|
Name |
Accession |
Description |
Interval |
E-value |
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-259 |
7.19e-179 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 492.04 E-value: 7.19e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCL 160
Cdd:COG4167 81 DYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|....*....
gi 447197775 241 PQHPITQRMIESHFTKAPT 259
Cdd:COG4167 241 PQHEVTKRLIESHFGEALT 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-259 |
1.16e-131 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 372.97 E-value: 1.16e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCL 160
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|....*....
gi 447197775 241 PQHPITQRMIESHFTKAPT 259
Cdd:PRK15112 241 PLHELTKRLIAGHFGEALT 259
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-252 |
1.62e-99 |
|
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: 299.90 E-value: 1.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRsgflRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:COG1123 260 LLEVRNLSKRYPVR----GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCKL---IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCL 160
Cdd:COG1123 336 SLRELrrrVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
250
....*....|..
gi 447197775 241 PQHPITQRMIES 252
Cdd:COG1123 496 PQHPYTRALLAA 507
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-247 |
6.02e-96 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 284.70 E-value: 6.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLRKQIQ--HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKD 81
Cdd:COG4608 7 LLEVRDLKKHFPVRGGLFGRTVGvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKL---IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRV 158
Cdd:COG4608 87 GRELRPLrrrMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 159 CLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
....*....
gi 447197775 239 ADPQHPITQ 247
Cdd:COG4608 247 ARPLHPYTQ 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-247 |
9.28e-90 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 268.76 E-value: 9.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGFLRKQIQ-HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEH 79
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPERLvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 KDYSTRCKL---IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQ 156
Cdd:PRK11308 82 ADPEAQKLLrqkIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHE 236
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250
....*....|.
gi 447197775 237 VLADPQHPITQ 247
Cdd:PRK11308 242 IFNNPRHPYTQ 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-252 |
7.07e-87 |
|
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: 261.14 E-value: 7.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP---TGGEIRVNGELLEHK 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVV-----KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKL----IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLP--EHAYFYPQMLATGQ 154
Cdd:COG0444 76 SEKELRKIrgreIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 155 KQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGET 234
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250
....*....|....*...
gi 447197775 235 HEVLADPQHPITQRMIES 252
Cdd:COG0444 236 EELFENPRHPYTRALLSS 253
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-252 |
9.03e-87 |
|
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: 258.19 E-value: 9.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:COG1124 1 MLEVRNLSVSYGQGG-----RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKrntSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARA 163
Cdd:COG1124 76 AFRRRVQMVFQDPYASLHPRHTVDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 164 LILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQH 243
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*....
gi 447197775 244 PITQRMIES 252
Cdd:COG1124 233 PYTRELLAA 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-254 |
3.24e-84 |
|
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: 261.16 E-value: 3.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLRKQIQH--AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVaPTGGEIRVNGELLEHKD 81
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFRRTVGHvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKL---IRMIFQDPNTSLNPRLQIGTILEGPLK-RNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQR 157
Cdd:COG4172 354 RRALRPLrrrMQVVFQDPFGSLSPRMTVGQIIAEGLRvHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEV 237
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|....*..
gi 447197775 238 LADPQHPITQRMIESHF 254
Cdd:COG4172 514 FDAPQHPYTRALLAAAP 530
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-232 |
5.27e-83 |
|
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: 248.19 E-value: 5.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFlrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKD-- 81
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 -YSTRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVK-DTLQRVGLLPEHAYFYPQMLATGQKQRVC 159
Cdd:cd03257 76 lRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 160 LARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-247 |
2.53e-74 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 229.59 E-value: 2.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSG----FLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELL-- 77
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 78 -EHKDYSTRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKR-NTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQK 155
Cdd:PRK15079 88 mKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250
....*....|..
gi 447197775 236 EVLADPQHPITQ 247
Cdd:PRK15079 248 EVYHNPLHPYTK 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-250 |
4.63e-64 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 210.87 E-value: 4.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLRKQIQ--HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehkD 81
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLNRVTRevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI---D 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKL------IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQK 155
Cdd:PRK10261 390 TLSPGKLqalrrdIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQR 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
|
250
....*....|....*
gi 447197775 236 EVLADPQHPITQRMI 250
Cdd:PRK10261 550 AVFENPQHPYTRKLM 564
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-242 |
3.74e-63 |
|
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: 205.91 E-value: 3.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrsgflRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTG---GEIRVNGELL 77
Cdd:COG1123 1 MTPLLEVRDLSVRY-------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 78 EHKDYSTRCKLIRMIFQDPNTSLNPrLQIGT-ILEGPlkRNTSMTPDARMRRVKDTLQRVGLlPEHAYFYPQMLATGQKQ 156
Cdd:COG1123 74 LELSEALRGRRIGMVFQDPMTQLNP-VTVGDqIAEAL--ENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHE 236
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
....*.
gi 447197775 237 VLADPQ 242
Cdd:COG1123 230 ILAAPQ 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-258 |
3.33e-60 |
|
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: 198.76 E-value: 3.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGflrkqIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLA----RMLAGMVAPTGGEIRVNGEL 76
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGG-----TVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 77 LEHKDYSTRCKL----IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLlPEHAY---FYPQM 149
Cdd:COG4172 78 LLGLSERELRRIrgnrIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERrldAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260 270
....*....|....*....|....*....|.
gi 447197775 230 EAGETHEVLADPQHPITQRMIES--HFTKAP 258
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLLAAepRGDPRP 267
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-252 |
4.55e-59 |
|
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: 188.48 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFVTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDY 82
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKL---IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVC 159
Cdd:TIGR02769 81 KQRRAFrrdVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 160 LARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|...
gi 447197775 240 DpQHPITQRMIES 252
Cdd:TIGR02769 241 F-KHPAGRNLQSA 252
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
27-242 |
1.22e-58 |
|
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: 186.00 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTslnprlQI 106
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDD------QL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 --GTILE----GPlkRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:COG1122 89 faPTVEEdvafGP--ENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 181 DMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:COG1122 166 DPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-230 |
2.15e-58 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 186.82 E-value: 2.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCKL---IRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCL 160
Cdd:PRK10419 83 QRKAFrrdIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVE 230
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-251 |
9.29e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 184.14 E-value: 9.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 2 SALLEVTNLHKDFVTRSGFLRKQI--QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVApTGGEIRVNGELLEH 79
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILKRTVdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 kdYSTRCKL-----IRMIFQDPNTSLNPRLQIGTILEGPLK-RNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATG 153
Cdd:PRK15134 352 --LNRRQLLpvrhrIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 154 QKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGE 233
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250
....*....|....*...
gi 447197775 234 THEVLADPQHPITQRMIE 251
Cdd:PRK15134 510 CERVFAAPQQEYTRQLLA 527
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-252 |
1.17e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 179.12 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSGflrkqIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYST 84
Cdd:COG1135 2 IELENLSKTFPTKGG-----PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL--TALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RcKL------IRMIFQDPNTsLNPRlqigTILEG---PLKRnTSMTPDARMRRVKDTLQRVGLlPEHAYFYPQMLATGQK 155
Cdd:COG1135 75 R-ELraarrkIGMIFQHFNL-LSSR----TVAENvalPLEI-AGVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250
....*....|....*..
gi 447197775 236 EVLADPQHPITQRMIES 252
Cdd:COG1135 227 DVFANPQSELTRRFLPT 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-242 |
4.60e-52 |
|
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: 169.30 E-value: 4.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE---LLEHK 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKV-----TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIRMIFQDPNTsLNPRlqigTILEG---PLKRnTSMTPDARMRRVKDTLQRVGLlPEHAYFYPQMLATGQKQR 157
Cdd:cd03258 76 ELRKARRRIGMIFQHFNL-LSSR----TVFENvalPLEI-AGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEV 237
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
....*
gi 447197775 238 LADPQ 242
Cdd:cd03258 229 FANPQ 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-239 |
4.30e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.77 E-value: 4.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:COG1131 1 IEVRGLTKRYGDK---------TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RcKLIRMIFQDPNtsLNPRLQIGTILE--GPLKRntsMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQKQRVCLAR 162
Cdd:COG1131 72 R-RRIGYVPQEPA--LYPDLTVRENLRffARLYG---LPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 163 ALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-232 |
7.41e-49 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 160.38 E-value: 7.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03259 1 LELKGLSKTY---------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCklIRMIFQDPntSLNPRLqigTILEG---PLKRNTSMTPDARmRRVKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLA 161
Cdd:cd03259 72 RN--IGMVFQDY--ALFPHL---TVAENiafGLKLRGVPKAEIR-ARVRELLELVGL-EGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-230 |
5.75e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.67 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtRSGflrKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG1136 1 MSPLLELRNLTKSY--GTG---EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKL----IRMIFQDPNtsLNPRLqigTILEG---PLkRNTSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATG 153
Cdd:COG1136 76 SERELARLrrrhIGFVFQFFN--LLPEL---TALENvalPL-LLAGVSRKERRERARELLERVG-LGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 154 QKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSqHIGVIKHITDKIIVMHEGDVVE 230
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVT-HDPELAARADRVIRLRDGRIVS 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-247 |
1.65e-46 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 157.96 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGflrkqIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP---TGGEIRVNG-EL 76
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDG-----DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGrEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 77 L---EHKDYSTRCKLIRMIFQDPNTSLNPRLQIGT------ILEGPLKRNTSMTPDARM-RRVK--DTLQRVGLlpehay 144
Cdd:PRK09473 84 LnlpEKELNKLRAEQISMIFQDPMTSLNPYMRVGEqlmevlMLHKGMSKAEAFEESVRMlDAVKmpEARKRMKM------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 145 fYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMH 224
Cdd:PRK09473 158 -YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250 260
....*....|....*....|...
gi 447197775 225 EGDVVEAGETHEVLADPQHPITQ 247
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSHPYSI 259
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-250 |
2.53e-46 |
|
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: 154.75 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKdfvtrsGFLRKQIQhavKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG1127 2 SEPMIEVRNLTK------SFGDRVVL---DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIR---MIFQDPN--TSLnprlqigTILEG---PLKRNTSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLAT 152
Cdd:COG1127 73 SEKELYELRRrigMLFQGGAlfDSL-------TVFENvafPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|....*...
gi 447197775 233 eTHEVLADPQHPITQRMI 250
Cdd:COG1127 225 -TPEELLASDDPWVRQFL 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-226 |
8.08e-46 |
|
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: 152.62 E-value: 8.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 23 KQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSL-N 101
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDDQFfG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 102 PrlqigTILE----GPlkRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:cd03225 91 P-----TVEEevafGL--ENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447197775 178 NGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-252 |
1.04e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.42 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 6 EVTNLHKDFVTRSgflrKQIqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE---LLEHKDY 82
Cdd:PRK11153 3 ELKNISKVFPQGG----RTI-HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKLIRMIFQDPNTsLNPRlqigTILEG---PLKrnTSMTPDARMR-RVKDTLQRVGlLPEHAYFYPQMLATGQKQRV 158
Cdd:PRK11153 78 RKARRQIGMIFQHFNL-LSSR----TVFDNvalPLE--LAGTPKAEIKaRVTELLELVG-LSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 159 CLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250
....*....|....
gi 447197775 239 ADPQHPITQRMIES 252
Cdd:PRK11153 230 SHPKHPLTREFIQS 243
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-248 |
3.68e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.99 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTrsgflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:COG1126 1 MIEIENLHKSFGD---------LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRcKLIR---MIFQDPNtsLNPRLqigTILE----GPLK-RNtsMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQK 155
Cdd:COG1126 72 IN-KLRRkvgMVFQQFN--LFPHL---TVLEnvtlAPIKvKK--MSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
250
....*....|...
gi 447197775 236 EVLADPQHPITQR 248
Cdd:COG1126 222 EFFENPQHERTRA 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-239 |
3.81e-44 |
|
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: 149.24 E-value: 3.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:COG4555 1 MIEVENLSKKY---------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRcKLIRMIFQDPNtsLNPRLqigTILE-----GPLKRntsMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQKQRV 158
Cdd:COG4555 72 AR-RQIGVLPDERG--LYDRL---TVREniryfAELYG---LFDEELKKRIEELIELLG-LEEFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 159 CLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
.
gi 447197775 239 A 239
Cdd:COG4555 221 E 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-229 |
3.90e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.44 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFVTRsgflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDY 82
Cdd:COG3638 1 PMLELRNLSKRYPGG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKL---IRMIFQDPNtsLNPRLqigTILE----------GPLKRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQM 149
Cdd:COG3638 73 RALRRLrrrIGMIFQQFN--LVPRL---SVLTnvlagrlgrtSTWRSLLGLFPPEDRERALEALERVGLA-DKAYQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-226 |
6.29e-44 |
|
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: 146.39 E-value: 6.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehKDYST 84
Cdd:cd03230 1 IEVRNLSKRYGKK---------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-----KDIKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKLIRmifqdpntslnprlqigtilegplkrntsmtpdarmrrvkdtlQRVGLLPEHAYFYPQM-------LATGQKQR 157
Cdd:cd03230 67 EPEEVK-------------------------------------------RRIGYLPEEPSLYENLtvrenlkLSGGMKQR 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-226 |
2.17e-43 |
|
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: 146.48 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03255 1 IELKNLSKTYGGG-----GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKLIR----MIFQDPNtsLNPRLqigTILEG---PLkRNTSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQKQR 157
Cdd:cd03255 76 LAAFRRrhigFVFQSFN--LLPDL---TALENvelPL-LLAGVPKKERRERAEELLERVG-LGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSqHIGVIKHITDKIIVMHEG 226
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVT-HDPELAEYADRIIELRDG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-258 |
2.61e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 153.71 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 2 SALLEVTNLHKDFvtRSGflrKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLA----RML-AGMVAPTGGEIRVNGEL 76
Cdd:PRK15134 3 QPLLAIENLSVAF--RQQ---QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLpSPPVVYPSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 77 LEHKDYST----RCKLIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGL--LPEHAYFYPQML 150
Cdd:PRK15134 78 LLHASEQTlrgvRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVE 230
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|....*...
gi 447197775 231 AGETHEVLADPQHPITQRMIESHFTKAP 258
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNSEPSGDP 265
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
2.88e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.86 E-value: 2.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTrsgflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELL--- 77
Cdd:COG3842 2 AMPALELENVSKRYGD---------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtgl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 78 --EHKDystrcklIRMIFQDPntSLNPRLqigTILEG---PLKRNtSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLAT 152
Cdd:COG3842 73 ppEKRN-------VGMVFQDY--ALFPHL---TVAENvafGLRMR-GVPKAEIRARVAELLELVG-LEGLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSqhigvikH-------ITDKIIVMHE 225
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVT-------HdqeealaLADRIAVMND 211
|
250
....*....|....*....
gi 447197775 226 GDVVEAGETHEVLADPQHP 244
Cdd:COG3842 212 GRIEQVGTPEEIYERPATR 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-245 |
5.93e-43 |
|
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: 146.11 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE----LLEHK 80
Cdd:cd03261 1 IELRGLTKSFGGR---------TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisgLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKlIRMIFQDPN--TSLnprlqigTILEG---PLKRNTSMTPDARMRRVKDTLQRVGLLPEhAYFYPQMLATGQK 155
Cdd:cd03261 72 LYRLRRR-MGMLFQSGAlfDSL-------TVFENvafPLREHTRLSEEEIREIVLEKLEAVGLRGA-EDLYPAELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
250
....*....|
gi 447197775 236 EVLADpQHPI 245
Cdd:cd03261 223 ELRAS-DDPL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-226 |
6.17e-43 |
|
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: 144.25 E-value: 6.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrsgflrKQIQhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03229 1 LELKNVSKRY--------GQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RC--KLIRMIFQDPNtsLNPRLQIgtilegplkrntsmtpdarmrrvkdtLQRVGLLpehayfypqmLATGQKQRVCLAR 162
Cdd:cd03229 72 PPlrRRIGMVFQDFA--LFPHLTV--------------------------LENIALG----------LSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 163 ALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-260 |
9.65e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 145.43 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFVTRSGFLRkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP----TGGEIRVNGELLE 78
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVK-----AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 79 HKDYSTRCKLIR----MIFQDPNTSLNPRLQIGT-----ILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYF--YP 147
Cdd:COG4170 77 KLSPRERRKIIGreiaMIFQEPSSCLDPSAKIGDqlieaIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMnsYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 148 QMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGD 227
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
250 260 270
....*....|....*....|....*....|...
gi 447197775 228 VVEAGETHEVLADPQHPITQRMIEShftkAPTF 260
Cdd:COG4170 237 TVESGPTEQILKSPHHPYTKALLRS----MPDF 265
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-240 |
4.72e-41 |
|
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: 141.80 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 24 QIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGelLEHKDYSTRcKLIR----MIFQDPNTS 99
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENL-WEIRkkvgMVFQNPDNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 100 LnprlqIGTILE-----GPLKRNtsmTPDARMR-RVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIA 173
Cdd:TIGR04520 90 F-----VGATVEddvafGLENLG---VPREEMRkRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 174 DEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIG-VIKhiTDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-250 |
1.27e-40 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 147.69 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLRkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKD-- 81
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIA-----AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 ------------YSTRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYF--YP 147
Cdd:PRK10261 87 vielseqsaaqmRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILsrYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 148 QMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGD 227
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|...
gi 447197775 228 VVEAGETHEVLADPQHPITQRMI 250
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALL 269
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-178 |
1.43e-40 |
|
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: 137.01 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNtsLNPRLQIGT 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 109 IL--EGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:pfam00005 79 NLrlGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
2.25e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGflrkqIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGG-----GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYStrcklIRMIFQDPntSLNPRLqigTILE----GPlkRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQ 156
Cdd:COG1116 79 GPD-----RGVVFQEP--ALLPWL---TVLDnvalGL--ELRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSqhigvikH-------ITDKIIVM 223
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVT-------HdvdeavfLADRVVVL 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-242 |
2.33e-40 |
|
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: 139.11 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03219 1 LEVRGLTKRF---GGL------VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKL-IRMIFQdpNTSLNPRLqigTILE----GPLKRNTSMTPDARMR--------RVKDTLQRVGlLPEHAYFYPQMLA 151
Cdd:cd03219 72 IARLgIGRTFQ--IPRLFPEL---TVLEnvmvAAQARTGSGLLLARARreereareRAEELLERVG-LADLADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 152 TGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEA 231
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|.
gi 447197775 232 GETHEVLADPQ 242
Cdd:cd03219 225 GTPDEVRNNPR 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-229 |
3.28e-39 |
|
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: 136.54 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrsgflrKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEL---LEHKD 81
Cdd:cd03256 1 IEVENLSKTY--------PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKLIRMIFQDPNtsLNPRLQIGT-ILEGPLKRNT------SMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQ 154
Cdd:cd03256 73 LRQLRRQIGMIFQQFN--LIERLSVLEnVLSGRLGRRStwrslfGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 155 KQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-223 |
9.85e-39 |
|
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: 134.52 E-value: 9.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSGFLrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLE--HKDy 82
Cdd:cd03293 1 LEVRNVSKTYGGGGGAV-----TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 strcklIRMIFQDPntSLNPRLqigTILEG---PLKRNtSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVC 159
Cdd:cd03293 75 ------RGYVFQQD--ALLPWL---TVLDNvalGLELQ-GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 160 LARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVM 223
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-226 |
1.48e-38 |
|
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: 131.98 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQdpntslnprlq 105
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 igtilegplkrntsmtpdarmrrvkdtlqrvgllpehayfypqmLATGQKQRVCLARALILQPSIIIADEALNGLDMAMR 185
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447197775 186 SQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-252 |
1.76e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 136.80 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFVTRSGFLRkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTG----GEIRVNGELLE 78
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 79 HKDYSTRCKLI----RMIFQDPNTSLNPRLQIG-TILEGpLKRNTSMTPDARMRRVKDTLQRVGLlPEHAY---FYPQML 150
Cdd:PRK11022 77 RISEKERRNLVgaevAMIFQDPMTSLNPCYTVGfQIMEA-IKVHQGGNKKTRRQRAIDLLNQVGI-PDPASrldVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVE 230
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250 260
....*....|....*....|..
gi 447197775 231 AGETHEVLADPQHPITQRMIES 252
Cdd:PRK11022 235 TGKAHDIFRAPRHPYTQALLRA 256
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
26-242 |
1.25e-37 |
|
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: 131.98 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE----LLEHKdystrcKLIRMIFQdpNTSLN 101
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnLPPHK------RPVNTVFQ--NYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 102 PRLQIGTILEGPLKRNtSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:cd03300 85 PHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 182 MAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-226 |
6.38e-37 |
|
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: 128.27 E-value: 6.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlq 105
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDP--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 igTILEGPLKRNtsmtpdarmrrvkdtlqrvgllpehayfypqMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMR 185
Cdd:cd03228 86 --FLFSGTIREN-------------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447197775 186 SQILNLFLELQEEMGVsfVYVSQHIGVIKHiTDKIIVMHEG 226
Cdd:cd03228 133 ALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-238 |
7.63e-37 |
|
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: 136.81 E-value: 7.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQdpntslNPRLQ 105
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQ------NPYLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IGTILEgplkrNTSM-TPDARMRRVKDTLQRVGLLPEHAYFyPQMLAT-----------GQKQRVCLARALILQPSIIIA 173
Cdd:COG4988 424 AGTIRE-----NLRLgRPDASDEELEAALEAAGLDEFVAAL-PDGLDTplgeggrglsgGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 174 DEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHItDKIIVMHEGDVVEAGeTHEVL 238
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQA-DRILVLDDGRIVEQG-THEEL 558
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-239 |
9.03e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 9.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNG-ELLEHKDYSTRcKLIRMIFQDPNTSLnprl 104
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmVLSEETVWDVR-RQVGMVFQNPDNQF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 qIGTILEGPLK---RNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:PRK13635 95 -VGATVQDDVAfglENIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 182 MAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-233 |
1.88e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR---MIFQDpnTSLNP 102
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRrigVVFQD--FRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLqigTILEG---PLkRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNG 179
Cdd:COG2884 93 DR---TVYENvalPL-RVTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447197775 180 LDMAMRSQILNLFLELQeEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGE 233
Cdd:COG2884 168 LDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-226 |
3.32e-36 |
|
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: 127.65 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTrsgflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03262 1 IEIKNLHKSFGD---------FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RckLIR----MIFQDPNtsLNPRLQI-GTILEGPLKRNtSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVC 159
Cdd:cd03262 72 N--ELRqkvgMVFQQFN--LFPHLTVlENITLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 160 LARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-241 |
3.64e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 128.57 E-value: 3.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 20 FLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQdpnts 99
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 100 lnprlQIGTILEGPLKRNTSMTP-------DARMRRVKDTLQRVGLLPEH-AYFYPQMLATGQKQRVCLARALILQPSII 171
Cdd:cd03295 83 -----QIGLFPHMTVEENIALVPkllkwpkEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 172 IADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
29-254 |
4.86e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 128.62 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSLNprlqiGT 108
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAPFG-----LT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILE----------GPLKRNTsmtpDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:COG1120 92 VRElvalgryphlGLFGRPS----AEDREAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 179 GLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLadpqhpiTQRMIESHF 254
Cdd:COG1120 167 HLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-------TPELLEEVY 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-242 |
8.56e-36 |
|
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: 128.53 E-value: 8.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTR---------SGFLRKQIQH------AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGE 69
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllaKGKSKEEILKktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 70 IRVNGE---LLEHKDYST-RCKLIRMIFQdpNTSLNPRLqigTILEgplkrNTS-------MTPDARMRRVKDTLQRVGL 138
Cdd:cd03294 81 VLIDGQdiaAMSRKELRElRRKKISMVFQ--SFALLPHR---TVLE-----NVAfglevqgVPRAEREERAAEALELVGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 139 LPeHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITD 218
Cdd:cd03294 151 EG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGD 229
|
250 260
....*....|....*....|....
gi 447197775 219 KIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:cd03294 230 RIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
27-237 |
1.16e-35 |
|
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: 126.91 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMV-----APTGGEIRVNGELLEHKDY---STRCKlIRMIFQDPNt 98
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlELRRR-VGMVFQKPN- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 99 slnprlqigtILEGPLKRNTSMTP--------DARMRRVKDTLQRVGLLPE-----HAYfypqMLATGQKQRVCLARALI 165
Cdd:cd03260 92 ----------PFPGSIYDNVAYGLrlhgiklkEELDERVEEALRKAALWDEvkdrlHAL----GLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 166 LQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEV 237
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
28-239 |
2.99e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 133.04 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDpntslnPRLQIG 107
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQD------VFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEgplkrNTSMT-PDARMRRVKDTLQRVGL------LPeHAYFYP-----QMLATGQKQRVCLARALILQPSIIIADE 175
Cdd:COG2274 564 TIRE-----NITLGdPDATDEEIIEAARLAGLhdfieaLP-MGYDTVvgeggSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 176 ALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLA 698
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
4.39e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.34 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSalLEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllehk 80
Cdd:COG1118 1 MS--IEVRNISKRF---GSF------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKL----IRMIFQDPntSLNPRLqigTILE----GPLKRNTSmtPDARMRRVKDTLQRVGLlPEHAYFYPQMLAT 152
Cdd:COG1118 65 DLFTNLPPrerrVGFVFQHY--ALFPHM---TVAEniafGLRVRPPS--KAEIRARVEELLELVQL-EGLADRYPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSqhigvikH-------ITDKIIVMHE 225
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVT-------HdqeealeLADRVVVMNQ 209
|
250
....*....|....*....
gi 447197775 226 GDVVEAGETHEVLADPQHP 244
Cdd:COG1118 210 GRIEQVGTPDEVYDRPATP 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-226 |
5.08e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.54 E-value: 5.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSGFlrkqiqhavKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehKDYST 84
Cdd:COG4619 1 LELEGLSFRVGGKPIL---------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG-----KPLSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 ------RcKLIRMIFQDP----NTslnprlqIGTILEGPLK-RNTSMTPDarmrRVKDTLQRVGlLPEHAYFYP-QMLAT 152
Cdd:COG4619 67 mpppewR-RQVAYVPQEPalwgGT-------VRDNLPFPFQlRERKFDRE----RALELLERLG-LPPDILDKPvERLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-238 |
5.87e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHkdfVTRSGflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG1121 3 MMPAIELENLT---VSYGG------RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DystrcKLIRMIFQdpNTSLNPRLQIgTILE----------GPLKRNTSmtpdARMRRVKDTLQRVGLLPehayFYPQML 150
Cdd:COG1121 74 R-----RRIGYVPQ--RAEVDWDFPI-TVRDvvlmgrygrrGLFRRPSR----ADREAVDEALERVGLED----LADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 151 AT---GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGd 227
Cdd:COG1121 138 GElsgGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG- 215
|
250
....*....|.
gi 447197775 228 VVEAGETHEVL 238
Cdd:COG1121 216 LVAHGPPEEVL 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-234 |
9.49e-35 |
|
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: 124.47 E-value: 9.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 2 SALLEVTNLHKDFVTRSGFLrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKD 81
Cdd:COG4181 6 APIIELRGLTKTVGTGAGEL-----TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKL----IRMIFQdpNTSLNPRLqigTILEgplkrNTsMTP-------DARmRRVKDTLQRVGlLPEHAYFYPQML 150
Cdd:COG4181 81 EDARARLrarhVGFVFQ--SFQLLPTL---TALE-----NV-MLPlelagrrDAR-ARARALLERVG-LGHRLDHYPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVE 230
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
....
gi 447197775 231 AGET 234
Cdd:COG4181 227 DTAA 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-241 |
8.52e-34 |
|
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: 125.21 E-value: 8.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehkdYSTRCKL--------IRMIFQDPntSLNPR 103
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL----QDSARGIflpphrrrIGYVFQEA--RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLpEHayfYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMA 183
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLL-DR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 184 MRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
33-244 |
9.04e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.17 E-value: 9.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 33 SFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRckLIRMIFQDPN--TSLNPRLQIGTIL 110
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--PVSMLFQENNlfPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 111 EGPLKrntsMTPDARmRRVKDTLQRVGLlpehAYF---YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:COG3840 97 RPGLK----LTAEQR-AQVEQALERVGL----AGLldrLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 188 ILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHP 244
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-239 |
9.96e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 122.11 E-value: 9.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDF-------------VTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTG 67
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 68 GEIRVNGE---LLEHkdystrcklirmifqdpNTSLNPRLQ-------IGTILeGplkrntsMTP---DARMRRVKD--T 132
Cdd:COG1134 81 GRVEVNGRvsaLLEL-----------------GAGFHPELTgreniylNGRLL-G-------LSRkeiDEKFDEIVEfaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 133 LQRVGLLPEHAYfypqmlATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGV 212
Cdd:COG1134 136 LGDFIDQPVKTY------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGA 208
|
250 260
....*....|....*....|....*..
gi 447197775 213 IKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:COG1134 209 VRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-232 |
1.37e-33 |
|
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: 120.78 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehkdyst 84
Cdd:cd03268 1 LKTNDLTKTYGKK---------RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 rcklirmifQDPNTSLNPRLQIGTILEGP-----------LKRNTSMtPDARMRRVKDTLQRVGlLPEHAYFYPQMLATG 153
Cdd:cd03268 62 ---------KSYQKNIEALRRIGALIEAPgfypnltarenLRLLARL-LGIRKKRIDEVLDVVG-LKDSAKKKVKGFSLG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 154 QKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSfVYVSQHI-GVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GIT-VLISSHLlSEIQKVADRIGIINKGKLIEEG 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-252 |
1.68e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 121.96 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGFLRkqiqhavkpVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRV---NGELL 77
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRD---------VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 78 E--HKDYSTRCKLIR----MIFQDPNTSLNPRLQIGTILEGPLkrntsMTPDAR-MRRVKDT----LQRVGLLPEHAYFY 146
Cdd:PRK11701 74 DlyALSEAERRRLLRtewgFVHQHPRDGLRMQVSAGGNIGERL-----MAVGARhYGDIRATagdwLERVEIDAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 147 PQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|....*.
gi 447197775 227 DVVEAGETHEVLADPQHPITQRMIES 252
Cdd:PRK11701 229 RVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-243 |
4.35e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.26 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDY 82
Cdd:COG3839 2 ASLELENVSKSY---GGV------EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCklIRMIFQDPntSLNPRLqigTILEG---PLKrNTSMTPDARMRRVKDTLQRVGLLPeHAYFYPQMLATGQKQRVC 159
Cdd:COG3839 73 KDRN--IAMVFQSY--ALYPHM---TVYENiafPLK-LRKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 160 LARALILQPSIIIADEALNGLD----MAMRSQIlnlfLELQEEMGVSFVYVSqhigvikH-------ITDKIIVMHEGDV 228
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrVEMRAEI----KRLHRRLGTTTIYVT-------HdqveamtLADRIAVMNDGRI 212
|
250
....*....|....*
gi 447197775 229 VEAGETHEVLADPQH 243
Cdd:COG3839 213 QQVGTPEELYDRPAN 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-250 |
5.82e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG1129 1 AEPLLEMRGISKSF---GGV------KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKL-IRMIFQDPNtsLNPRLqigTILE----GPLKRNTSMTPDARMRR-VKDTLQRVGL-LPehayfyPQM---- 149
Cdd:COG1129 72 SPRDAQAAgIAIIHQELN--LVPNL---SVAEniflGREPRRGGLIDWRAMRRrARELLARLGLdID------PDTpvgd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADE---ALNgldmamRSQILNLF---LELQEEmGVSFVYVSQHIGVIKHITDKIIVM 223
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEptaSLT------EREVERLFriiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
250 260
....*....|....*....|....*..
gi 447197775 224 HEGDVVEAGETHEVladPQHPITQRMI 250
Cdd:COG1129 214 RDGRLVGTGPVAEL---TEDELVRLMV 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-240 |
7.64e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.96 E-value: 7.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGelLEHKDYSTRCKlIR----MIFQDPNTSLnpr 103
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWD-IRnkagMVFQNPDNQI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 lqIGTILE-----GPlkRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:PRK13633 99 --VATIVEedvafGP--ENLGIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 179 GLDMAMRSQILNLFLELQEEMGVSFVYVSQHIG-VIKhiTDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEeAVE--ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
8.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.63 E-value: 8.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSLnprlqIG 107
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQF-----VG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLK---RNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAM 184
Cdd:PRK13648 99 SIVKYDVAfglENHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 185 RSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
26-232 |
1.06e-32 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 118.90 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEL---LEHKDystrcKLIRMIFQdpNTSLNP 102
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdLPPKD-----RDIAMVFQ--NYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIGTILEGPLKRNTSMTP--DARMRRVKDTLQRVGLLPEhayfYPQMLATGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:cd03301 86 HMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEHLLDR----KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447197775 181 DMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
29-232 |
1.50e-32 |
|
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: 117.15 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQdpntslnprlqigt 108
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ilegplkrntsmtpdarmrrvkdTLQRVGLLP-EHAYFypQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:cd03214 81 -----------------------ALELLGLAHlADRPF--NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447197775 188 ILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-252 |
1.78e-32 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 121.06 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVTRSGFLRkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP----TGGEIRVNGELLEH 79
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVK-----AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 KDYSTRCKLIR----MIFQDPNTSLNPRLQIGTILEGPLKRNTSMTP-----DARMRRVKDTLQRVGLLPEHAYF--YPQ 148
Cdd:PRK15093 78 LSPRERRKLVGhnvsMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIKDHKDAMrsFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 149 MLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDV 228
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260
....*....|....*....|....
gi 447197775 229 VEAGETHEVLADPQHPITQRMIES 252
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRA 261
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-240 |
2.53e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.57 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehkDYSTRC-----KLIRMIFQDPNTSLN 101
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYSRKGlmklrESVGMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 102 PRLQIGTILEGPLkrNTSMTPDARMRRVKDTLQRVGLlpEHAYFYP-QMLATGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:PRK13636 97 SASVYQDVSFGAV--NLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 181 DMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-237 |
3.52e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSalLEVTNLHKDFVTRSGFLRKqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGelLEHK 80
Cdd:PRK13637 1 MS--IKIENLTHIYMEGTPFEKK----ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIR----MIFQDPNTSLNPRLQIGTILEGPlkRNTSMTPDARMRRVKDTLQRVGLLPE-HAYFYPQMLATGQK 155
Cdd:PRK13637 73 DKKVKLSDIRkkvgLVFQYPEYQLFEETIEKDIAFGP--INLGLSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
..
gi 447197775 236 EV 237
Cdd:PRK13637 231 EV 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
1.35e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSLnprlqIG 107
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNQF-----IG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLK---RNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAM 184
Cdd:PRK13632 99 ATVEDDIAfglENKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 185 RSQILNLFLELQEEMGVSFVYVSQHIG-VIKhiTDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK13632 178 KREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-232 |
1.41e-31 |
|
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: 115.86 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEaGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELL----EHKDYSTRCKLIRMIFQdpNTSLNPRLQIG 107
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQ--QYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRNTSMTPDARMRRVKDTLQRVGLLpehaYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLDHLL----NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447197775 188 ILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-243 |
1.61e-31 |
|
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: 121.80 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 24 QIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDP---NTSL 100
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPhlfDTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 101 --NprLQIGtilegplkrntsmTPDARMRRVKDTLQRVGLlpehAYFY---PQMLAT-----------GQKQRVCLARAL 164
Cdd:COG4987 426 reN--LRLA-------------RPDATDEELWAALERVGL----GDWLaalPDGLDTwlgeggrrlsgGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 165 ILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHItDKIIVMHEGDVVEAGETHEVLADPQH 243
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-239 |
2.90e-31 |
|
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: 115.40 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNG-ELLEHKDYSTRcKLIRMIFQDPntslnprlq 105
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGiDIRDISRKSLR-SMIGVVLQDT--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 igTILEGPLKRNTSM-TPDARMRRVKDTLQRVGL------LPEHAYFYP----QMLATGQKQRVCLARALILQPSIIIAD 174
Cdd:cd03254 87 --FLFSGTIMENIRLgRPNATDEEVIEAAKEAGAhdfimkLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEemGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-251 |
5.47e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.23 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALlEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRV-NGELLEH 79
Cdd:PRK11264 1 MSAI-EVKNLVKKF---------HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIDTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 KDYSTRCKLIR-------MIFQdpNTSLNP-RLQIGTILEGPL--KRNTSMTPDARMRRVkdtLQRVGLL-PEHAYfyPQ 148
Cdd:PRK11264 71 RSLSQQKGLIRqlrqhvgFVFQ--NFNLFPhRTVLENIIEGPVivKGEPKEEATARAREL---LAKVGLAgKETSY--PR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 149 MLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGvSFVYVSQHIGVIKHITDKIIVMHEGDV 228
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
250 260
....*....|....*....|...
gi 447197775 229 VEAGETHEVLADPQHPITQRMIE 251
Cdd:PRK11264 223 VEQGPAKALFADPQQPRTRQFLE 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-244 |
7.40e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.80 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGelLEHKDYSTRCKLIR----MIFQDPNtsLNPRLqig 107
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIRqeagMVFQQFY--LFPHL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILE----GPLKRNTSMTPDARmRRVKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMA 183
Cdd:PRK09493 93 TALEnvmfGPLRVRGASKEEAE-KQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 184 MRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHP 244
Cdd:PRK09493 171 LRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-250 |
1.50e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKdfvtRSGflrkqiQHAV-KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE---LLEHK 80
Cdd:PRK10619 6 LNVIDLHK----RYG------EHEVlKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRC------KLIR----MIFQDPNT-SLNPRLQigTILEGPLKRNTSMTPDARMRRVKdTLQRVGLLPEHAYFYPQM 149
Cdd:PRK10619 76 DGQLKVadknqlRLLRtrltMVFQHFNLwSHMTVLE--NVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250 260
....*....|....*....|.
gi 447197775 230 EAGETHEVLADPQHPITQRMI 250
Cdd:PRK10619 232 EEGAPEQLFGNPQSPRLQQFL 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-244 |
6.93e-30 |
|
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: 112.05 E-value: 6.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrSGFLrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03296 3 IEVRNVSKRF---GDFV------ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCklIRMIFQdpNTSLNPRLqigTILEG-----PLKRNTSMTPDARMR-RVKDTLQRVGLlPEHAYFYPQMLATGQKQRV 158
Cdd:cd03296 74 RN--VGFVFQ--HYALFRHM---TVFDNvafglRVKPRSERPPEAEIRaKVHELLKLVQL-DWLADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 159 CLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....*.
gi 447197775 239 ADPQHP 244
Cdd:cd03296 226 DHPASP 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-229 |
6.96e-30 |
|
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: 111.44 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrsgflRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehKDYST 84
Cdd:cd03263 1 LQIRNLTKTY-------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-----YSIRT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKLIRM----IFQDpNT---SLNPR--LQIGTILEGplkrntsmTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQK 155
Cdd:cd03263 69 DRKAARQslgyCPQF-DAlfdELTVRehLRFYARLKG--------LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEemGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
1.46e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS---TRcKLIRMIFQDPNTSL-NPR 103
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVR-KTVGIVFQNPDDQLfAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQiGTILEGPLkrNTSMTPDARMRRVKDTLQRVGLL------PEHayfypqmLATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:PRK13639 96 VE-EDVAFGPL--NLGLSKEEVEKRVKEALKAVGMEgfenkpPHH-------LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 178 NGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-257 |
1.68e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.42 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYST---RcKLIRMIFQDPntslnprl 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLeslR-RQIGVVPQDT-------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 qigTILEGPLKRNTSM-TPDARMRRVKDTLQRVGL------LPEhAYFYP-----QMLATGQKQRVCLARALILQPSIII 172
Cdd:COG1132 424 ---FLFSGTIRENIRYgRPDATDEEVEEAAKAAQAhefieaLPD-GYDTVvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 173 ADEALNGLDMAMRSQILNLFLELQEEMgVSFVyVSQHIGVIKHiTDKIIVMHEGDVVEAGeTHEVLADpQHPITQRMIES 252
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMKGR-TTIV-IAHRLSTIRN-ADRILVLDDGRIVEQG-THEELLA-RGGLYARLYRL 574
|
....*
gi 447197775 253 HFTKA 257
Cdd:COG1132 575 QFGEE 579
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-247 |
3.03e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK11607 16 LTPLLEIRNLTKSF---------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCklIRMIFQdpNTSLNPRLQIGTILEGPLKRNTsmTPDARMR-RVKDTLQRVGLLpEHAYFYPQMLATGQKQRVC 159
Cdd:PRK11607 87 PPYQRP--INMMFQ--SYALFPHMTVEQNIAFGLKQDK--LPKAEIAsRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 160 LARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLa 239
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY- 238
|
....*...
gi 447197775 240 dpQHPITQ 247
Cdd:PRK11607 239 --EHPTTR 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-229 |
3.24e-29 |
|
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: 108.28 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03216 1 LELRGITKRF---GGV------KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKL-IRMIFQdpntslnprlqigtilegplkrntsmtpdarmrrvkdtlqrvgllpehayfypqmLATGQKQRVCLARA 163
Cdd:cd03216 72 ARRAgIAMVYQ-------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 164 LILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-232 |
3.41e-29 |
|
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: 109.76 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFVtrsgfLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:cd03266 1 MITADALTKRFR-----DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRcklIRMIFQDPNTSLNPRLQIGTILE--GPLKrntSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQKQRVCLA 161
Cdd:cd03266 76 AR---RRLGFVSDSTGLYDRLTARENLEyfAGLY---GLKGDELTARLEELADRLG-MEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 162 RALILQPSIIIADEALNGLDMaMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-232 |
3.56e-29 |
|
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: 109.29 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSgflrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSt 84
Cdd:cd03269 1 LEVENVTKRFGRVT---------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 rckliRMIFQDPNTSLNPRLQIGTILE--GPLKrntSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQKQRVCLAR 162
Cdd:cd03269 71 -----RIGYLPEERGLYPKMKVIDQLVylAQLK---GLKKEEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 163 ALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-241 |
4.58e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.20 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDF---------VTRSGFLRKQIQH------AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP 65
Cdd:PRK10070 1 MAIKLEIKNLYKIFgehpqrafkYIEQGLSKEQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 66 TGGEIRVNG----ELLEHKDYSTRCKLIRMIFQD----PNTSLNPRLQIGTILEGplkrntsMTPDARMRRVKDTLQRVG 137
Cdd:PRK10070 81 TRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSfalmPHMTVLDNTAFGMELAG-------INAEERREKALDALRQVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 138 LlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHIT 217
Cdd:PRK10070 154 L-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIG 232
|
250 260
....*....|....*....|....
gi 447197775 218 DKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK10070 233 DRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-232 |
8.26e-29 |
|
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: 108.73 E-value: 8.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 33 SFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCklIRMIFQDPNtsLNPRLQIGTILEG 112
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENN--LFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 113 PLKRNTSMTPDARmRRVKDTLQRVGLLPEHAYFyPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLF 192
Cdd:cd03298 94 GLSPGLKLTAEDR-QAIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447197775 193 LELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
8.65e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.49 E-value: 8.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR----MIFQDPNTSLNPR 103
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRkkvgIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIGTILEGPLkrNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMA 183
Cdd:PRK13634 102 TVEKDICFGPM--NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 184 MRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-223 |
9.91e-29 |
|
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: 108.39 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDystrcKLIRMIFQdpNTSLNPRLQ 105
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ--RRSIDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IgTILE----------GPLKRNTSmtpdARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADE 175
Cdd:cd03235 85 I-SVRDvvlmglyghkGLFRRLSK----ADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447197775 176 ALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVM 223
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-239 |
1.39e-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: 113.69 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDystRCKLIRMIF---QDPntslnprlq 105
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELGRHIGylpQDV--------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 igTILEGPLKRNTSMTPDARMRRVKDTLQRVGL------LPEHayfY-------PQMLATGQKQRVCLARALILQPSIII 172
Cdd:COG4618 416 --ELFDGTIAENIARFGDADPEKVVAAAKLAGVhemilrLPDG---YdtrigegGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 173 ADEALNGLDmAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:COG4618 491 LDEPNSNLD-DEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
28-241 |
1.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 109.69 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGelLEHKDYSTRC---KLIRMIFQDPNTSLNPRL 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQgirKLVGIVFQNPETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 QIGTILEGPlkRNTSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAM 184
Cdd:PRK13644 95 VEEDLAFGP--ENLCLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 185 RSQILNLFLELQEEmGVSFVYVSQHIGVIkHITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-240 |
1.60e-28 |
|
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: 107.91 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKL-------IRMIFqdpnts 99
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgigyvpeGRRIF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 100 lnPRLqigTILEgplkrNTSMTPDARMR-RVKDTLQRV-GLLPEHAYFYPQMLAT---GQKQRVCLARALILQPSIIIAD 174
Cdd:cd03224 88 --PEL---TVEE-----NLLLGAYARRRaKRKARLERVyELFPRLKERRKQLAGTlsgGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-194 |
1.82e-28 |
|
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: 107.56 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFVTRSGFlrkqiqhavKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDY 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLF---------SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRcklIRMIFQDPNTSLNPRLqigTILEgplkrNTSM-----TPDARMRRVKDTLQRVGLLPeHAYFYPQMLATGQKQR 157
Cdd:COG4133 72 DYR---RRLAYLGHADGLKPEL---TVRE-----NLRFwaalyGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRR 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLE 194
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-232 |
4.81e-28 |
|
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: 106.51 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrsgflRKQiqHAVKPVSFTLEAGQTiGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE-LLEHKDYS 83
Cdd:cd03264 1 LQLENLTKRY-------GKK--RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRckLIRMIFQDPNTSlnPRLQIGTILE--GPLKRNTSMTPDARMRRVkdtLQRVGLLpEHAYFYPQMLATGQKQRVCLA 161
Cdd:cd03264 71 RR--RIGYLPQEFGVY--PNFTVREFLDyiAWLKGIPSKEVKARVDEV---LELVNLG-DRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmgvSFVYVSQHI-GVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED---RIVILSTHIvEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
29-229 |
6.74e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.80 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDystRCKLIRMIFQDPNTslnprlQIGT 108
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQDVDY------QLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ------ILEGplkrntSMTPDARMRRVKDTLQRVGLLPEHAYfYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:cd03226 87 dsvreeLLLG------LKELDAGNEQAETVLKDLDLYALKER-HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447197775 183 AMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:cd03226 160 KNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
29-253 |
9.58e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 106.71 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP----TGGEIRVNGELLEHKdySTRCKLIRMIFQDPNTSLNPRL 104
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC--ALRGRKIATIMQNPRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 QIGTILEGPLKRNTSMTPDARMRRVkdtLQRVGLLPEHAYF--YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAA---LEAVGLENAARVLklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 183 AMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPITQRMIESH 253
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAH 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
32-242 |
1.22e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGElleHKDYSTRC--KLIR-------MIFQDPNtsLNP 102
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKTPsdKAIRelrrnvgMVFQQYN--LWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQ-IGTILEGPLKRnTSMTPDARMRRVKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:PRK11124 96 HLTvQQNLIEAPCRV-LGLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 182 MAMRSQILNLFLELQeEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGeTHEVLADPQ 242
Cdd:PRK11124 174 PEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQ 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-250 |
1.42e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 45 IGQNGSGKSTLARMLAGMV-----APTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSlnPRLQIGTILEGPLKRNTS 119
Cdd:PRK14247 35 MGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 120 MTPDARMR-RVKDTLQRVGLLPE--HAYFYPQ-MLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLEL 195
Cdd:PRK14247 113 VKSKKELQeRVRWALEKAQLWDEvkDRLDAPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 196 QEEMGVsfVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPITQRMI 250
Cdd:PRK14247 193 KKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-226 |
1.51e-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: 104.44 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHkdfvtrsgflrkqIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDY 82
Cdd:cd03215 3 PVLEVRGLS-------------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKL-IRMIFQDpntslnpRLQIGTILEGPLKRNTSMtpdarmrrvkdtlqrvgllpehayfyPQMLATGQKQRVCLA 161
Cdd:cd03215 70 RDAIRAgIAYVPED-------RKREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVLA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03215 117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-242 |
3.31e-27 |
|
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: 105.11 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrSGFLRKQiqhavkpVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELL-----EH 79
Cdd:cd03299 1 LKVENLSKDW---KEFKLKN-------VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlppEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 KDYStrcklirMIFQdpNTSLNPRLQIGTILEGPLKRNTSMTPDaRMRRVKDTLQRVGLlpEHA-YFYPQMLATGQKQRV 158
Cdd:cd03299 71 RDIS-------YVPQ--NYALFPHMTVYKNIAYGLKKRKVDKKE-IERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 159 CLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
....
gi 447197775 239 ADPQ 242
Cdd:cd03299 219 KKPK 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-239 |
3.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.95 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDV------NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIRMIFQDPNTSLnprlqIGTILEGPLK---RNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQR 157
Cdd:PRK13642 75 NVWNLRRKIGMVFQNPDNQF-----VGATVEDDVAfgmENQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEV 237
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
..
gi 447197775 238 LA 239
Cdd:PRK13642 228 FA 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-240 |
7.53e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 7.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:COG4152 2 LELKGLTKRFGDK---------TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 -------RcklirmifqdpntSLNPRLQIGTILE--GPLKrntSMTPDARMRRVKDTLQRVGlLPEHAYFYPQMLATGQK 155
Cdd:COG4152 73 igylpeeR-------------GLYPKMKVGEQLVylARLK---GLSKAEAKRRADEWLERLG-LGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
....*
gi 447197775 236 EVLAD 240
Cdd:COG4152 215 EIRRQ 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-239 |
8.93e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.89 E-value: 8.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 31 PVSFTL--EAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllEHKDYSTRCKLIRMIFQDPN--TSLNPRLQI 106
Cdd:PRK10771 15 PMRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNlfSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 GTILEGPLKRNtsmtpDARMRRVKDTLQRVGLlpeHAYF--YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAM 184
Cdd:PRK10771 93 GLGLNPGLKLN-----AAQREKLHAIARQMGI---EDLLarLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 185 RSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-241 |
1.20e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKdySTRCKLIRMIFQdpNTSLNPRLQIGTILE 111
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR--SIQQRDICMVFQ--SYALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 GPLKRnTSMTPDARMRRVKDTLQRVGLlpehAYF---YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQI 188
Cdd:PRK11432 101 YGLKM-LGVPKEERKQRVKEALELVDL----AGFedrYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447197775 189 LNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-229 |
1.55e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 103.18 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRS--GFLRKQIQH----------AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRV 72
Cdd:cd03267 1 IEVSNLSKSYRVYSkePGLIGSLKSlfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 73 NGELlehkDYSTRCKLIRMI---FQDPNT---SLNPRlqigtilEG-PLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYF 145
Cdd:cd03267 81 AGLV----PWKRRKKFLRRIgvvFGQKTQlwwDLPVI-------DSfYLLAAIYDLPPARFKKRLDELSELLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 146 YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHE 225
Cdd:cd03267 150 PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
....
gi 447197775 226 GDVV 229
Cdd:cd03267 230 GRLL 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-240 |
1.61e-26 |
|
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: 103.63 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 2 SALLEVTNLHkdfVTRSGflrKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPT-GGEIRVNGELLEHK 80
Cdd:COG1119 1 DPLLELRNVT---VRRGG---KTI---LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DystrcklIRMIfqdpntslnpRLQIG---TILEGPLKRNTS----------------MTPDARMR-RVKDTLQRVGL-- 138
Cdd:COG1119 72 D-------VWEL----------RKRIGlvsPALQLRFPRDETvldvvlsgffdsiglyREPTDEQReRARELLELLGLah 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 139 LPEHAYfypQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITD 218
Cdd:COG1119 135 LADRPF---GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGIT 211
|
250 260
....*....|....*....|..
gi 447197775 219 KIIVMHEGDVVEAGETHEVLAD 240
Cdd:COG1119 212 HVLLLKDGRVVAAGPKEEVLTS 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-228 |
1.95e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNL----HKDfvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEL 76
Cdd:PRK13650 1 MSNIIEVKNLtfkyKED----------QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 77 LEHKDYSTRCKLIRMIFQDPNTSLnprlqIGTILEGPLK---RNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATG 153
Cdd:PRK13650 71 LTEENVWDIRHKIGMVFQNPDNQF-----VGATVEDDVAfglENKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 154 QKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKhITDKIIVMHEGDV 228
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-242 |
2.89e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP---TGGEIRVNG-ELLEHKDYSTRCKlIRMIFQDPNTSLnpr 103
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGiTLTAKTVWDIREK-VGIVFQNPDNQF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 lqIGTILE-----GPLKRNTsmtPDARMRR-VKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:PRK13640 98 --VGATVGddvafGLENRAV---PRPEMIKiVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 178 NGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-240 |
4.14e-26 |
|
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: 106.43 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGE--IRVNGELLEHK----DYSTRCK-LIRMIFQDpnTSL 100
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTkpgpDGRGRAKrYIGILHQE--YDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 101 NPRlqiGTILEGPLKRNTSMTPD--ARMRRVKdTLQRVGLLPEHAYF----YPQMLATGQKQRVCLARALILQPSIIIAD 174
Cdd:TIGR03269 377 YPH---RTVLDNLTEAIGLELPDelARMKAVI-TLKMVGFDEEKAEEildkYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-240 |
5.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKdysTRCKLIR-------MIFQDPNTSL 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK---TKDKYIRpvrkrigMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 101 NPRLQIGTILEGPlkRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:PRK13646 99 FEDTVEREIIFGP--KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 181 DMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-241 |
6.21e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.57 E-value: 6.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSLNPRLQI 106
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 GTILEGPLkrNTSMTPDARMRRVKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRS 186
Cdd:PRK13652 98 QDIAFGPI--NLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 187 QILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-254 |
8.39e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 101.65 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMV-----APTGGEIRVNGELLEHKDYST---RCKlIRMIFQDPN- 97
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDIYDPDVDVvelRRR-VGMVFQKPNp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 98 --TSL--N----PRLQigtileGPLKRntsmtpdARMR-RVKDTLQRVGL-------LPEHAYFypqmLATGQKQRVCLA 161
Cdd:COG1117 104 fpKSIydNvaygLRLH------GIKSK-------SELDeIVEESLRKAALwdevkdrLKKSALG----LSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSqhigvikH-------ITDKIIVMHEGDVVEAGET 234
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVT-------HnmqqaarVSDYTAFFYLGELVEFGPT 237
|
250 260
....*....|....*....|
gi 447197775 235 HEVLADPQHPITQRMIESHF 254
Cdd:COG1117 238 EQIFTNPKDKRTEDYITGRF 257
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
28-223 |
1.15e-25 |
|
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: 105.06 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqig 107
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHP----------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRNTSM-TPDARMRRVKDTLQRVGLLPEHAYFyPQMLAT-----------GQKQRVCLARALILQPSIIIADE 175
Cdd:TIGR02857 406 FLFAGTIAENIRLaRPDASDAEIREALERAGLDEFVAAL-PQGLDTpigeggaglsgGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447197775 176 ALNGLDMAMRSQILNLFLELQEemGVSFVYVSqHIGVIKHITDKIIVM 223
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ--GRTVLLVT-HRLALAALADRIVVL 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-239 |
1.37e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 20 FLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehkDYSTRCKL-----IRMIFQ 94
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLalrqqVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 95 DPNTSLNpRLQIGTILEGPLkRNTSMTPDARMRRVKDTLQRVGllPEHAYFYP-QMLATGQKQRVCLARALILQPSIIIA 173
Cdd:PRK13638 85 DPEQQIF-YTDIDSDIAFSL-RNLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 174 DEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-236 |
1.45e-25 |
|
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: 100.14 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrSGFLrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehkdYST 84
Cdd:cd03265 1 IEVENLVKKY---GDFE------AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-------HDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RC------KLIRMIFQDPntSLNPRL------QIGTILEGpLKRntsmtpDARMRRVKDTLQRVGLLpEHAYFYPQMLAT 152
Cdd:cd03265 65 VReprevrRRIGIVFQDL--SVDDELtgwenlYIHARLYG-VPG------AERRERIDELLDFVGLL-EAADRLVKTYSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03265 135 GMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
....
gi 447197775 233 ETHE 236
Cdd:cd03265 215 TPEE 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-239 |
4.23e-25 |
|
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: 99.48 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDpNTSLNprlqiGTILE 111
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQE-NVLFN-----RSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 gplkrNTSMT-PDARMRRVKDTLQRVGL------LPEHayfYPQM-------LATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:cd03252 95 -----NIALAdPGMSMERVIEAAKLAGAhdfiseLPEG---YDTIvgeqgagLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 178 NGLDMAMRSQIlnlflelQEEM-----GVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:cd03252 167 SALDYESEHAI-------MRNMhdicaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-228 |
7.81e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPNtslnprLQIGTILE 111
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDE------LFSGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 gplkrntsmtpdarmrrvkdtlqrvgllpehayfypQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNL 191
Cdd:cd03246 95 ------------------------------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 447197775 192 FLELQEEmGVSFVYVSQHIGVIKhITDKIIVMHEGDV 228
Cdd:cd03246 139 IAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-232 |
1.43e-24 |
|
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: 97.66 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 24 QIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnpr 103
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDV------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 lqigTILEGPLKRNTSM-TPDARMRRVKDTLQRVGL---LPEHAYFYPQM-------LATGQKQRVCLARALILQPSIII 172
Cdd:cd03245 88 ----TLFYGTLRDNITLgAPLADDERILRAAELAGVtdfVNKHPNGLDLQigergrgLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 173 ADEALNGLDMAMRSQilnLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03245 164 LDEPTSAMDMNSEER---LKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
38-228 |
1.59e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 38 AGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRV-NGELLEHKDYstrcklIRMIFQDPntslnpRL--------QIGT 108
Cdd:PRK11247 37 AGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgTAPLAEARED------TRLMFQDA------RLlpwkkvidNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKrntsmtPDARmrrvkDTLQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQI 188
Cdd:PRK11247 105 GLKGQWR------DAAL-----QALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447197775 189 LNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDV 228
Cdd:PRK11247 173 QDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-259 |
2.27e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR----MIFQDPNTSLNPRLQIG 107
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvsLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPlkRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:PRK13641 106 DVEFGP--KNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 188 ILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQhpitqrMIESHFTKAPT 259
Cdd:PRK13641 184 MMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE------WLKKHYLDEPA 248
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-232 |
6.79e-24 |
|
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: 96.06 E-value: 6.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSGF-------------LRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIR 71
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 72 VNGEllehkdystrcklIRMIFqDPNTSLNPRLQ-------IGTILegplkrntSMTPDARMRRVKDTLQRVGLlpEHAY 144
Cdd:cd03220 81 VRGR-------------VSSLL-GLGGGFNPELTgreniylNGRLL--------GLSRKEIDEKIDEIIEFSEL--GDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 145 FYP-QMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQeEMGVSFVYVSQHIGVIKHITDKIIVM 223
Cdd:cd03220 137 DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVL 215
|
....*....
gi 447197775 224 HEGDVVEAG 232
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
30-239 |
9.86e-24 |
|
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: 95.76 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 30 KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDpnTSL-NprlqiGT 108
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD--TVLfN-----DT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKRNTSMTPD-----ARMRRVKDTLQRvglLPEHayfYPQ-------MLATGQKQRVCLARALILQPSIIIADEA 176
Cdd:cd03253 91 IGYNIRYGRPDATDEevieaAKAAQIHDKIMR---FPDG---YDTivgerglKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 177 LNGLDMAMRSQILNLFLELQEemGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-232 |
1.06e-23 |
|
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: 95.25 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqig 107
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDP----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRN---TSMTPDARMRRVkdtLQRVGLLPEHAYFYPQM----------LATGQKQRVCLARALILQPSIIIAD 174
Cdd:cd03244 88 VLFSGTIRSNldpFGEYSDEELWQA---LERVGLKEFVESLPGGLdtvveeggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 175 EALNGLDMAMRSQILNLfleLQEEM-GVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAG 232
Cdd:cd03244 165 EATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-239 |
2.31e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.31 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 6 EVTNLHKDFVTR---SGFL---------RKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVN 73
Cdd:COG4586 3 EVENLSKTYRVYekePGLKgalkglfrrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 74 GE--LLEHKDYSTRC--------------------KLIRMIFQDPNTSLNPR-------LQIGTILEGPLkRNTSMtpda 124
Cdd:COG4586 83 GYvpFKRRKEFARRIgvvfgqrsqlwwdlpaidsfRLLKAIYRIPDAEYKKRldelvelLDLGELLDTPV-RQLSL---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 125 rmrrvkdtlqrvgllpehayfypqmlatGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFV 204
Cdd:COG4586 158 ----------------------------GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTIL 209
|
250 260 270
....*....|....*....|....*....|....*
gi 447197775 205 YVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:COG4586 210 LTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
28-209 |
4.53e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 93.63 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR---MIFQDpnTSLNPRL 104
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRkigVVFQD--FRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 QIGTILEGPLkRNTSMTPDARMRRVKDTLQRVGLLPEHAYfYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAM 184
Cdd:cd03292 94 NVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180
....*....|....*....|....*
gi 447197775 185 RSQILNLFLELQeEMGVSFVyVSQH 209
Cdd:cd03292 172 TWEIMNLLKKIN-KAGTTVV-VATH 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-241 |
5.03e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSalLEVTNLHKDFVtrsgflRKQIQHavkPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehK 80
Cdd:PRK10851 1 MS--IEIANIKKSFG------RTQVLN---DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG-----T 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYS---TRCKLIRMIFQdpNTSLNPRLqigTILEG------PLKRNTSMTPDARMRRVKDTLQRVGLlpEH-AYFYPQML 150
Cdd:PRK10851 65 DVSrlhARDRKVGFVFQ--HYALFRHM---TVFDNiafgltVLPRRERPNAAAIKAKVTQLLEMVQL--AHlADRYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVE 230
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
250
....*....|.
gi 447197775 231 AGETHEVLADP 241
Cdd:PRK10851 218 AGTPDQVWREP 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-250 |
5.74e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR------MIFQDPNTSlnP 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKlrkevgMVFQQPNPF--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEhayFYPQM------LATGQKQRVCLARALILQPSIIIADEA 176
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE---VYDRLnspasqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 177 LNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPITQRMI 250
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
8.23e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.78 E-value: 8.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 2 SALLEVTNLHKDFVTrsgflrKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELL---- 77
Cdd:PRK09452 12 SPLVELRGISKSFDG------KEV---ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 78 -EHKDYSTrcklirmIFQdpNTSLNPRLqigTILEgplkrNTSM------TPDARMR-RVKDTLQRVGLlPEHAYFYPQM 149
Cdd:PRK09452 83 aENRHVNT-------VFQ--SYALFPHM---TVFE-----NVAFglrmqkTPAAEITpRVMEALRMVQL-EEFAQRKPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSqhigvikH-------ITDKIIV 222
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVT-------HdqeealtMSDRIVV 217
|
250
....*....|....*....
gi 447197775 223 MHEGDVVEAGETHEVLADP 241
Cdd:PRK09452 218 MRDGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-242 |
9.67e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.03 E-value: 9.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHkdfvtrsgFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNG-ELLEH 79
Cdd:PRK13647 1 MDNIIEVEDLH--------FRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrEVNAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 KDYSTRCKlIRMIFQDPNTSLNPrlqiGTILE----GPlkRNTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQK 155
Cdd:PRK13647 73 NEKWVRSK-VGLVFQDPDDQVFS----STVWDdvafGP--VNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETh 235
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK- 222
|
....*..
gi 447197775 236 EVLADPQ 242
Cdd:PRK13647 223 SLLTDED 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-226 |
1.47e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE---LLEHKDYSTRCKLIRMIFQDPNTSLNP 102
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditRLKNREVPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIGTILegPLKRNTSMTPDARmRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:PRK10908 95 TVYDNVAI--PLIIAGASGDDIR-RRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447197775 183 AMRSQILNLFLELQeEMGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:PRK10908 171 ALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-238 |
1.58e-22 |
|
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: 92.68 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGelLEHKDYSTRC--KLIRMIFQDPntslnpRLQ 105
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYTLASlrRQIGLVSQDV------FLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IGTILEgplkrNTSM-TPDARMRRVKDTLQRVGL------LPEHayfYPQM-------LATGQKQRVCLARALILQPSII 171
Cdd:cd03251 89 NDTVAE-----NIAYgRPGATREEVEEAARAANAhefimeLPEG---YDTVigergvkLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 172 IADEALNGLDMAMRSQILNLFLELQEEMgVSFVyVSQHIGVIKHItDKIIVMHEGDVVEAGeTHEVL 238
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNR-TTFV-IAHRLSTIENA-DRIVVLEDGKIVERG-THEEL 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-232 |
3.64e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.06 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 24 QIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLeHKDYSTRCKLIRMIFQDP---NTSL 100
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISVLNQRPylfDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 101 npRLQIGTILEGplkrntsmtpdarmrrvkdtlqrvgllpehayfypqmlatGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:cd03247 92 --RNNLGRRFSG----------------------------------------GERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447197775 181 DMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHItDKIIVMHEGDVVEAG 232
Cdd:cd03247 130 DPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-240 |
4.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGM-VAPTG----GEIRVNGELLEHKDYSTRCKLIRMIFQDPNTSLNP 102
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGqtivGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIGTILEGPLkrNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:PRK13645 106 ETIEKDIAFGPV--NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 183 AMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-241 |
4.46e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRC----------------KLIRM 91
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfkelrRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 92 IFQDPNTSLNPRLQIGTILEGPLKRNTSMTpDARmRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSII 171
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVALGVKKS-EAK-KLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 172 IADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKhITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLE-VADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
28-250 |
6.66e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.46 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNgelLEHKDYSTRCKLIRMIFQDPNTSLNP----- 102
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI---FKDEKNKKKTKEKEKVLEKLVIQKTRfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 -----RLQIG-------------TILE----GPlkRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCL 160
Cdd:PRK13651 99 kikeiRRRVGvvfqfaeyqlfeqTIEKdiifGP--VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
250
....*....|
gi 447197775 241 PQHPITQRMI 250
Cdd:PRK13651 256 NKFLIENNME 265
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-229 |
7.57e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDfvtrsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:COG1129 256 VLEVEGLSVG-------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCKL-IRMIFQDpntslnpRLQIGTILEGPLKRNTSMTPDARMRR------------VKDTLQRVGLLPEHAYFYPQML 150
Cdd:COG1129 323 DAIRAgIAYVPED-------RKGEGLVLDLSIRENITLASLDRLSRgglldrrreralAEEYIKRLRIKTPSPEQPVGNL 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-240 |
7.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR----MIFQDPNTSLNPRLQIG 107
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkvgLVFQFPESQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPlkRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:PRK13649 106 DVAFGP--QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447197775 188 ILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13649 184 LMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-221 |
9.01e-22 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 89.98 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 7 VTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRC 86
Cdd:TIGR03608 1 LKNISKKFGDK---------VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 87 KLIR----MIFQD----PNTSLNPRLQIGTILEgplKRNTSmtpdARMRRVKDTLQRVGL-LPEHAYFYPqmLATGQKQR 157
Cdd:TIGR03608 72 KFRReklgYLFQNfaliENETVEENLDLGLKYK---KLSKK----EKREKKKEALEKVGLnLKLKQKIYE--LSGGEQQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSqHIGVIKHITDKII 221
Cdd:TIGR03608 143 VALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVT-HDPEVAKQADRVI 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-241 |
2.26e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 30 KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnpRLQIGTI 109
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEP------VLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 110 LEGPLKRNTSmTPDARMRRVKDTLQRVGLLPEHAYFYP-------QMLATGQKQRVCLARALILQPSIIIADEALNGLDm 182
Cdd:TIGR00958 572 RENIAYGLTD-TPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 183 amrSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-203 |
2.27e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.92 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 22 RKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDySTRCklirMIFQDpnTSLN 101
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-ADRG----VVFQK--DALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 102 PRLQIGTILEGPLKRNtSMTPDARMRRVKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:COG4525 89 PWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180
....*....|....*....|..
gi 447197775 182 MAMRSQILNLFLELQEEMGVSF 203
Cdd:COG4525 167 ALTREQMQELLLDVWQRTGKGV 188
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-241 |
2.52e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.66 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSA-LLEVTNLHKDFvtrSGFLrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLE- 78
Cdd:PRK11300 1 MSQpLLSVSGLMMRF---GGLL------AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 79 ---HKdySTRCKLIRMiFQdpntslNPRL----------------QIGT-ILEGPLKrntsmTPDAR------MRRVKDT 132
Cdd:PRK11300 72 lpgHQ--IARMGVVRT-FQ------HVRLfremtvienllvaqhqQLKTgLFSGLLK-----TPAFRraeseaLDRAATW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 133 LQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGV 212
Cdd:PRK11300 138 LERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
250 260
....*....|....*....|....*....
gi 447197775 213 IKHITDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK11300 217 VMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-229 |
2.61e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.86 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNlhkdfVTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK10535 1 MTALLELKD-----IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKLIR----MIFQD----PNTSLNPRLQIGTILEGPLKRntsmtpdARMRRVKDTLQRVGLlPEHAYFYPQMLAT 152
Cdd:PRK10535 76 DADALAQLRRehfgFIFQRyhllSHLTAAQNVEVPAVYAGLERK-------QRLLRAQELLQRLGL-EDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSqHIGVIKHITDKIIVMHEGDVV 229
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVT-HDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
28-254 |
2.64e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGM--VAP---TGGEIRVNGelleHKDYSTRC------KLIRMIFQDP 96
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNG----HNIYSPRTdtvdlrKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 97 N---TSLNPRLQIGTILEGPLKR-------NTSMTPDARMRRVKDTLQRVGLlpehayfypqMLATGQKQRVCLARALIL 166
Cdd:PRK14239 96 NpfpMSIYENVVYGLRLKGIKDKqvldeavEKSLKGASIWDEVKDRLHDSAL----------GLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 167 QPSIIIADEALNGLDMAMRSQILNLFLELQEEMgvSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPIT 246
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
....*...
gi 447197775 247 QRMIESHF 254
Cdd:PRK14239 244 EDYISGKF 251
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-242 |
3.18e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 30 KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCklIRMIFQD----PNTSLNPRLQ 105
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQSyalyPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IGTILEGPLKRNTsmtpDARMRRVKDTLQRVGLLPEHayfyPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMR 185
Cdd:PRK11000 98 FGLKLAGAKKEEI----NQRVNQVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 186 SQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK11000 170 VQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-207 |
8.87e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.95 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 2 SALLEVTNLHKDFvtRSGFLRKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKD 81
Cdd:PRK11629 3 KILLQCDNLCKRY--QEGSVQTDV---LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKL----IRMIFQdpntsLNPRLQIGTILEgplkrNTSM-------TPDARMRRVKDTLQRVGLlPEHAYFYPQML 150
Cdd:PRK11629 78 SAAKAELrnqkLGFIYQ-----FHHLLPDFTALE-----NVAMplligkkKPAEINSRALEMLAAVGL-EHRANHRPSEL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVS 207
Cdd:PRK11629 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVT 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-250 |
8.87e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.36 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMV-----APTGGEIRVNGELLEHKDYS---TRcKLIRMIFQDPNT 98
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDpieVR-REVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 99 SlnPRLQIGTILEGPLKRNTSMTPDARM-RRVKDTLQRVGLLPE---HAYFYPQMLATGQKQRVCLARALILQPSIIIAD 174
Cdd:PRK14267 97 F--PHLTIYDNVAIGVKLNGLVKSKKELdERVEWALKKAALWDEvkdRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEEMgvSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPITQRMI 250
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-228 |
2.63e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 86.37 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqigT 108
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEP-----------V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKRNTSM-TPDARMRRVKDTLQRVG---LLPEHAYFYPQ-------MLATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:cd03248 99 LFARSLQDNIAYgLQSCSFECVKEAAQKAHahsFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447197775 178 NGLDMAMRSQILNLFLELQEEMGVSFvyVSQHIGVIKHiTDKIIVMHEGDV 228
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERRTVLV--IAHRLSTVER-ADQILVLDGGRI 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-237 |
3.02e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:COG3845 2 MPPALELRGITKRF---GGV------VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 dySTRCKL---IRMIFQDPntSLNPRLqigTILE------GPLKRNTSMTPDARmRRVKDTLQRVGL-LPEHAyfYPQML 150
Cdd:COG3845 73 --SPRDAIalgIGMVHQHF--MLVPNL---TVAEnivlglEPTKGGRLDRKAAR-ARIRELSERYGLdVDPDA--KVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDmamRSQILNLFLELQE--EMGVSFVYVSQHIGVIKHITDKIIVMHEGDV 228
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLT---PQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
....*....
gi 447197775 229 VEAGETHEV 237
Cdd:COG3845 220 VGTVDTAET 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-236 |
4.01e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK15439 8 APPLLCARSISKQY---SGV------EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKL-IRMIFQDPNtsLNPRLqigTILEGPLKRNTSmtPDARMRRVKDTLQRVGllpehAYFYPQMLA----TGQK 155
Cdd:PRK15439 79 TPAKAHQLgIYLVPQEPL--LFPNL---SVKENILFGLPK--RQASMQKMKQLLAALG-----CQLDLDSSAgsleVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 156 QRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETH 235
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
.
gi 447197775 236 E 236
Cdd:PRK15439 226 D 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-213 |
4.18e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELlehkdystrckliRMIFQDPNTSLNPRLQIg 107
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-------------RVAYVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILE----------GPLKRntsMTPDARmRRVKDTLQRVGLlpehAYFYPQMLAT---GQKQRVCLARALILQPSIIIAD 174
Cdd:NF040873 73 TVRDlvamgrwarrGLWRR---LTRDDR-AAVDDALERVGL----ADLAGRQLGElsgGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVI 213
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-241 |
4.48e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHkdfVTRSGflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:PRK09536 4 IDVSDLS---VEFGD------TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKLIRMIFQDpnTSLNPRLQIGTILE---GP-LKRNTSMTPDARmRRVKDTLQRVGLlpehAYFYPQ---MLATGQKQR 157
Cdd:PRK09536 75 ASRRVASVPQD--TSLSFEFDVRQVVEmgrTPhRSRFDTWTETDR-AAVERAMERTGV----AQFADRpvtSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 158 VCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEV 237
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
....
gi 447197775 238 LADP 241
Cdd:PRK09536 227 LTAD 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-238 |
7.53e-20 |
|
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: 85.28 E-value: 7.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 30 KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYSTRC--KLIRMIFQDPNtslnprLQIG 107
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWlrSQIGLVSQEPV------LFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPL--KRNTSMTPDARMRRVKDTLQRVGLLPE----HAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:cd03249 92 TIAENIRygKPDATDEEVEEAAKKANIHDFIMSLPDgydtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 182 MAMRSQI---LNLFLElqeemGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGeTHEVL 238
Cdd:cd03249 172 AESEKLVqeaLDRAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG-THDEL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-229 |
1.03e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSGFLRkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE----LLEHK 80
Cdd:COG1101 2 LELKNLSKTFNPGTVNEK----RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtkLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 dystRCKLIRMIFQDP--NTSlnPRLqigTILEgplkrNTSMtpdARMRRVKDTLQRvGLLPEHAYFYPQMLAT------ 152
Cdd:COG1101 78 ----RAKYIGRVFQDPmmGTA--PSM---TIEE-----NLAL---AYRRGKRRGLRR-GLTKKRRELFRELLATlglgle 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 153 ------------GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmgvsfvyvsqhigviKHIT--- 217
Cdd:COG1101 140 nrldtkvgllsgGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEE---------------NNLTtlm 204
|
250 260
....*....|....*....|....
gi 447197775 218 ------------DKIIVMHEGDVV 229
Cdd:COG1101 205 vthnmeqaldygNRLIMMHEGRII 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-240 |
1.26e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR----MIFQDPNTSLNPR 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIGTILEGPlkRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMA 183
Cdd:PRK13643 101 TVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 184 MRSQILNLFlELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13643 179 ARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-241 |
1.68e-19 |
|
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: 84.13 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRsgflrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYST 84
Cdd:cd03218 1 LRAENLSKRYGKR---------KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 85 RCKL-IRMIFQDPNT--SLNPRLQIGTILEGplkrnTSMTPDARMRRVKDTLQRVGLlpEH-----AYFypqmLATGQKQ 156
Cdd:cd03218 72 RARLgIGYLPQEASIfrKLTVEENILAVLEI-----RGLSKKEREEKLEELLEEFHI--THlrkskASS----LSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEemgvsfvyvsQHIGVI--KH-------ITDKIIVMHEGD 227
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD----------RGIGVLitDHnvretlsITDRAYIIYEGK 210
|
250
....*....|....
gi 447197775 228 VVEAGETHEVLADP 241
Cdd:cd03218 211 VLAEGTPEEIAANE 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-238 |
1.74e-19 |
|
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: 87.57 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 30 KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllehkDystrcklIRMIFQDpntSLnpRLQIG-- 107
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ-----D-------IRDVTQA---SL--RAAIGiv 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 ---TILegplkRNTSM-------TPDARMRRVKDTLQRVGL------LPEHayfYPQM-------LATGQKQRVCLARAL 164
Cdd:COG5265 438 pqdTVL-----FNDTIayniaygRPDASEEEVEAAARAAQIhdfiesLPDG---YDTRvgerglkLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 165 ILQPSIIIADEALNGLDMAMRSQILNlflELQEemgvsfvyVSQH---IgVIKH----IT--DKIIVMHEGDVVEAGeTH 235
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQA---ALRE--------VARGrttL-VIAHrlstIVdaDEILVLEAGRIVERG-TH 576
|
...
gi 447197775 236 EVL 238
Cdd:COG5265 577 AEL 579
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
26-209 |
2.49e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 87.03 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPN---TSLNP 102
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHlfdTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIGtilegplkrntsmTPDARMRRVKDTLQRVGL------LP--------EHAyfypQMLATGQKQRVCLARALILQP 168
Cdd:TIGR02868 428 NLRLA-------------RPDATDEELWAALERVGLadwlraLPdgldtvlgEGG----ARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447197775 169 SIIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQH 209
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-232 |
3.93e-19 |
|
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: 82.85 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqig 107
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDP----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRNT---SMTPDARMR---RVKDTlqrvGLlpehayfypqMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:cd03369 92 TLFSGTIRSNLdpfDEYSDEEIYgalRVSEG----GL----------NLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447197775 182 MAMRSQILNLfleLQEEM-GVSFVYVSQHIGVIKHItDKIIVMHEGDVVEAG 232
Cdd:cd03369 158 YATDALIQKT---IREEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-230 |
3.96e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.28 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEL---LEHKDystrcKLIRMIFQdpNTSLNPRL 104
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvneLEPAD-----RDIAMVFQ--NYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 QIGTILEGPLKrNTSMTPDARMRRVKDTLQRVGLLPehayfY----PQMLATGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:PRK11650 92 SVRENMAYGLK-IRGMPKAEIEERVAEAARILELEP-----LldrkPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 181 D----MAMRSQIlnlfLELQEEMGVSFVYVSqhigvikH-------ITDKIIVMHEGdVVE 230
Cdd:PRK11650 166 DaklrVQMRLEI----QRLHRRLKTTSLYVT-------HdqveamtLADRVVVMNGG-VAE 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-247 |
8.60e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGE----LLEHKDYSTRcKLIRMIFQdpNTSLNPRLQIG 107
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipaMSRSRLYTVR-KRMSMLFQ--SGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEhAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:PRK11831 103 DNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 188 ILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPITQ 247
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQ 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-207 |
9.15e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 9.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKL----IRMIFQD----PNTSLNPR 103
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSfmliPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIGTILEGPLKRNTSmtpdarmRRVKDTLQRVGlLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMA 183
Cdd:PRK10584 109 VELPALLRGESSRQSR-------NGAKALLEQLG-LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....
gi 447197775 184 MRSQILNLFLELQEEMGVSFVYVS 207
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVT 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-240 |
1.10e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKL-IRMIFQDPNT----SLN 101
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVidelTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 102 PRLQIGTIlegPLKR--NTSMTPDARMR-RVKDTLQRVGLLPEHAYFYPQmLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:PRK09700 99 ENLYIGRH---LTKKvcGVNIIDWREMRvRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 179 GLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-240 |
1.35e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHkdfVTRSGflrKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEhkDY 82
Cdd:PRK13548 1 AMLEARNLS---VRLGG---RTL---LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA--DW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRcKLIR---MIFQdpNTSLNPRLQIGTILE-GPLKRNTSMTPDARMrrVKDTLQRVGLLPEHAYFYPQmLATGQKQRV 158
Cdd:PRK13548 70 SPA-ELARrraVLPQ--HSSLSFPFTVEEVVAmGRAPHGLSRAEDDAL--VAAALAQVDLAHLAGRDYPQ-LSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 159 CLARALI------LQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
....*...
gi 447197775 233 ETHEVLAD 240
Cdd:PRK13548 224 TPAEVLTP 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-239 |
1.82e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.47 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGM--VAPTGGEIRVNGELLEHKDY 82
Cdd:TIGR03269 1 IEVKNLTKKF---DGK------EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 -------STRC-------KLIRMIFQDPNTSLNPRL--QIG-------------TILEGPLK--RNTSMTPDARMRRVKD 131
Cdd:TIGR03269 72 verpskvGEPCpvcggtlEPEEVDFWNLSDKLRRRIrkRIAimlqrtfalygddTVLDNVLEalEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 132 TLQRVGLlpEHAYFY-PQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHI 210
Cdd:TIGR03269 152 LIEMVQL--SHRITHiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 447197775 211 GVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-241 |
2.10e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.70 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHkdfVTRSGflrKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEhkDYS 83
Cdd:COG4559 1 MLEAENLS---VRLGG---RTL---LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA--AWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRcKLIRM---IFQdpNTSLN---PRLQIgtILEGPLKRNTSMTPDARmrRVKDTLQRVGLLPEHAYFYPQmLATGQKQR 157
Cdd:COG4559 70 PW-ELARRravLPQ--HSSLAfpfTVEEV--VALGRAPHGSSAAQDRQ--IVREALALVGLAHLAGRSYQT-LSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 158 VCLARALI-------LQPSIIIADEALNGLDMAMRSQILNLfleLQEemgvsfvYVSQHIGVI---------KHITDKII 221
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRL---ARQ-------LARRGGGVVavlhdlnlaAQYADRIL 211
|
250 260
....*....|....*....|
gi 447197775 222 VMHEGDVVEAGETHEVLADP 241
Cdd:COG4559 212 LLHQGRLVAQGTPEEVLTDE 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-241 |
2.17e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMvAPTGGEIRVNG--ELLEHKDYSTRCKLIR------MIFQDPN 97
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrvEFFNQNIYERRVNLNRlrrqvsMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 98 ----------------TSLNPRLQIGTILEGPLKrntsmtpDARM-RRVKDTLQRVGLlpehayfypqMLATGQKQRVCL 160
Cdd:PRK14258 99 lfpmsvydnvaygvkiVGWRPKLEIDDIVESALK-------DADLwDEIKHKIHKSAL----------DLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHE-----GDVVEAGETH 235
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
....*.
gi 447197775 236 EVLADP 241
Cdd:PRK14258 242 KIFNSP 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-230 |
4.23e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKdfvtrsGFLRKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVnGELLEHKDYS 83
Cdd:COG0488 315 VLELEGLSK------SYGDKTL---LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 trcklirmifQDpNTSLNPRLqigTILEGpLKRntsMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARA 163
Cdd:COG0488 385 ----------QH-QEELDPDK---TVLDE-LRD---GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 164 LILQPSIIIADEALNGLDMAMRsQILNLFLElqeemgvSF----VYVSqhigvikH-------ITDKIIVMHEGDVVE 230
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETL-EALEEALD-------DFpgtvLLVS-------HdryfldrVATRILEFEDGGVRE 509
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-232 |
5.55e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHkdfVTRSGflrKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAG--MVAPTGGEIRVNGELLEHKDY 82
Cdd:COG0396 1 LEIKNLH---VSVEG---KEI---LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKL-IRMIFQDP------------NTSLNPRlqigtilegplkRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYpqm 149
Cdd:COG0396 72 DERARAgIFLAFQYPveipgvsvsnflRTALNAR------------RGEELSAREFLKLLKEKMKELGLDEDFLDRY--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LAT----GQKQRVCLARALILQPSIIIADEALNGLDM-AMR--SQILNlflELQEEmGVSFVYVSQHIGVIKHIT-DKII 221
Cdd:COG0396 137 VNEgfsgGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRivAEGVN---KLRSP-DRGILIITHYQRILDYIKpDFVH 212
|
250
....*....|.
gi 447197775 222 VMHEGDVVEAG 232
Cdd:COG0396 213 VLVDGRIVKSG 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
42-239 |
7.62e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.46 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 42 IGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqigTILEGPLKRNTSMT 121
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDP-----------VVLADTFLANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 122 PDARMRRVKDTLQRVGL------LPE--HAYFYPQ--MLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNL 191
Cdd:PRK10790 439 RDISEEQVWQALETVQLaelarsLPDglYTPLGEQgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447197775 192 FLELQEEmgVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK10790 519 LAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA 563
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
30-226 |
8.11e-18 |
|
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: 77.49 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 30 KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVngellehkdystrcklirmifqdpntslNPRLQIGti 109
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------------------------GSTVKIG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 110 legplkrntsmtpdarmrrvkdtlqrvgllpehayFYPQmLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQIL 189
Cdd:cd03221 67 -----------------------------------YFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 447197775 190 NLFLELQeemGvSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03221 111 EALKEYP---G-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-194 |
9.17e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIrmifqDPNTSLNPRLQIGTILE 111
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYL-----GHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 gpLKRNTSMTPDarmRRVKDTLQRVGLLP-EHAYFypQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILN 190
Cdd:PRK13539 96 --FWAAFLGGEE---LDIAAALEAVGLAPlAHLPF--GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
....
gi 447197775 191 LFLE 194
Cdd:PRK13539 169 LIRA 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-240 |
9.65e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 81.98 E-value: 9.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 33 SFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGE--------IRVNGELLEhkdystrcKLIRMIFQDPNTS-LNP- 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQ--------KLVSDEWQRNNTDmLSPg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 -----RLQIGTILEGpLKRNTSMTPDARMRRVKDTLQRvgllpehAYFYpqmLATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:PRK10938 95 eddtgRTTAEIIQDE-VKDPARCEQLAQQFGITALLDR-------RFKY---LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 178 NGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-226 |
1.29e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrsGFLRkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGmVAPTG---GEIRVNGELL 77
Cdd:PRK13549 2 MEYLLEMKNITKTF----GGVK-----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 78 EHKDYS-TRCKLIRMIFQDpnTSLNPRLqigTILEG-----PLKRNTSMTPDARMRRVKDTLQRVGLLPEHAyfYPQM-L 150
Cdd:PRK13549 72 QASNIRdTERAGIAIIHQE--LALVKEL---SVLENiflgnEITPGGIMDYDAMYLRAQKLLAQLKLDINPA--TPVGnL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 151 ATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-239 |
2.05e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllehkDYS--TRCKLIRMI---FQDP---NTS 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT-----DIRtvTRASLRRNIavvFQDAglfNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 100 LNPRLQIGtilegplKRNTSmtpDARMRRVKDTLQRVGLLPEHAYFYP-------QMLATGQKQRVCLARALILQPSIII 172
Cdd:PRK13657 425 IEDNIRVG-------RPDAT---DEEMRAAAERAQAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 173 ADEALNGLDMAMRSQiLNLFLELQEEMGVSFVyVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK13657 495 LDEATSALDVETEAK-VKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-252 |
2.91e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 81.36 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllEHKDYSTR--CKLIRMIFQDPntslnprlqigTI 109
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR--EIGAYGLRelRRQFSMIPQDP-----------VL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 110 LEGPLKRNTSMTPDARMRRVKDTLQRVGL--------------LPEHAYFYpqmlATGQKQRVCLARALILQPS-IIIAD 174
Cdd:PTZ00243 1396 FDGTVRQNVDPFLEASSAEVWAALELVGLrervasesegidsrVLEGGSNY----SVGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 175 EALNGLDMAMRSQILNLFlelqeeMGVSFVYVSQHIGVIKHIT---DKIIVMHEGDVVEAGETHEVLADPQhPITQRMIE 251
Cdd:PTZ00243 1472 EATANIDPALDRQIQATV------MSAFSAYTVITIAHRLHTVaqyDKIIVMDHGAVAEMGSPRELVMNRQ-SIFHSMVE 1544
|
.
gi 447197775 252 S 252
Cdd:PTZ00243 1545 A 1545
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-184 |
3.03e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELlehkdystrckliRMIF--QDPN------------ 97
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------------RIGYlpQEPPldddltvldtvl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 98 TSLNPRLQIGTILEGPLKRNTSMTPD--------ARM---------RRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCL 160
Cdd:COG0488 84 DGDAELRALEAELEELEAKLAEPDEDlerlaelqEEFealggweaeARAEEILSGLGFPEEDLDRPVSELSGGWRRRVAL 163
|
170 180
....*....|....*....|....
gi 447197775 161 ARALILQPSIIIADEALNGLDMAM 184
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLES 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-226 |
3.98e-17 |
|
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: 80.25 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDF--VTrsgflrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGmVAPTG---GEIRVNGELLE 78
Cdd:TIGR02633 1 LLEMKGIVKTFggVK-----------ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 79 HKDYS-TRCKLIRMIFQD----PNTSLNPRLQIGTILEGPLKRntsMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATG 153
Cdd:TIGR02633 69 ASNIRdTERAGIVIIHQEltlvPELSVAENIFLGNEITLPGGR---MAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 154 QKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-241 |
4.42e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.27 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMvAPTGGEIRVNG-EL--LEHKDYStrcKLIRMIFQdpntslNPRLQ 105
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGiELreLDPESWR---KHLSWVGQ------NPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IGTILEgplkrNTSM-TPDARMRRVKDTLQRVGLLpEHAYFYPQMLAT-----------GQKQRVCLARALILQPSIIIA 173
Cdd:PRK11174 436 HGTLRD-----NVLLgNPDASDEQLQQALENAWVS-EFLPLLPQGLDTpigdqaaglsvGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 174 DEALNGLDMAMRSQILNlflELQEEM-GVSFVYVSQHIGVIKHItDKIIVMHEGDVVEAGETHEVLADP 241
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQ---ALNAASrRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-240 |
4.60e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 24 QIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYStRCKLIRMIfqdpnTSLNPR 103
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI--ADYS-EAALRQAI-----SVVSQR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQigtILEGPLKRNTSM-TPDARMRRVKDTLQRVGL--LPEHayfyPQMLAT-----------GQKQRVCLARALILQPS 169
Cdd:PRK11160 423 VH---LFSATLRDNLLLaAPNASDEALIEVLQQVGLekLLED----DKGLNAwlgeggrqlsgGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 170 IIIADEALNGLDMAMRSQILNLFLELQEemGVSFVYVSQHIGVIKHItDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-200 |
5.61e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDyS 83
Cdd:PRK11248 1 MLQISHLYADY---------GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCklirMIFQD----PNTSLNPRLQIGTILEGplkrntsMTPDARMRRVKDTLQRVGLLPEHAYFYPQmLATGQKQRVC 159
Cdd:PRK11248 71 ERG----VVFQNegllPWRNVQDNVAFGLQLAG-------VEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447197775 160 LARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMG 200
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETG 179
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-250 |
6.75e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 19 GFLRKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGeIRVNGELL-------EHKDYSTRCKLIRM 91
Cdd:PRK14271 30 GFAGKTV---LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrsifNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 92 IFQDPNTSlnPRLQIGTILEGplKRNTSMTPDARMRRVKDT-LQRVGL---LPEHAYFYPQMLATGQKQRVCLARALILQ 167
Cdd:PRK14271 106 LFQRPNPF--PMSIMDNVLAG--VRAHKLVPRKEFRGVAQArLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 168 PSIIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQHPITQ 247
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
...
gi 447197775 248 RMI 250
Cdd:PRK14271 260 RYV 262
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-232 |
6.90e-17 |
|
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: 76.44 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHKDFVTRSGFLRKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAG--MVAPTGGEIRVNGELLEHKDY 82
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQL---LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 StrcKLIRMIFQDpnTSLNPRLQigtilegplkrntsmtpdarmrrVKDTLQRVGLLpehayfypQMLATGQKQRVCLAR 162
Cdd:cd03213 81 R---KIIGYVPQD--DILHPTLT-----------------------VRETLMFAAKL--------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 163 ALILQPSIIIADEALNGLDMAMRSQILNLFLELQeEMGVSfVYVSQH--IGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRT-IICSIHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-232 |
1.25e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.64 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 5 LEVTNLHkdfVTRSGflrKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGM--VAPTGGEIRVNGELLEHKDY 82
Cdd:cd03217 1 LEIKDLH---VSVGG---KEI---LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKL-IRMIFQDPntslnprlqigtilegplkrntsmtPDARMRRVKDTLQRVGllpehayfypQMLATGQKQRVCLA 161
Cdd:cd03217 72 EERARLgIFLAFQYP-------------------------PEIPGVKNADFLRYVN----------EGFSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHI-TDKIIVMHEGDVVEAG 232
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-240 |
1.37e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllEHKDYSTRCKLIRMIFQDPNTslnpRLQIGTILE 111
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK--EINALSTAQRLARGLVYLPED----RQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 GPLKRNTSMTPDARM----RRVKD--TLQR----VGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:PRK15439 356 APLAWNVCALTHNRRgfwiKPAREnaVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 182 MAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD 493
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-192 |
1.70e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.61 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDpntslnprlQIGTILE 111
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP---------GIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 gPLKRNTSMTPDARMRRVKDTLQRVGLLP-EHAYFypQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILN 190
Cdd:cd03231 90 -VLENLRFWHADHSDEQVEEALARVGLNGfEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
..
gi 447197775 191 LF 192
Cdd:cd03231 167 AM 168
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
46-242 |
1.77e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 46 GQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYSTRCKL------IRMIFQD----PNTSLNPRLQIGtilegplk 115
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKGICLppekrrIGYVFQDarlfPHYKVRGNLRYG-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 116 rntsMTPDarMRRVKDTLqrVGLLP-EHAY-FYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNlFL 193
Cdd:PRK11144 101 ----MAKS--MVAQFDKI--VALLGiEPLLdRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP-YL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447197775 194 E-LQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLADPQ 242
Cdd:PRK11144 172 ErLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-234 |
1.84e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHkdySTRCKLIRMIFQDPNTSLN-PRLQI 106
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQSEEVDWSfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 GTILEGplkRNTSM----TPDARMR-RVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:PRK15056 99 DVVMMG---RYGHMgwlrRAKKRDRqIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447197775 182 MAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDkIIVMHEGDVVEAGET 234
Cdd:PRK15056 175 VKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPT 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-238 |
1.90e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.12 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 31 PVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVaPTGGEIRVNGELLEhkDYSTrCKLIRM----IFQDPNTSLNPRLQI 106
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLE--AWSA-AELARHraylSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 GTiLEGPLKRNTSMTPDArMRRVKDTLQRVGLLPEHAyfypQMLATGQKQRVCLArALILQ--PSI------IIADEALN 178
Cdd:PRK03695 90 LT-LHQPDKTRTEAVASA-LNEVAEALGLDDKLGRSV----NQLSGGEWQRVRLA-AVVLQvwPDInpagqlLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 179 GLDMAMRS---QILNLFLELqeemGVSfVYVSQHI--GVIKHiTDKIIVMHEGDVVEAGETHEVL 238
Cdd:PRK03695 163 SLDVAQQAaldRLLSELCQQ----GIA-VVMSSHDlnHTLRH-ADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-209 |
2.38e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRM-----------IFQdp 96
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMsqafslygeltVRQ-- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 97 NTSLNPRLqigtilegplkrnTSMTPDARMRRVKDTLQRVGLLpEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEA 176
Cdd:NF033858 359 NLELHARL-------------FHLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190
....*....|....*....|....*....|...
gi 447197775 177 LNGLDMAMRSQILNLFLELQEEMGVSfVYVSQH 209
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVT-IFISTH 456
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-215 |
2.50e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.93 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIrvngellehkdysTRCKLIRMIF--QDPntslnpRLQI 106
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-------------ARPAGARVLFlpQRP------YLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 GTilegpLKR------NTSMTPDARMRRVkdtLQRVGL--LPEHAYF---YPQMLATGQKQRVCLARALILQPSIIIADE 175
Cdd:COG4178 440 GT-----LREallypaTAEAFSDAELREA---LEAVGLghLAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447197775 176 ALNGLDMAMRSQILNLfleLQEEM-GVSFVYVSQHIGVIKH 215
Cdd:COG4178 512 ATSALDEENEAALYQL---LREELpGTTVISVGHRSTLAAF 549
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-236 |
3.15e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVapTGGEI-RVNGELLEH 79
Cdd:PRK09984 1 MQTIIRVEKLAKTF---------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGDKSaGSHIELLGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 ---------KDYSTRCKLIRMIFQDPNtsLNPRLqigTILEGPLKRNTSMTP----------DARMRRVKDTLQRVGLlp 140
Cdd:PRK09984 70 tvqregrlaRDIRKSRANTGYIFQQFN--LVNRL---SVLENVLIGALGSTPfwrtcfswftREQKQRALQALTRVGM-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 141 ehAYFYPQMLAT---GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHIT 217
Cdd:PRK09984 143 --VHFAHQRVSTlsgGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYC 220
|
250
....*....|....*....
gi 447197775 218 DKIIVMHEGDVVEAGETHE 236
Cdd:PRK09984 221 ERIVALRQGHVFYDGSSQQ 239
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-231 |
7.89e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 21 LRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMV--APTGGEIRVngellehkdystrcklirmifqdpnt 98
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 99 slnPRLQIG---TILEGPLKRNTsmtPDARMRRvkdtLQRVGLlpEHAYFY---PQMLATGQKQRVCLARALILQPSIII 172
Cdd:COG2401 92 ---PDNQFGreaSLIDAIGRKGD---FKDAVEL----LNAVGL--SDAVLWlrrFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 173 ADEALNGLD--MAMRsqILNLFLELQEEMGVSFVYVSQHIGVIKHIT-DKIIVMHEGDVVEA 231
Cdd:COG2401 160 IDEFCSHLDrqTAKR--VARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-194 |
1.02e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 33 SFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQdpnTSLNPRLqigTILEG 112
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQ---PGIKTEL---TALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 113 pLKRNTSMTPDARMRRVKDTLQRVGL-----LPEHAyfypqmLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:PRK13538 95 -LRFYQRLHGPGDDEALWEALAQVGLagfedVPVRQ------LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
....*..
gi 447197775 188 ILNLFLE 194
Cdd:PRK13538 168 LEALLAQ 174
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-188 |
1.32e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKlIRMIFQDPNTSLNPRLQIGT 108
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQFDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKRNTSMTPDArmrrVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQI 188
Cdd:PRK13536 136 LVFGRYFGMSTREIEA----VIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-243 |
1.73e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrSGFLrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllEHK 80
Cdd:PRK11288 1 SSPYLSFDGIGKTF---PGVK------ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--EMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKL---IRMIFQDPNtsLNPRLQIG-TILEGPLKRNTSMTPDARMR-RVKDTLQRVGLlpehaYFYPQM----LA 151
Cdd:PRK11288 70 FASTTAALaagVAIIYQELH--LVPEMTVAeNLYLGQLPHKGGIVNRRLLNyEAREQLEHLGV-----DIDPDTplkyLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 152 TGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVea 231
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYV-- 219
|
250
....*....|..
gi 447197775 232 gETHEVLADPQH 243
Cdd:PRK11288 220 -ATFDDMAQVDR 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-230 |
1.79e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.39 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDpntslnprLQIG 107
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTD--------FHLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRntsmtpDARMRRVKDTLQRVGL-----LPEHAYFYPQmLATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:PRK10522 410 DQLLGPEGK------PANPALVEKWLERLKMahkleLEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447197775 183 AMRSQILNLFLELQEEMGVSFVYVSqHIGVIKHITDKIIVMHEGDVVE 230
Cdd:PRK10522 483 HFRREFYQVLLPLLQEMGKTIFAIS-HDDHYFIHADRLLEMRNGQLSE 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-238 |
2.22e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 31 PVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVaPTGGEIRVNGELLEhkDYST------RCKLIRmifQDPNTSLNPRL 104
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLS--DWSAaelarhRAYLSQ---QQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 QIGTiLEGPLKRNTSMTPDArmrrVKDTLQRVGLLPehayFYPQMLAT---GQKQRVCLArALILQ--PSI------IIA 173
Cdd:COG4138 88 QYLA-LHQPAGASSEAVEQL----LAQLAEALGLED----KLSRPLTQlsgGEWQRVRLA-AVLLQvwPTInpegqlLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 174 DEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
32-225 |
2.56e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELlehkdystrckliRMIFQDPNTSLNPRLqigtile 111
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-------------RIGYVPQKLYLDTTL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 gPL--KRNTSMTPDARMRRVKDTLQRVGllPEHAYFYP-QMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQI 188
Cdd:PRK09544 83 -PLtvNRFLRLRPGTKKEDILPALKRVQ--AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 447197775 189 LNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHE 225
Cdd:PRK09544 160 YDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-232 |
4.47e-15 |
|
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: 72.30 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMV---APTGGEIRVNGELLEHKDYSTRCKLIRmifQDPNT--SLNPRLQI 106
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQKCVAYVR---QDDILlpGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 GTILEGPLKRNTS------MTPDARMRRVKDTlqRVGllpeHAYFypQMLATGQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:cd03234 103 TYTAILRLPRKSSdairkkRVEDVLLRDLALT--RIG----GNLV--KGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447197775 181 DMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
28-254 |
4.48e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGM--VAPTggeIRVNGELLEH-KD-YSTRC------KLIRMIFQDPN 97
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPG---FRVEGKVTFHgKNlYAPDVdpvevrRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 98 ---TSLNPRLQIGTILEGpLKRNTSMTPDARMRR------VKDTLQRVGLlpehayfypqMLATGQKQRVCLARALILQP 168
Cdd:PRK14243 102 pfpKSIYDNIAYGARING-YKGDMDELVERSLRQaalwdeVKDKLKQSGL----------SLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 169 SIIIADEALNGLDMAMRSQILNLFLELQEEMgvSFVYVSQHIGVIKHITDKIIVMH---------EGDVVEAGETHEVLA 239
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFN 248
|
250
....*....|....*
gi 447197775 240 DPQHPITQRMIESHF 254
Cdd:PRK14243 249 SPQQQATRDYVSGRF 263
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-226 |
5.81e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKdySTRCKL---IRMIFQDpntslnpRLQ 105
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR--SPQDGLangIVYISED-------RKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IGTILEGPLKRNTSMTP-------------DARMRRVKDTL-----------QRVGLLpehayfypqmlATGQKQRVCLA 161
Cdd:PRK10762 339 DGLVLGMSVKENMSLTAlryfsraggslkhADEQQAVSDFIrlfniktpsmeQAIGLL-----------SGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-226 |
8.41e-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: 69.88 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIrvngELLEHKDystrcklirMIFqdpntslnprlqigt 108
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGED---------LLF--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ilegplkrntsmtpdarmrrvkdtlqrvglLPEHAYF----------YP--QMLATGQKQRVCLARALILQPSIIIADEA 176
Cdd:cd03223 69 ------------------------------LPQRPYLplgtlreqliYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447197775 177 LNGLDMAMRSQILNLFlelqEEMGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:cd03223 119 TSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-238 |
1.25e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 31 PVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnPRLQIGTIL 110
Cdd:PRK10575 29 PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL-----PAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 111 E----------GPLKRNTSmtpdARMRRVKDTLQRVGLLPeHAYFYPQMLATGQKQRVCLArALILQPS-IIIADEALNG 179
Cdd:PRK10575 104 ElvaigrypwhGALGRFGA----ADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIA-MLVAQDSrCLLLDEPTSA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 180 LDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
2.44e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFVTRSgflrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKL---------VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 DYSTRCKlIRMIFQ----DPNTSLNPRLQIgtilegpLKRNTSMTPdARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQ 156
Cdd:PRK13537 75 ARHARQR-VGVVPQfdnlDPDFTVRENLLV-------FGRYFGLSA-AAARALVPPLLEFAKLENKADAKVGELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHE 236
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
...
gi 447197775 237 VLA 239
Cdd:PRK13537 225 LIE 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-183 |
3.88e-14 |
|
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: 68.92 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLeHKDYSTRCKLIRMIFQDPntSLNPRLqig 107
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLP--GLKPEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEG-----PLKRNTSMTPDarmrrvkDTLQRVGL-----LPEHAyfypqmLATGQKQRVCLARALILQPSIIIADEAL 177
Cdd:TIGR01189 89 SALENlhfwaAIHGGAQRTIE-------DALAAVGLtgfedLPAAQ------LSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*.
gi 447197775 178 NGLDMA 183
Cdd:TIGR01189 156 TALDKA 161
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-236 |
6.06e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 22 RKQIQHAVkpvSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAP---TGGEIRVNGELLEHKDYSTRCKLIRmifQDpnt 98
Cdd:TIGR00955 37 RKHLLKNV---SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYVQ---QD--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 99 slnpRLQIGT-------ILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEH-----AYFYPQMLATGQKQRVCLARALIL 166
Cdd:TIGR00955 108 ----DLFIPTltvrehlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 167 QPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHE 236
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
32-231 |
1.59e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIrvngeLLEHKDYSTrcklirmifqdpntsLNP---RLQIGT 108
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-----LFEGEDIST---------------LKPeiyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGP---------------LKRNtsMTPDarMRRVKDTLQRVGlLPEHAYFYP-QMLATGQKQRVCLARALILQPSIII 172
Cdd:PRK10247 86 CAQTPtlfgdtvydnlifpwQIRN--QQPD--PAIFLDDLERFA-LPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 173 ADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVM--HEGDVVEA 231
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHAGEMQEA 220
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-239 |
1.59e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.92 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 12 KDFVTRSGflRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEllehkdystrCKLIRM 91
Cdd:PRK13545 25 KDLFFRSK--DGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 92 ifqdpNTSLNPRLqigTILEGPLKRNTSMtpDARMRRVKDTLQRVGLLPEHAYFYPQMLAT---GQKQRVCLARALILQP 168
Cdd:PRK13545 93 -----SSGLNGQL---TGIENIELKGLMM--GLTKEKIKEIIPEIIEFADIGKFIYQPVKTyssGMKSRLGFAISVHINP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 169 SIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-237 |
1.68e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHkdFVTRSGflrkqiQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS 83
Cdd:COG3845 257 VLEVENLS--VRDDRG------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCKL-IRMIFQDpntslnpRLQIGTILEGPLKRNTSMTpdarmRRVKDTLQRVGLL----------------------P 140
Cdd:COG3845 329 ERRRLgVAYIPED-------RLGRGLVPDMSVAENLILG-----RYRRPPFSRGGFLdrkairafaeelieefdvrtpgP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 141 EHAyfyPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKI 220
Cdd:COG3845 397 DTP---ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRI 472
|
250
....*....|....*..
gi 447197775 221 IVMHEGDVVEAGETHEV 237
Cdd:COG3845 473 AVMYEGRIVGEVPAAEA 489
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-239 |
1.94e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEH---KDYSTRCKLIrmifqdpntSLNPRL 104
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqlDSWRSRLAVV---------SQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 105 QIGTI-----LEGPLKRNTSMTPDARMRRVKDTLQRVgllpehayfyPQ-----------MLATGQKQRVCLARALILQP 168
Cdd:PRK10789 401 FSDTVanniaLGRPDATQQEIEHVARLASVHDDILRL----------PQgydtevgergvMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 169 SIIIADEALNGLDMAMRSQILNLFLELQEEmgvSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGeTHEVLA 239
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQRG-NHDQLA 537
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-240 |
3.54e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.53 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELlehkdystrcKLIRMifqdpNTSLNPRLqi 106
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV----------SVIAI-----SAGLSGQL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 gTILEGPLKRNTSMtpDARMRRVKDTLQRVGLLPEHAYFYPQML---ATGQKQRVCLARALILQPSIIIADEALNGLDMA 183
Cdd:PRK13546 101 -TGIENIEFKMLCM--GFKRKEIKAMTPKIIEFSELGEFIYQPVkkySSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 184 MRSQILNLFLELQEEMGVSFvYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIF-FVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-236 |
3.62e-13 |
|
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: 68.70 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMV-APTGGEIRVNGELLehkDYSTRCKLIR----MIFQD-PNTSLNP 102
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPV---DIRNPAQAIRagiaMVPEDrKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIG-TILEGPLKRNTSMT---PDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:TIGR02633 353 ILGVGkNITLSVLKSFCFKMridAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 179 GLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG----DVVEAGETHE 236
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGklkgDFVNHALTQE 493
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-95 |
4.81e-13 |
|
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: 68.29 E-value: 4.81e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQD 95
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSD 414
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
32-238 |
6.51e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYSTRcKLIRMIfqdpntSLNPrlQIGTILE 111
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSR-QLARRL------ALLP--QHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 GPLKRNT-------------SMTPDARMrRVKDTLQRVGL--LPEHAYfypQMLATGQKQRVCLARALILQPSIIIADEA 176
Cdd:PRK11231 90 GITVRELvaygrspwlslwgRLSAEDNA-RVNQAMEQTRInhLADRRL---TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 177 LNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-239 |
8.68e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehKDYS-----TRCKLIRM---IFQDpnTS 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTlaslrNQVALVSQnvhLFND--TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 100 LN----------PRLQIgtilEGPLKRNTSMTPDARMRRVKDTLqrVGllpEHAYfypqMLATGQKQRVCLARALILQPS 169
Cdd:PRK11176 434 ANniayarteqySREQI----EEAARMAYAMDFINKMDNGLDTV--IG---ENGV----LLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 170 IIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-222 |
9.75e-13 |
|
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: 65.89 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 33 SFTLEA-------GQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK------DYSTRCK-LIRMIFQDPNT 98
Cdd:cd03237 12 EFTLEVeggsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKpqyikaDYEGTVRdLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 99 S-------LNPrLQIGTILEgplkrntsmtpdarmRRVKDtlqrvgllpehayfypqmLATGQKQRVCLARALILQPSII 171
Cdd:cd03237 92 HpyfkteiAKP-LQIEQILD---------------REVPE------------------LSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447197775 172 IADEALNGLDMAMR---SQILNLFLELQEEmgVSFVyVSQHIGVIKHITDKIIV 222
Cdd:cd03237 138 LLDEPSAYLDVEQRlmaSKVIRRFAENNEK--TAFV-VEHDIIMIDYLADRLIV 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-241 |
1.82e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGmVAPTG---GEIRVNGELLEHKDYSTRCKL-IRMIFQDpnTSLNPRLQIG 107
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFDGEVCRFKDIRDSEALgIVIIHQE--LALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 --TILEGPLKRNTSMTPDARMRRVKDTLQRVGlLPEHayfyPQMLAT----GQKQRVCLARALILQPSIIIADE---ALN 178
Cdd:NF040905 97 enIFLGNERAKRGVIDWNETNRRARELLAKVG-LDES----PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEptaALN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 179 GLDMAmrsQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVeagETHEVLADP 241
Cdd:NF040905 172 EEDSA---ALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTI---ETLDCRADE 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-230 |
2.31e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKD-YSTRCKLIRMIFQDpntslnpRLQIG 107
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITES-------RRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQM----------------LATGQKQRVCLARALILQPSII 171
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRellalkchsvnqniteLSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447197775 172 IADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVE 230
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-242 |
2.59e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 31 PVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKdySTR---------CK---------LIRMI 92
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR--SPRdairagimlCPedrkaegiiPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 93 FQDPNTSLNPR-LQIGTILEGPLKRNTSMTPDARMR-RVKDTLQRVGLLpehayfypqmlATGQKQRVCLARALILQPSI 170
Cdd:PRK11288 349 ADNINISARRHhLRAGCLINNRWEAENADRFIRSLNiKTPSREQLIMNL-----------SGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 171 IIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVveAGETHEVLADPQ 242
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI--AGELAREQATER 486
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-226 |
2.89e-12 |
|
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: 64.03 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehkdystrckliRMIFqdpnTSLNPRLQIGTILE 111
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------------SIAY----VSQEPWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 gplkrNTSMTPDARMRRVKDTLQRVGLLPEHAYFyPQMLAT-----------GQKQRVCLARALILQPSIIIADEALNGL 180
Cdd:cd03250 85 -----NILFGKPFDEERYEKVIKACALEPDLEIL-PDGDLTeigekginlsgGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447197775 181 DMAMRSQIL-NLFLELQEEmGVSFVYVSQHIGVIKHiTDKIIVMHEG 226
Cdd:cd03250 159 DAHVGRHIFeNCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-242 |
3.08e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 3 ALLEVTNLHKDFVTRSgflrkqiqhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDY 82
Cdd:PRK10895 2 ATLTAKNLAKAYKGRR---------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 83 STRCKliRMIFQDPN-TSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLlpEHAY-FYPQMLATGQKQRVCL 160
Cdd:PRK10895 73 HARAR--RGIGYLPQeASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLRdSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 161 ARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAD 240
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
..
gi 447197775 241 PQ 242
Cdd:PRK10895 228 EH 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-238 |
5.77e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 7 VTNLHKDFVTRsGFLRKQIQHAVkpvSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRC 86
Cdd:PRK10253 5 VARLRGEQLTL-GYGKYTVAENL---TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 87 KLIRMIFQDPNTSLNPRLQiGTILEGPLKRNTSMTpdaRMRR-----VKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLA 161
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQ-ELVARGRYPHQPLFT---RWRKedeeaVTKAMQATGI-THLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 162 RALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVL 238
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-228 |
2.81e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.27 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 18 SGFLRKQIQHAVKpvsFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVN-----GELLEHKdystrcklirmi 92
Cdd:PRK10636 320 AGYGDRIILDSIK---LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQ------------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 93 fqdpntslnprLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIII 172
Cdd:PRK10636 385 -----------LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 173 ADEALNGLDMAMRSQILNLFLELQEemgvSFVYVSQHIGVIKHITDKIIVMHEGDV 228
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
146-251 |
4.16e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 146 YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHE 225
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
90 100 110
....*....|....*....|....*....|
gi 447197775 226 ----GDVVEAGETHEVLADPQHPITQRMIE 251
Cdd:PTZ00265 1434 pdrtGSFVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-239 |
5.79e-11 |
|
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: 62.66 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 22 RKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNG-ELLEHKDYSTRCKlIRMIFQDP---- 96
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIGLHDLRFK-ITIIPQDPvlfs 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 97 ---NTSLNPRLQ-----IGTILE-GPLKRNTSMTPDArmrrvkdtlqrvglLPEHAYFYPQMLATGQKQRVCLARALILQ 167
Cdd:TIGR00957 1374 gslRMNLDPFSQysdeeVWWALElAHLKTFVSALPDK--------------LDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 168 PSIIIADEALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHITdKIIVMHEGDVVEAGETHEVLA 239
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTV--LTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-181 |
6.94e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHKDFvtrsgflrkQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEhKDYS 83
Cdd:PRK13540 1 MLDVIELDFDY---------HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 TRCKliRMIFQDPNTSLNPRLqigTILEGPL----KRNTSMTPDARMRRVKdtlqrvgllPEHAYFYP-QMLATGQKQRV 158
Cdd:PRK13540 71 TYQK--QLCFVGHRSGINPYL---TLRENCLydihFSPGAVGITELCRLFS---------LEHLIDYPcGLLSSGQKRQV 136
|
170 180
....*....|....*....|...
gi 447197775 159 CLARALILQPSIIIADEALNGLD 181
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-229 |
1.04e-10 |
|
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: 59.58 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 14 FVTRSGFLRKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMvapTGGEIRVNGEL----LEHKDYSTRCKli 89
Cdd:cd03233 11 FTTGKGRSKIPI---LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIhyngIPYKEFAEKYP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 90 rmifqdpntslnprlqiGTIL---EGPLKrNTSMTpdarmrrVKDTLQRVGLLPEHAYFypQMLATGQKQRVCLARALIL 166
Cdd:cd03233 83 -----------------GEIIyvsEEDVH-FPTLT-------VRETLDFALRCKGNEFV--RGISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447197775 167 QPSIIIADEALNGLDMAMRSQILNLFLELQEEMG-VSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-226 |
2.14e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 1 MSALLEVTNLHKDFvtrSGFlrkqiqHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:PRK10762 1 MQALLQLKGIDKAF---PGV------KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 81 D-YSTRCKLIRMIFQDPNtsLNPRLQIG-TILEGPLKRNTSMTPD-ARMRRVKDT-LQRVGlLPEHAYFYPQMLATGQKQ 156
Cdd:PRK10762 72 GpKSSQEAGIGIIHQELN--LIPQLTIAeNIFLGREFVNRFGRIDwKKMYAEADKlLARLN-LRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-236 |
8.88e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGmvAPTG---GEIRVNGELLEHKDYSTRCKL-IRMIFQD-PNTSLNPR 103
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGrweGEIFIDGKPVKIRNPQQAIAQgIAMVPEDrKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIG-TILEGPLKRNTSMT---PDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNG 179
Cdd:PRK13549 356 MGVGkNITLAALDRFTGGSridDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 180 LDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEG----DVVEAGETHE 236
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGklkgDLINHNLTQE 495
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-181 |
2.59e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 22 RKQIQhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellEH--KDYST---RCKlIRMIFQDP 96
Cdd:PTZ00265 395 RKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHnlKDINLkwwRSK-IGVVSQDP 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 97 -----------------------------------NTSLNPRLQIGTILEGPLK---RNTSMTPDARMRRVKDTLQR--- 135
Cdd:PTZ00265 470 llfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNdmsNTTDSNELIEMRKNYQTIKDsev 549
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 136 ------------VGLLPEHayfYPQM-------LATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:PTZ00265 550 vdvskkvlihdfVSALPDK---YETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-75 |
8.78e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 8.78e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 5 LEVTNLHKDFVTRsgFLrkqiqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVnGE 75
Cdd:PRK11819 325 IEAENLSKSFGDR--LL-------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE 385
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
29-239 |
1.02e-08 |
|
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: 54.53 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqigT 108
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP-----------I 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKRNTsmtpDARMRRVKDTLQR---VGLLPEHAYFYPQML-----------ATGQKQRVCLARALILQPSIIIAD 174
Cdd:cd03288 106 LFSGSIRFNL----DPECKCTDDRLWEaleIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEEMGVsfVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:cd03288 182 EATASIDMATENILQKVVMTAFADRTV--VTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-199 |
1.64e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNgellehkdystrCKLIRMIFQDPNTSLNP-RLQIG 107
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG------------TKLEVAYFDQHRAELDPeKTVMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGplkrNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQRVCLARaLILQPS-IIIADEALNGLDMAMrs 186
Cdd:PRK11147 403 NLAEG----KQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVET-- 475
|
170
....*....|...
gi 447197775 187 qilnlfLELQEEM 199
Cdd:PRK11147 476 ------LELLEEL 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-181 |
1.85e-08 |
|
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: 54.56 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVnGEL--LEHKDYStRCKLirmifqDPNTSL-------NP 102
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETvkLAYVDQS-RDAL------DPNKTVweeisggLD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 103 RLQIGtilegplkrNTSMTPDARMRRVK----DTLQRVGllpehayfypqMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:TIGR03719 413 IIKLG---------KREIPSRAYVGRFNfkgsDQQKKVG-----------QLSGGERNRVHLAKTLKSGGNVLLLDEPTN 472
|
...
gi 447197775 179 GLD 181
Cdd:TIGR03719 473 DLD 475
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-232 |
1.97e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 4 LLEVTNLHkdfvtrSGFLRKQIqhaVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVA--PTGGEIRVNGELLEHKD 81
Cdd:CHL00131 7 ILEIKNLH------ASVNENEI---LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKL-IRMIFQDP------------NTSLNPRLQIGTILEgplkrntsMTPDARMRRVKDTLQRVGLLPEhayFYPQ 148
Cdd:CHL00131 78 PEERAHLgIFLAFQYPieipgvsnadflRLAYNSKRKFQGLPE--------LDPLEFLEIINEKLKLVGMDPS---FLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 149 ML----ATGQKQRVCLARALILQPSIIIADEALNGLDM-AMR--SQILNLFLELQeemgvsfvyvsQHIGVIKH------ 215
Cdd:CHL00131 147 NVnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIdALKiiAEGINKLMTSE-----------NSIILITHyqrlld 215
|
250
....*....|....*....
gi 447197775 216 --ITDKIIVMHEGDVVEAG 232
Cdd:CHL00131 216 yiKPDYVHVMQNGKIIKTG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-236 |
2.31e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 6 EVTNLHKDFVTRSGFLRKQIQHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYS-- 83
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANea 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 84 --------TRCKLIRMIFQDPNTSLNP--------RLQIGTILEGPLKRNTSMTPDARmrRVKDTLQRVGLlpehayfyp 147
Cdd:PRK10982 321 inhgfalvTEERRSTGIYAYLDIGFNSlisnirnyKNKVGLLDNSRMKSDTQWVIDSM--RVKTPGHRTQI--------- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 148 QMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLEL-QEEMGVsfVYVSQHIGVIKHITDKIIVMHEG 226
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNG 467
|
250
....*....|
gi 447197775 227 DVVEAGETHE 236
Cdd:PRK10982 468 LVAGIVDTKT 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-71 |
3.20e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 3.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447197775 5 LEVTNLHKDFVTRSGFlrkqiqhavKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIR 71
Cdd:PRK15064 320 LEVENLTKGFDNGPLF---------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-232 |
3.34e-08 |
|
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: 54.25 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 28 AVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehKDYSTRCKLIRMifqdpNTSLNPRLQI- 106
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-----KDIETNLDAVRQ-----SLGMCPQHNIl 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 107 ---GTILEGPL--KRNTSMTPDARMRRVKDTLQRVGL---LPEHAyfypQMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:TIGR01257 1015 fhhLTVAEHILfyAQLKGRSWEEAQLEMEAMLEDTGLhhkRNEEA----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447197775 179 GLDMAMRSQILNLFLELQEemGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAG 232
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-224 |
5.19e-08 |
|
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: 52.37 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 21 LRKQIQHAVKPVSFTL------EAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNG---ELLEH------KDYSTR 85
Cdd:cd03236 2 LEDEPVHRYGPNSFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDEfrgselQNYFTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 86 CK--LIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDarmrRVKDTLQRVGLLPEHAyfypQMLATGQKQRVCLARA 163
Cdd:cd03236 82 LLegDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLD----ELVDQLELRHVLDRNI----DQLSGGELQRVAIAAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 164 LILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMH 224
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-226 |
5.24e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELlehkdystrcklirmifqdpntSLNPrlQIGT 108
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI----------------------SFSP--QTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKRNT--SMTPDA-RMRRVKDTLQrvglLPEHAYFYPQ-----------MLATGQKQRVCLARALILQPSIIIAD 174
Cdd:TIGR01271 498 IMPGTIKDNIifGLSYDEyRYTSVIKACQ----LEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447197775 175 EALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQhigvIKHI--TDKIIVMHEG 226
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSK----LEHLkkADKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-222 |
5.78e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 33 SFTLEA-------GQTIGFIGQNGSGKSTLARMLAGMVAPTGGEirVNGEL-LEHK------DYSTRCK-LIRMIFQDPN 97
Cdd:PRK13409 352 DFSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELkISYKpqyikpDYDGTVEdLLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 98 TS-----LNPRLQIGTILEgplkrntsmtpdarmRRVKDtlqrvgllpehayfypqmLATGQKQRVCLARALILQPSIII 172
Cdd:PRK13409 430 SSyykseIIKPLQLERLLD---------------KNVKD------------------LSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447197775 173 ADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIV 222
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-239 |
7.93e-08 |
|
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: 53.03 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLehkdYSTRCKLIRmifqdpNTSLNPRLQIGTILE 111
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA----YVPQQAWIQ------NDSLRENILFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 GPLKRNT----SMTPDARMRRVKDTLQrvglLPEHAYfypqMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQ 187
Cdd:TIGR00957 727 EKYYQQVleacALLPDLEILPSGDRTE----IGEKGV----NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 188 IlnlFLELQEEMGV----SFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLA 239
Cdd:TIGR00957 799 I---FEHVIGPEGVlknkTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-252 |
8.72e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehkdystrCKLIRMIFQDPNTSLNPRLQIGTILE 111
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-----------CDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 GPLKRNT---SMTPDARM------RRVKDTLQRVGL-LPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLD 181
Cdd:PLN03232 1324 GTVRFNIdpfSEHNDADLwealerAHIKDVIDRNPFgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 182 MAMRSQILNLFLElqEEMGVSFVYVSQHIGVIKHiTDKIIVMHEGDVVEAGETHEVLADPQHPITqRMIES 252
Cdd:PLN03232 1404 VRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF-RMVHS 1470
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-181 |
1.07e-07 |
|
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: 52.24 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIR-------------------------VNGELLEHKD 81
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgikvgylpqepqldptktvrenVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 82 YSTRCKLIRMIFQDPNTSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQrvgLLPEHAYFypQMLATGQKQRVCLA 161
Cdd:TIGR03719 99 ALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALR---CPPWDADV--TKLSGGERRRVALC 173
|
170 180
....*....|....*....|
gi 447197775 162 RALILQPSIIIADEALNGLD 181
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
27-181 |
1.36e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.39 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 27 HAV-KPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVApTGGEIRVNGellehkdystrCKLIRMIFQDPNTSLNPRLQ 105
Cdd:cd03289 17 NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-----------VSWNSVPLQKWRKAFGVIPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 106 IGTILEGPLKRNtsMTP-----DARMRRVKDtlqRVGLLPEHAYFYPQM----------LATGQKQRVCLARALILQPSI 170
Cdd:cd03289 85 KVFIFSGTFRKN--LDPygkwsDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcvLSHGHKQLMCLARSVLSKAKI 159
|
170
....*....|.
gi 447197775 171 IIADEALNGLD 181
Cdd:cd03289 160 LLLDEPSAHLD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-181 |
1.55e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMvAPTGGEIRVNGELLEHKDYSTRCKLIRMIFQDPntslnprlqigTILE 111
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKV-----------FIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 112 GPLKRNtsMTP-----DARMRRVKDtlqRVGL------LPEHAYFYPQ----MLATGQKQRVCLARALILQPSIIIADEA 176
Cdd:TIGR01271 1306 GTFRKN--LDPyeqwsDEEIWKVAE---EVGLksvieqFPDKLDFVLVdggyVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
....*
gi 447197775 177 LNGLD 181
Cdd:TIGR01271 1381 SAHLD 1385
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-229 |
1.74e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 24 QIQhAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGellehKDYStrcklirmifqDPNTSLNPR 103
Cdd:PRK11614 17 KIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-----KDIT-----------DWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIGTILEG-------PLKRNTSM--------TPDARMRRVKDTLQRvglLPEHAYFYPQMLATGQKQRVCLARALILQP 168
Cdd:PRK11614 80 EAVAIVPEGrrvfsrmTVEENLAMggffaerdQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 169 SIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-182 |
2.19e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 31 PVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGElleHKDYSTRCKLIRMIFQDPntSLNPRLqigTIL 110
Cdd:PRK13543 29 PLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHLP--GLKADL---STL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 111 EgplkrNTSMTPDARMRRVKDT----LQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:PRK13543 101 E-----NLHFLCGLHGRRAKQMpgsaLAIVGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-229 |
3.21e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 34 FTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGEL----LEhkdystrcklirmifQDPntslnPRLQIGT- 108
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivarLQ---------------QDP-----PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ---ILEG------PLKRNTSMT------PDARM--------------------RRVKDTLQRVGLLPEHAYfypQMLATG 153
Cdd:PRK11147 84 ydfVAEGieeqaeYLKRYHDIShlvetdPSEKNlnelaklqeqldhhnlwqleNRINEVLAQLGLDPDAAL---SSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 154 QKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEemgvSFVYVSQHIGVIKHITDKIIVMHEGDVV 229
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-226 |
4.42e-07 |
|
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: 49.25 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHKDYSTRCKLIR----MIFQDPnTSLNPRLQIG 107
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRysvaYAAQKP-WLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 TILEGPLKRNtsmtpdaRMRRVKD--TLQ-RVGLLPehayFYPQM--------LATGQKQRVCLARALILQPSIIIADEA 176
Cdd:cd03290 99 ITFGSPFNKQ-------RYKAVTDacSLQpDIDLLP----FGDQTeigerginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447197775 177 LNGLDMAMRSQILNL-FLELQEEMGVSFVYVSQHIGVIKHiTDKIIVMHEG 226
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
39-239 |
4.88e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 39 GQTIGFIGQNGSGKSTLARMLAGMVAPTGgeirVNGELLEHKDYSTRCKLIRMIFQDPNTSLNPRLQIGTILE--GPLKR 116
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVfcSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 117 NTSMTPDARMRRVKDTLQRVGLLP-EHAYF---YPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLF 192
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKcENTIIgnsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447197775 193 LELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:PLN03211 250 GSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
153-251 |
5.22e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 153 GQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFL--ELQeemGVSFVYVSQHIGVIKHItDKIIVMHEGDVVE 230
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIkdELR---GKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
90 100
....*....|....*....|.
gi 447197775 231 AGETHEVLADpqHPITQRMIE 251
Cdd:PLN03130 820 EGTYEELSNN--GPLFQKLME 838
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-226 |
5.75e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELlehkdystrcklirmifqdpntSLNPrlQIGT 108
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI----------------------SFSS--QFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 109 ILEGPLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYPQ----------MLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:cd03291 109 IMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447197775 179 GLDMAMRSQILNLFLeLQEEMGVSFVYVSQHIGVIKhITDKIIVMHEG 226
Cdd:cd03291 189 YLDVFTEKEIFESCV-CKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-70 |
1.11e-06 |
|
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: 49.40 E-value: 1.11e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 447197775 33 SFTLEA-------GQTIGFIGQNGSGKSTLARMLAGMVAPTGGEI 70
Cdd:COG1245 353 GFSLEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV 397
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-239 |
1.35e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLA----GMVAPTGGEIRVNG----ELLEHKdystRCKLIRMIFQD---PN 97
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpeEIKKHY----RGDVVYNAETDvhfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 98 TSLNPRLQIGTILEGPLKRNTSMTPDARMRRVKDTLQRV-GLlpEHAYF------YPQMLATGQKQRVCLARALILQPSI 170
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMATyGL--SHTRNtkvgndFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 171 IIADEALNGLDMAMRSQILNLFLELQEEM-GVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLA 239
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILdTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-233 |
1.39e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGM--VAPTGGEIRVNG-ELLEHKDYSTRCKLIRMIFQDP--------- 96
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGkDLLELSPEDRAGEGIFMAFQYPveipgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 97 ---NTSLNP-----------RLQIGTILEGPLKRnTSMTPDARMRRVKdtlqrVGllpehayfypqmLATGQKQRVCLAR 162
Cdd:PRK09580 97 fflQTALNAvrsyrgqepldRFDFQDLMEEKIAL-LKMPEDLLTRSVN-----VG------------FSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 163 ALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHIT-DKIIVMHEGDVVEAGE 233
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-243 |
4.84e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 32 VSFTLEAGQTIGFIGQNGSGKSTLARMLAG----MVAPTG----GEIRVNGELLEHKDySTRCKLIRMIFQDPNTSLNPR 103
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAID-APRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 104 LQIGTILEG--PLKRNTSMTPDARMRRVKDTLQRVGLLPEHAYFYpQMLATGQKQRVCLARAL---------ILQPSIII 172
Cdd:PRK13547 99 SAREIVLLGryPHARRAGALTHRDGEIAWQALALAGATALVGRDV-TTLSGGELARVQFARVLaqlwpphdaAQPPRYLL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447197775 173 ADEALNGLDMAMRSQILNLFLELQEEMGVSFVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEVLAdPQH 243
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
150-237 |
2.56e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLElQEEMGVSFVYVSQHIGVIKHItDKIIVMHEGDVV 229
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
....*...
gi 447197775 230 EAGETHEV 237
Cdd:PLN03232 819 EEGTFAEL 826
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
29-215 |
2.59e-05 |
|
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: 45.12 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 29 VKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVngellehkdySTRCKLIrMIFQDPNTSLNP-RLQIg 107
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----------PAKGKLF-YVPQRPYMTLGTlRDQI- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 108 tI----LEGPLKRNTSmtpDARMRRVKDTLQRVGLLPEHAYF-----YPQMLATGQKQRVCLARALILQPSIIIADEALN 178
Cdd:TIGR00954 536 -IypdsSEDMKRRGLS---DKDLEQILDNVQLTHILEREGGWsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|....*..
gi 447197775 179 GLDMAMRSQILNLFlelqEEMGVSFVYVSQHIGVIKH 215
Cdd:TIGR00954 612 AVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-209 |
2.61e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 25 IQHAVKPV----SFTLEAGQTIGFIGQNGSGKSTLARMLAGMvAPTG--------GEIRVNGELLE-------------H 79
Cdd:PRK10938 268 VSYNDRPIlhnlSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGysndltlfGRRRGSGETIWdikkhigyvssslH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 80 KDYSTRCKLIRMI---FQDpntslnprlQIGTIlegplkrntSMTPDARMRRVKDTLQRVGLLPEHAYFYPQMLATGQKQ 156
Cdd:PRK10938 347 LDYRVSTSVRNVIlsgFFD---------SIGIY---------QAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447197775 157 RVCLARALILQPSIIIADEALNGLDMAMRsQILNLFLE-LQEEMGVSFVYVSQH 209
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDvLISEGETQLLFVSHH 461
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-182 |
2.82e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 25 IQHAVKP----VSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIrvngelleHKDYSTRCKLIRmifQDPNTSL 100
Cdd:PRK15064 9 MQFGAKPlfenISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV--------SLDPNERLGKLR---QDQFAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 101 NPRLqIGTILEGPLK------------RNTSMTPDARMR------------------RVKDTLQRVGlLPEHAYFYP-QM 149
Cdd:PRK15064 78 EFTV-LDTVIMGHTElwevkqerdriyALPEMSEEDGMKvadlevkfaemdgytaeaRAGELLLGVG-IPEEQHYGLmSE 155
|
170 180 190
....*....|....*....|....*....|...
gi 447197775 150 LATGQKQRVCLARALILQPSIIIADEALNGLDM 182
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-74 |
3.96e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 3.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447197775 26 QHAVKPVSFTLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNG 74
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-99 |
6.32e-05 |
|
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: 41.98 E-value: 6.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447197775 39 GQTIGFIGQNGSGKSTLARMLAGMVAPTGGE-IRVNGELLEHKDYSTRCKLIRMIFQDPNTS 99
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKASGSG 63
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-80 |
6.94e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 6.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 447197775 39 GQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIRVNGELLEHK 80
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK 66
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-71 |
1.35e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.35e-04
10 20 30
....*....|....*....|....*....|...
gi 447197775 39 GQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIR 71
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR 65
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-70 |
7.98e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 7.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 447197775 21 LRKQIQHAVKPVSFTL------EAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEI 70
Cdd:COG1245 75 LEEDPVHRYGENGFRLyglpvpKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY 130
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-191 |
8.82e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 46 GQNGSGKSTLARMLAGMVAPTGGEIRVNGELLE--HKDYstrCKLIrmifqdpNTSLNPRLQIgTILEGpLK-----RNT 118
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPY---CTYI-------GHNLGLKLEM-TVFEN-LKfwseiYNS 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447197775 119 SMTPDARMRRVKDTlqrvGLLPEHAYfypqMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNL 191
Cdd:PRK13541 101 AETLYAAIHYFKLH----DLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
123-237 |
1.01e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 123 DARMRrVKDTLQRVGLlPEHAYFYPQMLATGQKQRVCLARALILQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVS 202
Cdd:NF000106 120 DARAR-ADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100 110
....*....|....*....|....*....|....*
gi 447197775 203 FVYVSQHIGVIKHITDKIIVMHEGDVVEAGETHEV 237
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
46-83 |
1.22e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.88 E-value: 1.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 447197775 46 GQNGSGKSTLARMLAGMVAPTGGEIRVNGELL--EHKDYS 83
Cdd:pfam06414 18 GQPGAGKTELARALLDELGRQGNVVRIDPDDFreLHPHYR 57
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-65 |
2.15e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 447197775 21 LRKQIQHAVKPVSFTL------EAGQTIGFIGQNGSGKSTLARMLAGMVAP 65
Cdd:PRK13409 75 LEEEPVHRYGVNGFKLyglpipKEGKVTGILGPNGIGKTTAVKILSGELIP 125
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-232 |
6.62e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.53 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447197775 150 LATGQKQRVCLARALI--LQPSIIIADEALNGLDMAMRSQILNLFLELQEEmGVSFVYVSQHIGVIKHiTDKIIVM---- 223
Cdd:cd03238 88 LSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFgpgs 165
|
90
....*....|.
gi 447197775 224 --HEGDVVEAG 232
Cdd:cd03238 166 gkSGGKVVFSG 176
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-70 |
8.48e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 8.48e-03
10 20 30
....*....|....*....|....*....|....*.
gi 447197775 35 TLEAGQTIGFIGQNGSGKSTLARMLAGMVAPTGGEI 70
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
39-71 |
8.71e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.84 E-value: 8.71e-03
10 20 30
....*....|....*....|....*....|...
gi 447197775 39 GQTIGFIGQNGSGKSTLARMLAGMVAPTGGEIR 71
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| |
