySLTLVFVSHDLGVVRHVCDRVAVM 209
Cdd:PRK13409 251 VARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-181 |
9.65e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYtrRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK-------RIDTLPere 74
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhRRAVCP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 75 lgflrselQIVFQdPMG---SLDPRMRVRDIIsEPLGR--------RDpARVSELLEAVGL---PADAAGryphQFSGGQ 140
Cdd:NF033858 77 --------RIAYM-PQGlgkNLYPTLSVFENL-DFFGRlfgqdaaeRR-RRIDELLRATGLapfADRPAG----KLSGGM 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039688293 141 RQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASL 181
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRI 182
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-217 |
1.08e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 55.19 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 2 IEVRDLERRYTRRD---VHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDtlpERELGFL 78
Cdd:COG4615 328 LELRGVTYRYPGEDgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 79 RSELQIVFQD------PMGsldprmrvrdiisePLGRRDPARVSELLEAVGLpAD----AAGRY-PHQFSGGQRQRISIA 147
Cdd:COG4615 405 RQLFSAVFSDfhlfdrLLG--------------LDGEADPARARELLERLEL-DHkvsvEDGRFsTTDLSQGQRKRLALL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039688293 148 RALAPNPSVLIADEPVSALDVSVRK----QILDLLASLvelySLTLVFVSHDlgvVR--HVCDRVAVMRRGEIVEL 217
Cdd:COG4615 470 VALLEDRPILVFDEWAADQDPEFRRvfytELLPELKAR----GKTVIAISHD---DRyfDLADRVLKMDYGKLVEL 538
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-216 |
1.14e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 1 MIEVRDLerryTRRDVHALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDT----------- 69
Cdd:PRK10982 250 ILEVRNL----TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgf 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 70 ---LPERELGFLRSELQIVFQDPMGSLDPRMRVRDIISEPLGRRDPARVSELLEaVGLPAdaagrypHQ-----FSGGQR 141
Cdd:PRK10982 326 alvTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMR-VKTPG-------HRtqigsLSGGNQ 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 142 QRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVElYSLTLVFVSHDLGVVRHVCDRVAVMRRGE---IVE 216
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLvagIVD 474
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-221 |
1.27e-08 |
|
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: 52.76 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 29 GQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgKRIDTLPERELGFLRSELQIVfqdpmgsldprmrvrdiiseplg 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV----IYIDGEDILEEVLDQLLLIIV----------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 109 rrdparvselleavglpadaaGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVEL---- 184
Cdd:smart00382 55 ---------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllks 113
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039688293 185 -YSLTLVFVSHDLGVVRhvcDRVAVMRRGEIVELGDVD 221
Cdd:smart00382 114 eKNLTVILTTNDEKDLG---PALLRRRFDRRIVLLLIL 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-222 |
1.73e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 29 GQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQ-GKRIDTLPerelgflrselqivfQDPmgSLDPRMRVRDIISEPL 107
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGYLP---------------QEP--QLDPEKTVRENVEEGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 108 GRR---------------DP-----------ARVSELLEAVGL---------PADAAgRYPH------QFSGGQRQRISI 146
Cdd:PRK11819 96 AEVkaaldrfneiyaayaEPdadfdalaaeqGELQEIIDAADAwdldsqleiAMDAL-RCPPwdakvtKLSGGERRRVAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039688293 147 ARALAPNPSVLIADEPVSALDV-SVrkqilDLLASLVELYSLTLVFVSHDlgvvRHVCDRVAvmrrGEIVELgdvDR 222
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAeSV-----AWLEQFLHDYPGTVVAVTHD----RYFLDNVA----GWILEL---DR 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-194 |
2.35e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 29 GQRFGIVGESGSGKSTLVRLLA--ALD-------------KPTAGSVSFQGKRIDTLPERELgFLRSELQIVFQD----- 88
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhAIDgipkncqilhveqEVVGDDTTALQCVLNTDIERTQ-LLEEEAQLVAQQrelef 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 89 PMGSLDPRMRVRDIISE-PLGRR---------------DPARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARALAP 152
Cdd:PLN03073 282 ETETGKGKGANKDGVDKdAVSQRleeiykrlelidaytAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFI 361
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039688293 153 NPSVLIADEPVSALDVSVrkqILDLLASLVElYSLTLVFVSH 194
Cdd:PLN03073 362 EPDLLLLDEPTNHLDLHA---VLWLETYLLK-WPKTFIVVSH 399
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-209 |
4.24e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 27 EAGQRFGIVGESGSGKSTLVRLLAALDKPTAGsvsfqgkRIDTLPERE--LGFLR-SELQIVFQDPM-GSLDPRMRVRDI 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDevLKRFRgTELQDYFKKLAnGEIKVAHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 103 isEPLGRRDPARVSELLEAV---GLPADAAG---------RYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDVSV 170
Cdd:COG1245 170 --DLIPKVFKGTVRELLEKVderGKLDELAEklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039688293 171 RKQILDLLASLVELYSLTLVfVSHDLGVVRHVCDRVAVM 209
Cdd:COG1245 248 RLNVARLIRELAEEGKYVLV-VEHDLAILDYLADYVHIL 285
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-167 |
5.60e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 19 LRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAldKPTAGSVsfQGK-RIDTLPERELGFLRSElQIVFQDPMGSldPRM 97
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDiRISGFPKKQETFARIS-GYCEQNDIHS--PQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 98 RVRD--IISEPLgrRDPARVS------------ELLE-------AVGLPADAAgryphqFSGGQRQRISIARALAPNPSV 156
Cdd:PLN03140 969 TVREslIYSAFL--RLPKEVSkeekmmfvdevmELVEldnlkdaIVGLPGVTG------LSTEQRKRLTIAVELVANPSI 1040
|
170
....*....|.
gi 1039688293 157 LIADEPVSALD 167
Cdd:PLN03140 1041 IFMDEPTSGLD 1051
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-207 |
8.54e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 21 GVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVsfqgkridtlperELGflrSELQIVFQDPM-GSLDPRMRV 99
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIG---ETVKLAYVDQSrDALDPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 100 RDIISE-----PLGRRD-PARV---------SELLEAVGlpadaagryphQFSGGQRQRISIARALAPNPSVLIADEPVS 164
Cdd:PRK11819 406 WEEISGgldiiKVGNREiPSRAyvgrfnfkgGDQQKKVG-----------VLSGGERNRLHLAKTLKQGGNVLLLDEPTN 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039688293 165 ALDVsvrkqilDLLASL---VELYSLTLVFVSHDlgvvRHVCDRVA 207
Cdd:PRK11819 475 DLDV-------ETLRALeeaLLEFPGCAVVISHD----RWFLDRIA 509
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-214 |
9.06e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 20 RGVSFDVEAGQRFGIVGESGSGKSTLVRLLAALDKPTAGSVSFQGK-RIDTLPERELGFLrselqivfqdpmgsldprmr 98
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGL-------------------- 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 99 vrDIISEPL---GRRDPARVSELLEA----VGLPADAAGRYPHQFSGGQRQRISIARALAPNPSVLIADEPVSALDvsvr 171
Cdd:PLN03073 586 --DLSSNPLlymMRCFPGVPEQKLRAhlgsFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---- 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039688293 172 kqiLDLLASLVE---LYSLTLVFVSHDLGVVRHVCDRVAVMRRGEI 214
Cdd:PLN03073 660 ---LDAVEALIQglvLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-218 |
1.51e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 15 DVHALRGVSFDVEAGQRFGIVGESGSGKSTLVR--LLAALDKptagsvSFQGKRIDTLPERELGFLR--SELQIVFQDPM 90
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALAR------RLHLKKEQPGNHDRIEGLEhiDKVIVIDQSPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 91 GSlDPR------MRVRDIISEPL-----GRR-------------------------------DPARVSELLEA---VGLP 125
Cdd:cd03271 81 GR-TPRsnpatyTGVFDEIRELFcevckGKRynretlevrykgksiadvldmtveealeffeNIPKIARKLQTlcdVGLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 126 ADAAGRYPHQFSGGQRQRISIARAL---APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSlTLVFVSHDLGVVRhV 202
Cdd:cd03271 160 YIKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIK-C 237
|
250
....*....|....*.
gi 1039688293 203 CDRvavmrrgeIVELG 218
Cdd:cd03271 238 ADW--------IIDLG 245
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
215-251 |
3.33e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 40.85 E-value: 3.33e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1039688293 215 VELGDVDRVYDAPEHEYTRELLAAAPNLRAELARLRG 251
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYT 37
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
213-240 |
8.66e-05 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 40.42 E-value: 8.66e-05
10 20
....*....|....*....|....*...
gi 1039688293 213 EIVELGDVDRVYDAPEHEYTRELLAAAP 240
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIP 28
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-218 |
1.10e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 130 GRYPHQFSGGQRQRISIARAL---APNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRhVCDRV 206
Cdd:PRK00635 804 GRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVK-VADYV 881
|
90
....*....|..
gi 1039688293 207 avmrrgeiVELG 218
Cdd:PRK00635 882 --------LELG 885
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-222 |
1.42e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 137 SGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELySLTLVFVSHDLGVVRHVCDRVAVMRRGEIVe 216
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT- 483
|
....*.
gi 1039688293 217 lGDVDR 222
Cdd:NF040905 484 -GELPR 488
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
137-248 |
1.50e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 137 SGGQRQRISIARALAPNPSVLIADEPVSALDVSVRKQILDLLASLVELYSLTlVFVS--------HDLgvvrhvCDRVAV 208
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVAiyqcsqdaYEL------FDKVIV 283
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039688293 209 MRRGEIVELGDVDRV--------YDAPEHEYTRELLAAAPNLRAELAR 248
Cdd:TIGR00956 284 LYEGYQIYFGPADKAkqyfekmgFKCPDRQTTADFLTSLTSPAERQIK 331
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-200 |
3.49e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 113 ARVSELLEAVGLPADAAGRYPHQFSGGQRQRISIARAL---APNPSVLIADEPVSALDVSVRKQILDLLASLVELYSlTL 189
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TV 885
|
90
....*....|.
gi 1039688293 190 VFVSHDLGVVR 200
Cdd:TIGR00630 886 VVIEHNLDVIK 896
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-201 |
7.31e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 16 VHALRGVSFDVEAGQRFGIVGESGSGKSTLV---------------------RLLAALDKPT-------AGSVSFQGKRI 67
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsieglSPAIAIDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039688293 68 DTLPERELGFLrSELQivfqDPMGSLDPRMRVRdiiseplgrrdpARVSELLEaVGLPADAAGRYPHQFSGGQRQRISIA 147
Cdd:cd03270 88 SRNPRSTVGTV-TEIY----DYLRLLFARVGIR------------ERLGFLVD-VGLGYLTLSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039688293 148 RALAPNPS--VLIADEPVSALDvsvRKQILDLLASLVELYSL--TLVFVSHDLGVVRH 201
Cdd:cd03270 150 TQIGSGLTgvLYVLDEPSIGLH---PRDNDRLIETLKRLRDLgnTVLVVEHDEDTIRA 204
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
30-71 |
9.75e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 39.27 E-value: 9.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1039688293 30 QRFGIVGESGSGKSTLVRLLAALDKPTAGsvSFQGKRIDTLP 71
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEG--DFIGLRGDALP 53
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-82 |
7.86e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.39 E-value: 7.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1039688293 34 IVGESGSGKSTLVRLLAALDKPTAGSVSFQGKRIDTLPERELGFLRSEL 82
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNL 79
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
17-52 |
8.60e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 8.60e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1039688293 17 HALRGVSFDVEAGQRFGIVGESGSGKSTLVRLLAAL 52
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| |
