|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-324 |
0e+00 |
|
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: 561.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsVVGGDILYEGKSLLGMKEKE 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHELSGGMLQRI 164
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 245 QNPKHPYTKGLLKSKPVMGKRIDKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNVHDENHKVACWLYEERA 324
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEEA 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-265 |
1.80e-157 |
|
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: 451.06 E-value: 1.80e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGM 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHELSGGM 160
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250 260
....*....|....*....|....*
gi 1355713525 241 LEIFQNPKHPYTKGLLKSKPVMGKR 265
Cdd:COG4172 242 AELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-318 |
1.58e-134 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 385.23 E-value: 1.58e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsVVGGDILYEGKSLLGM 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG-RIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHELSGGM 160
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 241 LEIFQNPKHPYTKGLLKSKPVMGKRIDKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEICkEEAPNLNVHDENHKVACW 318
Cdd:PRK09473 247 RDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-SSAPPLEEFGPGRLRACF 323
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-325 |
1.85e-125 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 362.13 E-value: 1.85e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHF-------QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYE 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS----GEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 74 GKSLLGMKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARadEIVHSYP 153
Cdd:COG4608 79 GQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRP--EHADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 HELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 234 VIEEAPVLEIFQNPKHPYTKGLLKSKPVM-----GKRIdklySIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNV 308
Cdd:COG4608 236 IVEIAPRDELYARPLHPYTQALLSAVPVPdperrRERI----VLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLRE 311
|
330
....*....|....*..
gi 1355713525 309 HDENHKVACWLYEERAG 325
Cdd:COG4608 312 VGPGHQVACHLAEEGSG 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-238 |
1.26e-122 |
|
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: 351.04 E-value: 1.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLLGMKEKe 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK----PTSGSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRkVGIARADEIVHSYPHELSGGMLQRI 164
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-326 |
1.33e-115 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 337.10 E-value: 1.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGMKEK 83
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHELSGGMLQR 163
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 244 FQNPKHPYTKGLLKSKPVMGKRIDKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNvHDENHKVACWLYEER 323
Cdd:PRK11022 242 FRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALN-MLAGRQSKCHYPLDD 320
|
...
gi 1355713525 324 AGQ 326
Cdd:PRK11022 321 AGR 323
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-262 |
7.34e-112 |
|
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: 334.18 E-value: 7.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEE-GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLG 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS----GSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSLRGnDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARadEIVHSYPHELSGG 159
Cdd:COG1123 332 LSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250 260
....*....|....*....|...
gi 1355713525 240 VLEIFQNPKHPYTKGLLKSKPVM 262
Cdd:COG1123 489 TEEVFANPQHPYTRALLAAVPSL 511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-248 |
1.94e-105 |
|
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: 317.62 E-value: 1.94e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSkAVVELKDLQTHFqtEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVvGGDILYEGKSLLGM 80
Cdd:COG1123 1 MT-PLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKelrsLRGNDIAMIFQEPMTSLNPVfTVGEQIVETLREHeLLSKNEAYKKAIELIRKVGIARadeIVHSYPHELSGGM 160
Cdd:COG1123 77 SEA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENL-GLSRAEARARVLELLEAVGLER---RLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
....*...
gi 1355713525 241 LEIFQNPK 248
Cdd:COG1123 228 EEILAAPQ 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-260 |
2.25e-101 |
|
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: 307.77 E-value: 2.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEG-------TVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsvVGGDILYEGKSL 77
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 LGMKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLREHEL-LSKNEAYKKAIELIRKVGIARADeiVHSYPHEL 156
Cdd:COG4172 350 DGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGLDPAA--RHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 157 SGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIE 236
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....
gi 1355713525 237 EAPVLEIFQNPKHPYTKGLLKSKP 260
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-284 |
8.87e-101 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 309.09 E-value: 8.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGK------ 75
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 76 SLLGMKEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHE 155
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1355713525 236 EEAPVLEIFQNPKHPYTKGLLKSKPVMGKRidKLYSIPGQVPnLVGLDE 284
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGAM--KGLDYPRRFP-LISLEH 294
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-256 |
2.71e-99 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 291.96 E-value: 2.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGMkekelrSLRGNDIAMIFQEPMTS 103
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVFTVGEQIVETLREHELLSKNeAYKKAIELIRKVGIARADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQ-ARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 184 TALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLL 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-317 |
6.29e-97 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 289.68 E-value: 6.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEEG---------TVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYE 73
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD----GEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 74 GKSLLGMKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLRE-HELLSKNEAYKKAIELIRKVGIAraDEIVHSY 152
Cdd:PRK15079 82 GKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLL--PNLINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 153 PHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGG 232
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 233 KVIEEAPVLEIFQNPKHPYTKGLLKSKPVMGKRIDKLYSI---PGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNVH 309
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGS 318
|
....*...
gi 1355713525 310 DEnHKVAC 317
Cdd:PRK15079 319 FR-HAVSC 325
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-317 |
3.71e-94 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 282.56 E-value: 3.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGMKEK 83
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSK-----NEAYKKAIELIRKVGIARADEIVHSYPHELSG 158
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 239 PVLEIFQNPKHPYTKGLLKSKPVMGKRI---DKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNVHdeNHKV 315
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMPDFRQPLphkSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIK--GHEF 319
|
..
gi 1355713525 316 AC 317
Cdd:COG4170 320 AC 321
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-260 |
2.51e-93 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 286.99 E-value: 2.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAeSGSVV--GGDILYEGKSLL 78
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP-SPPVVypSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 GMKEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHELSG 158
Cdd:PRK15134 80 HASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|..
gi 1355713525 239 PVLEIFQNPKHPYTKGLLKSKP 260
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNSEP 261
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-322 |
2.73e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 275.30 E-value: 2.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQ------TEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTAlSIMGLIAESGSvvgGDILYEG 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIETPTG---GELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 75 KSLLGMKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIaRAdEIVHSYPH 154
Cdd:PRK11308 77 QDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RP-EHYDRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 235 IEEAPVLEIFQNPKHPYTKGLLKSKPVMG-----KRIdklySIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNVH 309
Cdd:PRK11308 234 VEKGTKEQIFNNPRHPYTQALLSATPRLNpddrrERI----KLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDY 309
|
330
....*....|...
gi 1355713525 310 DEnHKVACWLYEE 322
Cdd:PRK11308 310 DG-RLVACFAVEQ 321
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-258 |
4.45e-89 |
|
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: 266.67 E-value: 4.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmKEKEL 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS----GEVTFDGRPV---TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGnDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLsknEAYKKAIELIRKVGIAraDEIVHSYPHELSGGMLQRIM 165
Cdd:COG1124 75 KAFRR-RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQ 245
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|...
gi 1355713525 246 NPKHPYTKGLLKS 258
Cdd:COG1124 229 GPKHPYTRELLAA 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-317 |
4.02e-78 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 241.63 E-value: 4.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGMKEKE 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVE-----TLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHELSGG 159
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQnipgwTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 240 VLEIFQNPKHPYTKGLLKSKPVMGKRI---DKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNVhdENHKVA 316
Cdd:PRK15093 243 SKELVTTPHHPYTQALIRAIPDFGSAMphkSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGA--KNHLYA 320
|
.
gi 1355713525 317 C 317
Cdd:PRK15093 321 C 321
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-256 |
5.59e-69 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 215.72 E-value: 5.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGmkekelRSLRGNDIAMIFQEPMTSL 104
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAP------CALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPVFTVGEQIVETLREHELLSKNEAykkAIELIRKVGIARADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTT 184
Cdd:PRK10418 93 NPLHTMHTHARETCLALGKPADDAT---LTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 185 ALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLL 256
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-237 |
8.45e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.43 E-value: 8.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSkAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLI--AESGSVvggdiLYEGKSLL 78
Cdd:COG1136 1 MS-PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPTSGEV-----LIDGQDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 GMKEKELRSLRGNDIAMIFQEPmtSLNPVFTVGEQIvetlrehEL------LSKNEAYKKAIELIRKVGIAradEIVHSY 152
Cdd:COG1136 74 SLSERELARLRRRHIGFVFQFF--NLLPELTALENV-------ALplllagVSRKERRERARELLERVGLG---DRLDHR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 153 PHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLgVVAEMADYVVVMYGG 232
Cdd:COG1136 142 PSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDG 220
|
....*
gi 1355713525 233 KVIEE 237
Cdd:COG1136 221 RIVSD 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-261 |
1.06e-65 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 217.80 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFQTEEG-------TVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEG 74
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 75 KSLLGMKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAraDEIVHSYPH 154
Cdd:PRK10261 386 QRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLL--PEHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
250 260
....*....|....*....|....*..
gi 1355713525 235 IEEAPVLEIFQNPKHPYTKGLLKSKPV 261
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-258 |
3.74e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.78 E-value: 3.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKS-----VTALsimgliaE---SGSVvggdiLYEGKSL 77
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKStlircINLL-------ErptSGSV-----LVDGVDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 LGMKEKELRSLRGNdIAMIFQEP--MTSLnpvfTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIA-RADeivhSYPH 154
Cdd:COG1135 70 TALSERELRAARRK-IGMIFQHFnlLSSR----TVAENVALPL-EIAGVPKAEIRKRVAELLELVGLSdKAD----AYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
250 260
....*....|....*....|....
gi 1355713525 235 IEEAPVLEIFQNPKHPYTKGLLKS 258
Cdd:COG1135 220 VEQGPVLDVFANPQSELTRRFLPT 243
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-258 |
3.91e-65 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 206.20 E-value: 3.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGK----- 75
Cdd:COG4107 4 EEQPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPTSGSVYYRDRdggpr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 76 SLLGMKEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLreheLLSKNEAY----KKAIELIRKVGI--ARADEiv 149
Cdd:COG4107 80 DLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERL----MAAGERHYgdirARALEWLERVEIplERIDD-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 150 hsYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVM 229
Cdd:COG4107 154 --LPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVM 231
|
250 260
....*....|....*....|....*....
gi 1355713525 230 YGGKVIEEAPVLEIFQNPKHPYTKGLLKS 258
Cdd:COG4107 232 KNGRVVESGLTDQVLEDPQHPYTQLLVSS 260
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-258 |
5.58e-64 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 203.15 E-value: 5.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEG-----TVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLl 78
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTS----GEILINGHKL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 gmkEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARadEIVHSYPHELSG 158
Cdd:COG4167 78 ---EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLP--EHANFYPHMLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYG 232
|
250 260
....*....|....*....|
gi 1355713525 239 PVLEIFQNPKHPYTKGLLKS 258
Cdd:COG4167 233 KTAEVFANPQHEVTKRLIES 252
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
1.21e-63 |
|
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: 200.79 E-value: 1.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEKEL 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPTS---GEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNDIAMIFQEPmtSLNPVFTVGEQiVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRIM 165
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTALEN-VELPLLLAGVPKKERRERAEELLERVGLG---DRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLgVVAEMADYVVVMYGGKV 234
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-253 |
7.73e-61 |
|
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: 194.43 E-value: 7.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSvvggdILYEGKSLLG 79
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPDSGE-----ILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSLRgNDIAMIFQEP--MTSLnpvfTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADeivHSYPHELS 157
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAA---DKMPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*.
gi 1355713525 238 APVLEIFQNPkHPYTK 253
Cdd:COG1127 224 GTPEELLASD-DPWVR 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-248 |
5.31e-60 |
|
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: 192.03 E-value: 5.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEKE 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPTS---GSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGNdIAMIFQE--PMTSLnpvfTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIA-RADeivhSYPHELSGGML 161
Cdd:cd03258 77 LRKARRR-IGMIFQHfnLLSSR----TVFENVALPL-EIAGVPKAEIEERVLELLELVGLEdKAD----AYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVL 241
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 1355713525 242 EIFQNPK 248
Cdd:cd03258 227 EVFANPQ 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-258 |
4.46e-58 |
|
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: 188.09 E-value: 4.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQT-----EEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLiaesGSVVGGDILYEGKSLL 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL----EKPAQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 GMKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAraDEIVHSYPHELSG 158
Cdd:TIGR02769 77 QLDRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLR--SEDADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250 260
....*....|....*....|
gi 1355713525 239 PVLEIFQNpKHPYTKGLLKS 258
Cdd:TIGR02769 234 DVAQLLSF-KHPAGRNLQSA 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-256 |
8.56e-58 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 194.54 E-value: 8.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFQTEEGTVK-------AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSvvggdILYEGKSLLG 79
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE-----IWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSLRgNDIAMIFQEPMTSLNPVFTVGEQIVETLREHE-LLSKNEAYKKAIELIRKVGIARADEivHSYPHELSG 158
Cdd:PRK15134 352 LNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDPETR--HRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
250
....*....|....*...
gi 1355713525 239 PVLEIFQNPKHPYTKGLL 256
Cdd:PRK15134 509 DCERVFAAPQQEYTRQLL 526
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-253 |
1.03e-57 |
|
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: 186.17 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKEL 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS----GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNdIAMIFQEP--MTSLnpvfTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIaRADEivHSYPHELSGGMLQR 163
Cdd:cd03261 73 YRLRRR-MGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAE--DLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|
gi 1355713525 244 FQNPkHPYTK 253
Cdd:cd03261 225 RASD-DPLVR 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-253 |
1.21e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 185.97 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGLIaesgSVVGGDILYEGKSLlGMKEK 83
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLrCINLLE----EPDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGNdIAMIFQepmtSLN--PVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIA-RADeivhSYPHELSGGM 160
Cdd:COG1126 71 DINKLRRK-VGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAdKAD----AYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMT-MVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
250
....*....|...
gi 1355713525 241 LEIFQNPKHPYTK 253
Cdd:COG1126 221 EEFFENPQHERTR 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-240 |
2.26e-56 |
|
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: 182.29 E-value: 2.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESGsvvgGDILYEGKSLLGmkeke 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIaGLERPTS----GEVLVDGEPVTG----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 lrslRGNDIAMIFQEPmtSLNPVFTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRI 164
Cdd:cd03293 71 ----PGPDRGYVFQQD--ALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLS---GFENAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYG--GKVIEEAPV 240
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-240 |
4.60e-56 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 182.60 E-value: 4.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESgsvvGGDILYEGKSLLG 79
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLRLIaGLEKPT----SGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 mkekelrslRGNDIAMIFQEPmtSLNPVFTVGEQIVETLREHElLSKNEAYKKAIELIRKVGIARAdeiVHSYPHELSGG 159
Cdd:COG1116 78 ---------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGF---EDAYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDlgvVAE---MADYVVVMYG--GKV 234
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVLSArpGRI 219
|
....*.
gi 1355713525 235 IEEAPV 240
Cdd:COG1116 220 VEEIDV 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-258 |
1.99e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 183.46 E-value: 1.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEKE 84
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPTS---GRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRgNDIAMIFQEpmtslnpvF------TVGEQIVETLrehEL--LSKNEAYKKAIELIRKVGIA-RADeivhSYPHE 155
Cdd:PRK11153 77 LRKAR-RQIGMIFQH--------FnllssrTVFDNVALPL---ELagTPKAEIKARVTELLELVGLSdKAD----RYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250 260
....*....|....*....|...
gi 1355713525 236 EEAPVLEIFQNPKHPYTKGLLKS 258
Cdd:PRK11153 221 EQGTVSEVFSHPKHPLTREFIQS 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-240 |
4.74e-55 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 180.27 E-value: 4.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSVTALSIMGLiaESGSvvGGDILYEGKSLLGMKEKELRSLRGnDIAMIFQEPMTSL 104
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL--ESPS--QGNVSWRGEPLAKLNRAQRKAFRR-DIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTT 184
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLD--DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 185 ALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-248 |
8.01e-52 |
|
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: 170.59 E-value: 8.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmKEKEL 85
Cdd:COG1122 1 IELENL--SFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS----GEVLVDGKDI---TKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRgNDIAMIFQEPMTslnpvftvgeQIVETLREHEL--------LSKNEAYKKAIELIRKVGIAradEIVHSYPHELS 157
Cdd:COG1122 71 RELR-RKVGLVFQNPDD----------QLFAPTVEEDVafgpenlgLPREEIRERVEEALELVGLE---HLADRPPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
250
....*....|.
gi 1355713525 238 APVLEIFQNPK 248
Cdd:COG1122 216 GTPREVFSDYE 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-260 |
7.29e-51 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 169.75 E-value: 7.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEE--GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGM 80
Cdd:cd03294 16 KAFKLLAKGKSKEEILKktGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS----GKVLIDGQDIAAM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNDIAMIFQEpmTSLNPVFTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIArADEivHSYPHELSGGM 160
Cdd:cd03294 92 SRKELRELRRKKISMVFQS--FALLPHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLE-GWE--HKYPDELSGGM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
250 260
....*....|....*....|....
gi 1355713525 241 LEIFQNPKHPY----TKGLLKSKP 260
Cdd:cd03294 246 EEILTNPANDYvrefFRGVDRAKV 269
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-233 |
6.41e-50 |
|
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: 165.33 E-value: 6.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKELR 86
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS----GEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 slrgNDIAMIFQEPMTSL-NPvfTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIM 165
Cdd:cd03225 75 ----RKVGLVFQNPDDQFfGP--TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-243 |
9.67e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.93 E-value: 9.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmkEKEL 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS----GEVRVLGEDV----ARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNdIAMIFQEPmtSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIM 165
Cdd:COG1131 69 AEVRRR-IGYVPQEP--ALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGL---TDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT-VLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-236 |
3.15e-47 |
|
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: 158.45 E-value: 3.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMkEKEL 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDS----GEILIDGRDVTGV-PPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RslrgnDIAMIFQEPmtSLNPVFTVGEQIVETLREHeLLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIM 165
Cdd:cd03259 72 R-----NIGMVFQDY--ALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGL---EGLLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIE 236
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-251 |
1.72e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 160.65 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGM 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE----TPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 K-EKelrslRgnDIAMIFQEPmtSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGG 159
Cdd:COG3842 73 PpEK-----R--NVGMVFQDY--ALFPHLTVAENVAFGLRMRGV-PKAEIRARVAELLELVGL---EGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLgvvAE---MADYVVVMYGGKVIE 236
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ---EEalaLADRIAVMNDGRIEQ 216
|
250
....*....|....*
gi 1355713525 237 EAPVLEIFQNPKHPY 251
Cdd:COG3842 217 VGTPEEIYERPATRF 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-239 |
1.56e-45 |
|
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: 154.51 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLiaESGSvvGGDILYEGKSLLG 79
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGL--DRPT--SGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSLRGNDIAMIFQEPMtsLNPVFTVGEQIVETLrehELLSKNEAYKKAIELIRKVGIA-RADeivHsYPHELSG 158
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSFQ--LLPTLTALENVMLPL---ELAGRRDARARARALLERVGLGhRLD---H-YPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGvVAEMADYVVVMYGGKVIEEA 238
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVEDT 228
|
.
gi 1355713525 239 P 239
Cdd:COG4181 229 A 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-258 |
6.31e-45 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 154.18 E-value: 6.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEEG-----TVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSL 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS----GELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 lGMKEKELRSLRgndIAMIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIaRADEIVHsYPHELS 157
Cdd:PRK15112 78 -HFGDYSYRSQR---IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL-LPDHASY-YPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|.
gi 1355713525 238 APVLEIFQNPKHPYTKGLLKS 258
Cdd:PRK15112 232 GSTADVLASPLHELTKRLIAG 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-258 |
1.28e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 153.16 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMG--LIAESGSVvggdiLYEGKS-----LLGMKEKELRSLRGND 92
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKT-TLLNALSarLAPDAGEV-----HYRMRDgqlrdLYALSEAERRRLLRTE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 93 IAMIFQEPMTSLNPVFTVGEQIVETL-----------REhellskneaykKAIELIRKVGI--ARADEIvhsyPHELSGG 159
Cdd:PRK11701 91 WGFVHQHPRDGLRMQVSAGGNIGERLmavgarhygdiRA-----------TAGDWLERVEIdaARIDDL----PTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250
....*....|....*....
gi 1355713525 240 VLEIFQNPKHPYTKGLLKS 258
Cdd:PRK11701 236 TDQVLDDPQHPYTQLLVSS 254
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
20-258 |
5.66e-44 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 151.14 E-value: 5.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKS-----LLGMKEKELRSLRGNDIA 94
Cdd:TIGR02323 14 GGGKGCRDVSFDLYPGEVLGIVGESGSGKS----TLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 95 MIFQEPMTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGI--ARADEIvhsyPHELSGGMLQRIMIAVALSC 172
Cdd:TIGR02323 90 FVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdpTRIDDL----PRAFSGGMQQRLQIARNLVT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 173 NPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYT 252
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYT 245
|
....*.
gi 1355713525 253 KGLLKS 258
Cdd:TIGR02323 246 QLLVSS 251
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
8.10e-44 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 149.60 E-value: 8.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLiaESGSvvGGDILYEGKSLLGmKEKEL 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL--EEPD--SGTIIIDGLKLTD-DKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRgNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRIM 165
Cdd:cd03262 72 NELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA---DKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-244 |
5.61e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.96 E-value: 5.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGLIAESGsvvgGDILYEGKSLLGMKEKELRSLrgndIAMIFQ 98
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKPSS----GEVLLDGRDLASLSRRELARR----IAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 EPMTSLNpvFTVgEQIVET-----LREHELLSKnEAYKKAIELIRKVGIAR-ADEIVHsyphELSGGMLQRIMIAVALSC 172
Cdd:COG1120 83 EPPAPFG--LTV-RELVALgryphLGLFGRPSA-EDREAVEEALERTGLEHlADRPVD----ELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 173 NPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-259 |
7.46e-42 |
|
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: 145.52 E-value: 7.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaESGSvvgGDILYEGKSLLGMKEKELRslrgNDIAMIFQE 99
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-EPTS---GEIFIDGEDIREQDPVELR----RKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmTSLNPVFTVGEQIVeTLREHELLSKNEAYKKAIELIRKVGIARAdEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIA 179
Cdd:cd03295 84 --IGLFPHMTVEENIA-LVPKLLKWPKEKIRERADELLALVGLDPA-EFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 180 DEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLLKSK 259
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-233 |
3.50e-41 |
|
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: 141.56 E-value: 3.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMkEKEL 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLTDL-EDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRgNDIAMIFQEPmtSLNPVFTVGEQIVetlrehellskneaykkaielirkvgiaradeivhsYPheLSGGMLQRIM 165
Cdd:cd03229 72 PPLR-RRIGMVFQDF--ALFPHLTVLENIA------------------------------------LG--LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
1.62e-40 |
|
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: 139.46 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESgsvvGGDILYEGKSLlgmkEKEL 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD----SGEIKVLGKDI----KKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNdIAMIFQEPmtSLNPVFTVGEQIvetlrehellskneaykkaielirkvgiaradeivhsyphELSGGMLQRIM 165
Cdd:cd03230 69 EEVKRR-IGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKT-ILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-239 |
3.44e-40 |
|
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: 140.78 E-value: 3.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFqteEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKELR 86
Cdd:cd03256 2 EVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS----GSVLIDGTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGnDIAMIFQEPmtSLNPVFTVGEQI-------VETLREHELLSKNEAYKKAIELIRKVGIA-----RADEivhsyph 154
Cdd:cd03256 75 QLRR-QIGMIFQQF--NLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLdkayqRADQ------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 eLSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03256 145 -LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
....*
gi 1355713525 235 IEEAP 239
Cdd:cd03256 224 VFDGP 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-248 |
7.07e-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: 139.88 E-value: 7.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALS-IMGLIAESGsvvgGDILYEGKSLLGMKEKEl 85
Cdd:cd03219 2 EVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFNlISGFLRPTS----GSVLFDGEDITGLPPHE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGndIAMIFQepMTSLNPVFTVGE--QIVETLREHELLSKN-------EAYKKAIELIRKVGIA-RADEIVHsyphE 155
Cdd:cd03219 72 IARLG--IGRTFQ--IPRLFPELTVLEnvMVAAQARTGSGLLLArarreerEARERAEELLERVGLAdLADRPAG----E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKkEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
250
....*....|...
gi 1355713525 236 EEAPVLEIFQNPK 248
Cdd:cd03219 223 AEGTPDEVRNNPR 235
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-236 |
1.00e-39 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 139.02 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEKE 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPTS---GEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGNDIAMIFQepMTSLNPVFTVGEQIVETLreheLL---SKNEAYKKAIELIRKVGIAraDEIVHsYPHELSGGML 161
Cdd:TIGR02211 77 RAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPL----LIgkkSVKEAKERAYEMLEKVGLE--HRINH-RPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGvVAEMADYVVVMYGGKVIE 236
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQLFN 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-248 |
1.31e-39 |
|
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: 139.39 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMK-EKElrslrgnDIAMIFQEpmTSLNP 106
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS----GKILLNGKDITNLPpEKR-------DISYVPQN--YALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 107 VFTVGEQIVETLReHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTAL 186
Cdd:cd03299 85 HMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 187 DVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPK 248
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
1.59e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGLIA-ESGSVvggdilyegkSLL 78
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLPpTSGTV----------RLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 GMKEKELRslrgNDIAMIFQepMTSLNPVF--TVGEqIVETLREHEL-----LSKnEAYKKAIELIRKVGIA-RADEIVH 150
Cdd:COG1121 67 GKPPRRAR----RRIGYVPQ--RAEVDWDFpiTVRD-VVLMGRYGRRglfrrPSR-ADREAVDEALERVGLEdLADRPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 151 syphELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMy 230
Cdd:COG1121 139 ----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKT-ILVVTHDLGAVREYFDRVLLL- 212
|
250
....*....|....*
gi 1355713525 231 GGKVIEEAPVLEIFQ 245
Cdd:COG1121 213 NRGLVAHGPPEEVLT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-184 |
3.26e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 135.47 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGmkeKELRSLRGNdIAMIFQEPmtSL 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL----SPTEGTILLDGQDLTD---DERKSLRKE-IGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIA-RADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGL-SKREKDARAEEALEKLGLGdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1355713525 184 T 184
Cdd:pfam00005 150 A 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-243 |
8.82e-39 |
|
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: 136.93 E-value: 8.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSV-VGGDILYEGKSLLGMKEKE 84
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LrSLRGNdIAMIFQEPmtslNPV-FTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAR--ADeivHSYPHELSGGML 161
Cdd:cd03260 77 L-ELRRR-VGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKD---RLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfkTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVL 241
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
..
gi 1355713525 242 EI 243
Cdd:cd03260 226 QI 227
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-234 |
1.21e-38 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 136.30 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLI--AESGSVvggDILyeGKSLLGMKE 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLIGGLrsVQEGSL---KVL--GQELHGASK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLRGNdIAMIFQEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQ 162
Cdd:TIGR02982 75 KQLVQLRRR-IGYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 163 RIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDlGVVAEMADYVVVMYGGKV 234
Cdd:TIGR02982 149 RVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-256 |
1.30e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.90 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSkavVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLI-AESGSVV-GGDILYegkSL 77
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKT-TLLRIIaGLEtPDSGRIVlNGRDLF---TN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 LGMKEkelrslRGndIAMIFQEPMtsLNPVFTVGEQIVETLReHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELS 157
Cdd:COG1118 70 LPPRE------RR--VGFVFQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQL---EGLADRYPSQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
250
....*....|....*....
gi 1355713525 238 APVLEIFQNPKHPYTKGLL 256
Cdd:COG1118 216 GTPDEVYDRPATPFVARFL 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-257 |
3.03e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.99 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAEsgsVVGGDILYEGKSLLGMKEKE 84
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEE---ITSGDLIVDGLKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 lRSLRgNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRI 164
Cdd:PRK09493 73 -RLIR-QEAGMVFQQ--FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLA---ERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMV-IVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
250
....*....|...
gi 1355713525 245 QNPKHPYTKGLLK 257
Cdd:PRK09493 225 KNPPSQRLQEFLQ 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-239 |
4.58e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.79 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSLRGNdIAMIFQE 99
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR-IGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmtslnpvF------TVGEQIVETLREHELlSKNEAYKKAIELIRKVGIA-RAdeivHSYPHELSGGMLQRIMIAVALSC 172
Cdd:COG2884 88 --------FrllpdrTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLSdKA----KALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 173 NPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-253 |
1.30e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.78 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAE--SGSVVGGDILYEGKSLLG 79
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TLLRCLNRMNDliPGARVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEK--ELRSlrgnDIAMIFQEPmtslNPvF--TVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAraDEI---VHSY 152
Cdd:COG1117 83 PDVDvvELRR----RVGMVFQKP----NP-FpkSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALW--DEVkdrLKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 153 PHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFktSILLITHDLGVVAEMADYVVVMYGG 232
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLG 229
|
250 260
....*....|....*....|.
gi 1355713525 233 KVIEEAPVLEIFQNPKHPYTK 253
Cdd:COG1117 230 ELVEFGPTEQIFTNPKDKRTE 250
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-256 |
2.91e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 133.72 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEgtvkAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLI--AESGSVVGGDILYEGKSLLGMK 81
Cdd:PRK11264 2 SAIEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRVGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLRgNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEivhSYPHELSGGML 161
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVL 241
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*
gi 1355713525 242 EIFQNPKHPYTKGLL 256
Cdd:PRK11264 230 ALFADPQQPRTRQFL 244
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-245 |
3.79e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQthFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIA-ESGSV-VGGDILYEgKSLL 78
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTItVGGMVLSE-ETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 GMKEKelrslrgndIAMIFQEPmtslNPVF---TVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHE 155
Cdd:PRK13635 78 DVRRQ---------VGMVFQNP----DNQFvgaTVQDDVAFGL-ENIGVPREEMVERVDQALRQVGM---EDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEmADYVVVMYGGKVI 235
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
250
....*....|
gi 1355713525 236 EEAPVLEIFQ 245
Cdd:PRK13635 220 EEGTPEEIFK 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-235 |
4.37e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.02 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGLIAESGsvvgGDILYEGKSLLGMKEKELRSLrgndIAMIFQ 98
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSS----GEILLDGKDLASLSPKELARK----IAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 epmtslnpvftvgeqivetlrehellskneaykkAIELirkVGIAradEIVHSYPHELSGGMLQRIMIAVALSCNPKLLI 178
Cdd:cd03214 81 ----------------------------------ALEL---LGLA---HLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 179 ADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-256 |
1.21e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 133.29 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALS-IMGLIAESGsvvgGDILYEGKSLLGMKEKELRslRGndIAMIFQ 98
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRmINRLIEPTS----GRILIDGEDIRDLDPVELR--RR--IGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 EpmTSLNPVFTVGEQIVETLReheLL--SKNEAYKKAIELIRKVGIArADEIVHSYPHELSGGMLQRIMIAVALSCNPKL 176
Cdd:COG1125 84 Q--IGLFPHMTVAENIATVPR---LLgwDKERIRARVDELLELVGLD-PEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 177 LIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDlgvVAE---MADYVVVMYGGKVIEEAPVLEIFQNPKHPYTK 253
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHD---IDEalkLGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
...
gi 1355713525 254 GLL 256
Cdd:COG1125 235 DFV 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-264 |
5.91e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 130.03 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAE--SGSVVGGDILYEGKSLLGM 80
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKS-TLLRVFNRLIElyPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRslrgNDIAMIFQEPmtslNPV--FTVGEQIVETLREHELL-SKNEAYKKAIELIRKVGIAraDEI---VHSYPH 154
Cdd:PRK14247 76 DVIELR----RRVQMVFQIP----NPIpnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLW--DEVkdrLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFktSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250 260 270
....*....|....*....|....*....|
gi 1355713525 235 IEEAPVLEIFQNPKHPYTKgllksKPVMGK 264
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTE-----KYVTGR 248
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-256 |
6.43e-36 |
|
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: 129.77 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKEl 85
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKT----TLLRLIAGLERPDSGTILFGGEDATDVPVQE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 rslRGndIAMIFQEpmTSLNPVFTVGEQIVETLRE---HELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQ 162
Cdd:cd03296 74 ---RN--VGFVFQH--YALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQL---DWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 163 RIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLE 242
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
250
....*....|....
gi 1355713525 243 IFQNPKHPYTKGLL 256
Cdd:cd03296 224 VYDHPASPFVYSFL 237
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-319 |
1.11e-35 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 124.40 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 233 KVIEEAPVLEIFQNPKHPYTKGLLKSKPVMGKRIDKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEICKEEAPNLNVHDEN 312
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 1355713525 313 HKVACWL 319
Cdd:TIGR01727 81 HRVACHL 87
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-234 |
1.69e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.62 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLqtHFQTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSvTALS-IMGLIaesgSVVGGDILYEGKSLLGMKEKEL 85
Cdd:COG4619 2 ELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKS-TLLRaLADLD----PPTSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSlrgnDIAMIFQEPmtslnPVF--TVGEQIVETLREHELLSKNEaykKAIELIRKVGiaRADEIVHSYPHELSGGMLQR 163
Cdd:COG4619 73 RR----QVAYVPQEP-----ALWggTVRDNLPFPFQLRERKFDRE---RALELLERLG--LPPDILDKPVERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-239 |
2.41e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 135.73 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKS-VTALsIMGLIA-ESGSvvggdILYEGKSLlgmKEK 83
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKStLLKL-LLGLYEpTSGR-----ILIDGIDL---RQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGNdIAMIFQEPMtslnpVFTvGeqiveTLREHELLSKNEA-YKKAIELIRKVGIaraDEIVHSYPH-------- 154
Cdd:COG2274 543 DPASLRRQ-IGVVLQDVF-----LFS-G-----TIRENITLGDPDAtDEEIIEAARLAGL---HDFIEALPMgydtvvge 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ---ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLGVVAeMADYVVVMYG 231
Cdd:COG2274 608 ggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG-RT-VIIIAHRLSTIR-LADRIIVLDK 684
|
....*...
gi 1355713525 232 GKVIEEAP 239
Cdd:COG2274 685 GRIVEDGT 692
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-248 |
3.19e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 127.74 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKEl 85
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIAGFETPTSGEILLDGKDITNLPPHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 rslRGndIAMIFQEpmTSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIM 165
Cdd:cd03300 72 ---RP--VNTVFQN--YALFPHLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL---EGYANRKPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQ 245
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
...
gi 1355713525 246 NPK 248
Cdd:cd03300 221 EPA 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-240 |
3.72e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 133.23 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSI-MGLI-AESGSvvggdILYEGksll 78
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKS-TLMKIlYGLYqPDSGE-----ILIDG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 gmKEKELRSLR-----GndIAMIFQEPMtsLNPVFTVGEQIV---ETLREHeLLSKNEAYKKAIELIRKVGIA-RADEIV 149
Cdd:COG3845 67 --KPVRIRSPRdaialG--IGMVHQHFM--LVPNLTVAENIVlglEPTKGG-RLDRKAARARIRELSERYGLDvDPDAKV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 150 hsypHELSGGMLQRIMIAVALSCNPKLLIADEPTTALdvTIQ--AQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVV 227
Cdd:COG3845 140 ----EDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAEGKS-IIFITHKLREVMAIADRVT 212
|
250
....*....|...
gi 1355713525 228 VMYGGKVIEEAPV 240
Cdd:COG3845 213 VLRRGKVVGTVDT 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-243 |
6.29e-35 |
|
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: 127.28 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLI-AESGSvvggdILYEGKSllgmKEKE 84
Cdd:COG4555 3 EVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKT-TLLRMLaGLLkPDSGS-----ILIDGED----VRKE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRgNDIAMIFQEPMtsLNPVFTVGEQIVETLREHELLSKnEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRI 164
Cdd:COG4555 69 PREAR-RQIGVLPDERG--LYDRLTVRENIRYFAELYGLFDE-ELKKRIEELIELLGL---EEFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-238 |
8.40e-35 |
|
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: 132.96 E-value: 8.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGTVkAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSvvggdILYEGKSLLGMKEKE 84
Cdd:COG4988 337 IELEDV--SFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGS-----ILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLrgndIAMIFQEPMtslnpVFTvgeqivETLREHELLSKNEAYKKAI-ELIRKVGiarADEIVHSYPH-------E- 155
Cdd:COG4988 409 WRRQ----IAWVPQNPY-----LFA------GTIRENLRLGRPDASDEELeAALEAAG---LDEFVAALPDgldtplgEg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 ---LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLGVVAEmADYVVVMYGG 232
Cdd:COG4988 471 grgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RT-VILITHRLALLAQ-ADRILVLDDG 547
|
....*.
gi 1355713525 233 KVIEEA 238
Cdd:COG4988 548 RIVEQG 553
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-233 |
8.49e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 124.28 E-value: 8.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKELR 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 slrgNDIAMIFQepmtslnpvftvgeqivetlrehellskneaykkaielirkvgiaradeivhsypheLSGGMLQRIMI 166
Cdd:cd00267 73 ----RRIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 167 AVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-251 |
1.12e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIaesgSVVGGDILYEGKSLLGMKE 82
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKS-TLLRMIaGLE----DPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KElRslrgnDIAMIFQEPmtSLNPVFTVGEQIVETLREHElLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQ 162
Cdd:COG3839 73 KD-R-----NIAMVFQSY--ALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGL---EDLLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 163 RIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLgvvAE---MADYVVVMYGGKVIEEAP 239
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ---VEamtLADRIAVMNDGRIQQVGT 217
|
250
....*....|..
gi 1355713525 240 VLEIFQNPKHPY 251
Cdd:COG3839 218 PEELYDRPANLF 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-248 |
1.23e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGL--IAESGSVVGGDILYEGKSllGMKEKELRSLRGNdIAMIF 97
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLleTPDSGQLNIAGHQFDFSQ--KPSEKAIRLLRQK-VGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 98 QEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVgiaRADEIVHSYPHELSGGMLQRIMIAVALSCNPKLL 177
Cdd:COG4161 89 QQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARL---RLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 178 IADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEMADYVVVMYGGKVIEEAPvLEIFQNPK 248
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-243 |
7.21e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 7.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMgliaeSGSVV--GGDILYEGKSLlg 79
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKS-TLMKIL-----SGVYQpdSGEILLDGEPV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 mkekELRSLR-----GndIAMIFQEPmtSLNPVFTVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIA-RADEIVhs 151
Cdd:COG1129 69 ----RFRSPRdaqaaG--IAIIHQEL--NLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDiDPDTPV-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 152 ypHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:COG1129 139 --GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRD 215
|
250
....*....|..
gi 1355713525 232 GKVIEEAPVLEI 243
Cdd:COG1129 216 GRLVGTGPVAEL 227
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
20-251 |
1.25e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 126.69 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVV--GGDIlyegkSLLGMKEKelrslrgnDIAMI 96
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLeRQTAGTIYqgGRDI-----TRLPPQKR--------DYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 97 FQEpmTSLNPVFTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIARADeivHSYPHELSGGMLQRIMIAVALSCNPKL 176
Cdd:TIGR03265 82 FQS--YALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQQQRVALARALATSPGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 177 LIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPY 251
Cdd:TIGR03265 156 LLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-248 |
1.25e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGL--IAESG--SVVGGDILYEGKSllgmKEKELRSLRgNDIAM 95
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLleMPRSGtlNIAGNHFDFSKTP----SDKAIRELR-RNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 96 IFQEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVgiaRADEIVHSYPHELSGGMLQRIMIAVALSCNPK 175
Cdd:PRK11124 87 VFQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERL---RLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKkefKTSI--LLITHDLGVVAEMADYVVVMYGGKVIEEAPVlEIFQNPK 248
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA---ETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-233 |
2.63e-33 |
|
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: 120.57 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKEL 85
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY----DPTSGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLrgndIAMIFQEPMtslnpVFTvgeqivETLREhellskNeaykkaIelirkvgiaradeivhsypheLSGGMLQRIM 165
Cdd:cd03228 75 RKN----IAYVPQDPF-----LFS------GTIRE------N------I---------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLGVVaEMADYVVVMYGGK 233
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKG-KT-VIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-234 |
3.59e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.87 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFQTEEgtvkAVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGLI-AESGSVvggdilyegkSLLGMKEKE 84
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLkPTSGSI----------RVFGKPLEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLrgndIAMIFQEpmTSLNPVF--TVgEQIVETLREHEL-----LSKnEAYKKAIELIRKVGIAradEIVHSYPHELS 157
Cdd:cd03235 66 ERKR----IGYVPQR--RSIDRDFpiSV-RDVVLMGLYGHKglfrrLSK-ADKAKVDEALERVGLS---ELADRQIGELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-234 |
4.16e-33 |
|
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: 121.59 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKEl 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS----GRIYIGGRDVTDLPPKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 rslrgNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIM 165
Cdd:cd03301 72 -----RDIAMVFQN--YALYPHMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-246 |
2.17e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 122.04 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVVGGDIlyegKSLLGMKE-KELRSLRgNDIAMIFQEP 100
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDY----AIPANLKKiKEVKRLR-KEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 101 MTSLnpvftvgeqIVETLRE-------HELLSKNEAYKKAIELIRKVGIARadEIVHSYPHELSGGMLQRIMIAVALSCN 173
Cdd:PRK13645 100 EYQL---------FQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 174 PKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQN 246
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-249 |
5.55e-32 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 119.11 E-value: 5.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmkekelrSLRGNDIAMIFQEpmTSLNPV 107
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKS----TLLNLISGLAQPTSGGVILEGKQI---------TEPGPDRMVVFQN--YSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 108 FTVGEQI---VETLREHelLSKNEAYKKAIELIRKVGIARAdeiVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTT 184
Cdd:TIGR01184 69 LTVRENIalaVDRVLPD--LSKSERRAIVEEHIALVGLTEA---ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 185 ALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI-FQNPKH 249
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-235 |
6.43e-32 |
|
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: 118.13 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLqtHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmKEKELR 86
Cdd:cd03226 1 RIENI--SFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS----GSILLNGKPI---KAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SlrgnDIAMIFQEPMTSLnpvFTvgeqivETLREHELLSKNEAYK---KAIELIRKVGIARADEiVHsyPHELSGGMLQR 163
Cdd:cd03226 71 K----SIGYVMQDVDYQL---FT------DSVREELLLGLKELDAgneQAETVLKDLDLYALKE-RH--PLSLSGGQKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03226 135 LAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-247 |
1.73e-31 |
|
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: 120.98 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvTAL-SIMGLI-AESGSV-VGGDILYEGKSLLGMKeKELRSlrgndIAMIFQEPmtSL 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKT-TLLrAIAGLErPDSGRIrLGGEVLQDSARGIFLP-PHRRR-----IGYVFQEA--RL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPVFTVGEQIVETLREHELLSKNEAYKKAIELirkVGIAradEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTT 184
Cdd:COG4148 89 FPHLSVRGNLLYGRKRAPRAERRISFDEVVEL---LGIG---HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 185 ALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNP 247
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-243 |
2.09e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.44 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmKEKE 84
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS----GEVLWDGEPL---DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSL------RGndiamifqepmtsLNPVFTVGEQIV--ETLREhelLSKNEAYKKAIELIRKVGIA--RADEIvhsypH 154
Cdd:COG4152 70 RRRIgylpeeRG-------------LYPKMKVGEQLVylARLKG---LSKAEAKRRADEWLERLGLGdrANKKV-----E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIFSSHQMELVEELCDRIVIINKGRK 207
|
....*....
gi 1355713525 235 IEEAPVLEI 243
Cdd:COG4152 208 VLSGSVDEI 216
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-262 |
2.45e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 117.59 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKekelrsLRGNDIAMIFQE 99
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDS----GRIRLNGQDATRVH------ARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmTSLNPVFTVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIAradeivHSYPHELSGGMLQRIMIAVALSCNPKLL 177
Cdd:TIGR00968 81 --YALFKHLTVRDNIAfgLEIRKHPKAKIKARVEELLELVQLEGLG------DRYPNQLSGGQRQRVALARALAVEPQVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 178 IADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLLK 257
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
....*
gi 1355713525 258 SKPVM 262
Cdd:TIGR00968 233 EVNVL 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-259 |
2.72e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSI--MG-LIAESgsVVGGDILYEGKSL 77
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPEV--TITGSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 LGMKEK--ELRslrgNDIAMIFQEPmtslNPV-FTVGEQIVETLREHELLSK---NEAYKKAIelirkVGIARADEI--- 148
Cdd:PRK14239 75 YSPRTDtvDLR----KEIGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKqvlDEAVEKSL-----KGASIWDEVkdr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 149 VHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFktSILLITHDLGVVAEMADYVVV 228
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGF 219
|
250 260 270
....*....|....*....|....*....|.
gi 1355713525 229 MYGGKVIEEAPVLEIFQNPKHPYTKGLLKSK 259
Cdd:PRK14239 220 FLDGDLIEYNDTKQMFMNPKHKETEDYISGK 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-257 |
3.12e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.76 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEgtvkAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLI---AESGSVVGGDILYEGKSL 77
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLekpSEGSIVVNGQTINLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 LGM----KEKELRSLRgNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIvhSYP 153
Cdd:PRK10619 76 DGQlkvaDKNQLRLLR-TRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG--KYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 HELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGK 229
|
250 260
....*....|....*....|....*...
gi 1355713525 234 VIEEAPVLEIFQNPKHP----YTKGLLK 257
Cdd:PRK10619 230 IEEEGAPEQLFGNPQSPrlqqFLKGSLK 257
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-248 |
4.11e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAES-GSVVGGDILYEGKSllgmKEKELRSLRgNDIAMIFQEPM 101
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITITHKT----KDKYIRPVR-KRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TSLnpvFtvgEQIVEtlREHELLSKN------EAYKKAIELIRKVGIARadEIVHSYPHELSGGMLQRIMIAVALSCNPK 175
Cdd:PRK13646 96 SQL---F---EDTVE--REIIFGPKNfkmnldEVKNYAHRLLMDLGFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPK 248
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-255 |
5.69e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 5.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTvkAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGM 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKS----GEIFYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRslrgNDIAMIFQEPMTSLnpvftVGEQI---VETLREHELLSKNEAYKKAIELIRKVG-IARADeivhSYPHEL 156
Cdd:PRK13648 77 NFEKLR----KHIGIVFQNPDNQF-----VGSIVkydVAFGLENHAVPYDEMHRRVSEALKQVDmLERAD----YEPNAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 157 SGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEmADYVVVMYGGKVIE 236
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYK 222
|
250
....*....|....*....
gi 1355713525 237 EAPVLEIFQNPKHPYTKGL 255
Cdd:PRK13648 223 EGTPTEIFDHAEELTRIGL 241
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-269 |
6.20e-31 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 118.26 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESG---SVVGGDILyegksllgmkeKELRSLRgNDIAMI 96
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSgtaRVAGYDVV-----------REPRKVR-RSIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 97 FQEPmtSLNPVFTvGEQIVETLREHELLSKNEAYKKAIELIRKVGIA-RADEIVHSYphelSGGMLQRIMIAVALSCNPK 175
Cdd:TIGR01188 72 PQYA--SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGeAADRPVGTY----SGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIfqnpKHPYTKGL 255
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVT-ILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL----KRRLGKDT 219
|
250
....*....|....
gi 1355713525 256 LKSKPVMGKRIDKL 269
Cdd:TIGR01188 220 LESRPRDIQSLKVE 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-243 |
6.85e-31 |
|
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: 115.93 E-value: 6.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGS--VVGGDILyegksllgmke 82
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRatVAGHDVV----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLRGNdIAMIFQEPmtSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIAR-ADEIVHSYphelSGGML 161
Cdd:cd03265 66 REPREVRRR-IGIVFQDL--SVDDELTGWENLYIHARLYGV-PGAERRERIDELLDFVGLLEaADRLVKTY----SGGMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVL 241
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
..
gi 1355713525 242 EI 243
Cdd:cd03265 218 EL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-239 |
9.34e-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: 9.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLLGMKEK 83
Cdd:COG4987 332 PSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLrgndIAMIFQEPmtslnPVFTvgeqivETLREHELLSKNEAY-KKAIELIRKVGIaraDEIVHSYPH-------E 155
Cdd:COG4987 406 DLRRR----IAVVPQRP-----HLFD------TTLRENLRLARPDATdEELWAALERVGL---GDWLAALPDgldtwlgE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 ----LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLgVVAEMADYVVVMYG 231
Cdd:COG4987 468 ggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RT-VLLITHRL-AGLERMDRILVLED 544
|
....*...
gi 1355713525 232 GKVIEEAP 239
Cdd:COG4987 545 GRIVEQGT 552
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-235 |
1.04e-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: 115.29 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqtEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKEL 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKT----TTLKMLTGELRPTSGTAYINGYSIRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSlrgndIAMIFQEPMtsLNPVFTVgeqiVETLREHELL---SKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQ 162
Cdd:cd03263 75 QS-----LGYCPQFDA--LFDELTV----REHLRFYARLkglPKSEIKEEVELLLRVLGLT---DKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 163 RIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-234 |
1.04e-30 |
|
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: 115.20 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSLRgNDIAMIFQE 99
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmTSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIARADeivHSYPHELSGGMLQRIMIAVALSCNPKLLIA 179
Cdd:cd03292 87 --FRLLPDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGLSHKH---RALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 180 DEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-237 |
1.38e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.43 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIA-----ESGSV-VGG-DIlyegksll 78
Cdd:COG1132 340 IEFENV--SFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLrfydpTSGRIlIDGvDI-------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 gmKEKELRSLRGNdIAMIFQEPMtslnpVFTvgeqivETLREHELLSKNEAYKKaiELIRKVGIARADEIVHSYPH---- 154
Cdd:COG1132 405 --RDLTLESLRRQ-IGVVPQDTF-----LFS------GTIRENIRYGRPDATDE--EVEEAAKAAQAHEFIEALPDgydt 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 -------ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSIlLITHDLGVVAeMADYVV 227
Cdd:COG1132 469 vvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTI-VIAHRLSTIR-NADRIL 545
|
250
....*....|
gi 1355713525 228 VMYGGKVIEE 237
Cdd:COG1132 546 VLDDGRIVEQ 555
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
1.73e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQthFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmK 81
Cdd:PRK13632 4 KSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS----GEIKIDGITI---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLRGNdIAMIFQEPmtslNPVF---TVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSG 158
Cdd:PRK13632 75 KENLKEIRKK-IGIIFQNP----DNQFigaTVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAeMADYVVVMYGGKVIEEA 238
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
....*...
gi 1355713525 239 PVLEIFQN 246
Cdd:PRK13632 225 KPKEILNN 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-257 |
2.76e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.60 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKELRSLRGNDIAMIFQE 99
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR----GQVLIDGVDIAKISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmTSLNPVFTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIA 179
Cdd:PRK10070 115 --FALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 180 DEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLLK 257
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
3.88e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLqtHFQTEEGTVkAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVV--GGDILYEGKSLLGMK 81
Cdd:PRK13639 1 ILETRDL--KYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLikGEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKelrslrgndIAMIFQEPMTSL-NPvfTVgEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVhsyPHELSGGM 160
Cdd:PRK13639 78 KT---------VGIVFQNPDDQLfAP--TV-EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*...
gi 1355713525 241 LEIFQNPK 248
Cdd:PRK13639 222 KEVFSDIE 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-236 |
4.48e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.96 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESGsvvgGDILYEGKSLLGmke 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIaGFLAPSS----GEITLDGVPVTG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 kelrslRGNDIAMIFQEpmTSLNPVFTVGEQIVETLReheL--LSKNEAYKKAIELIRKVGIARADEivhSYPHELSGGM 160
Cdd:COG4525 74 ------PGADRGVVFQK--DALLPWLNVLDNVAFGLR---LrgVPKAERRARAEELLALVGLADFAR---RRIWQLSGGM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDlgvVAE---MADYVVVMYG--GKVI 235
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVMSPgpGRIV 216
|
.
gi 1355713525 236 E 236
Cdd:COG4525 217 E 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-246 |
4.80e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.53 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVVGGDILYEGKSLlgmKEKELRslrgNDIAMIFQEPM 101
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDITDKKV---KLSDIR----KKVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TSLnpvF--TVGEQIVETLREHELlSKNEAYKKAIELIRKVGIARaDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIA 179
Cdd:PRK13637 94 YQL---FeeTIEKDIAFGPINLGL-SEEEIENRVKRAMNIVGLDY-EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 180 DEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQN 246
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-237 |
7.30e-30 |
|
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: 113.79 E-value: 7.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGtVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSllgMKEKEL 85
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVD---IRDLNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNdIAMIFQEPMtslnpVFTVgeqiveTLREHELLSKNEAykKAIELIRKVGIARADEIVHSYPH----------- 154
Cdd:cd03249 73 RWLRSQ-IGLVSQEPV-----LFDG------TIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDgydtlvgergs 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsiLLITHDLGVVAEmADYVVVMYGGKV 234
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIRN-ADLIAVLQNGQV 215
|
...
gi 1355713525 235 IEE 237
Cdd:cd03249 216 VEQ 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-235 |
1.98e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.00 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 34 EGETVCVVGESGCGKSvTALSIM-GLIaesgSVVGGDILYEGKSLLGMKEKELRSLRGNDIAMIFQEpmTSLNPVFTVGE 112
Cdd:cd03297 22 NEEVTGIFGASGAGKS-TLLRCIaGLE----KPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 113 QIVETLREHellSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQA 192
Cdd:cd03297 95 NLAFGLKRK---RNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1355713525 193 QILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-253 |
2.09e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 113.22 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 40 VVGESGCGKSvTALSIMGLIAE---SGSVVGGDILYEGKSLLGMKEKELRslrgNDIAMIFQEPmtSLNPVFTVGEQIVE 116
Cdd:PRK14246 41 IMGPSGSGKS-TLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQP--NPFPHLSIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 117 TLREHELLSKNEAYKKAIELIRKVGIAR-ADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQIL 195
Cdd:PRK14246 114 PLKSHGIKEKREIKKIVEECLRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 196 DLLRQIKKEFktSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTK 253
Cdd:PRK14246 194 KLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-284 |
2.19e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.74 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQthFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-----AESGSVVGGDILYEgK 75
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnPNSKITVDGITLTA-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 76 SLLGMKEKelrslrgndIAMIFQEPMTSLNPVfTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHE 155
Cdd:PRK13640 78 TVWDIREK---------VGIVFQNPDNQFVGA-TVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGML---DYIDSEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGvVAEMADYVVVMYGGKVI 235
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1355713525 236 EEAPVLEIFQNPKHPYTKGLlkSKPVMGKRIDKLYSIPGQVPNLVGLDE 284
Cdd:PRK13640 223 AQGSPVEIFSKVEMLKEIGL--DIPFVYKLKNKLKEKGISVPQEINTEE 269
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-255 |
2.35e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIA-ESGSV-VGGDILYEGKsllgmKEKELRSLRgNDIAMIFQEP 100
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVtIGERVITAGK-----KNKKLKPLR-KKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 101 mtslnpvftvgeqivetlrEHEL-----------------LSKNEAYKKAIELIRKVGIAraDEIVHSYPHELSGGMLQR 163
Cdd:PRK13634 95 -------------------EHQLfeetvekdicfgpmnfgVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
250
....*....|..
gi 1355713525 244 FQNPKHPYTKGL 255
Cdd:PRK13634 234 FADPDELEAIGL 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-222 |
2.92e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.22 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 18 EEGTVKA--VNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEKELRSLRGNDIAM 95
Cdd:PRK11629 16 QEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPTS---GDVIFNGQPMSKLSSAAKAELRNQKLGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 96 IFQepMTSLNPVFTVGEQIVETLreheLLSK---NEAYKKAIELIRKVGIARAdeiVHSYPHELSGGMLQRIMIAVALSC 172
Cdd:PRK11629 92 IYQ--FHHLLPDFTALENVAMPL----LIGKkkpAEINSRALEMLAAVGLEHR---ANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1355713525 173 NPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEM 222
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-239 |
3.18e-29 |
|
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: 111.37 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLLGMKEkELR 86
Cdd:cd03224 2 EVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPP-HER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGndIAMIFQEPMtsLNPVFTVgeqiVETLREHELLSKNEAYKKAIELIRKVgIARADEIVHSYPHELSGGmlQRIMI 166
Cdd:cd03224 73 ARAG--IGYVPEGRR--IFPELTV----EENLLLGAYARRRAKRKARLERVYEL-FPRLKERRKQLAGTLSGG--EQQML 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 167 AV--ALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:cd03224 142 AIarALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-238 |
3.56e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.79 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIA--ESGSvvGGDILYEGKSLLGMKE 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS----TLLAILAglDDGS--SGEVSLVGQPLHQMDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLRGNDIAMIFQEPMtsLNPVFTVGE--QIVETLREHellSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGM 160
Cdd:PRK10584 80 EARAKLRAKHVGFVFQSFM--LIPTLNALEnvELPALLRGE---SSRQSRNGAKALLEQLGLG---KRLDHLPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEmADYVVVMYGGKVIEEA 238
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEEA 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-238 |
1.46e-28 |
|
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: 109.23 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESgsvvGGDILYEGKSLLGMKEKEL 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD----SGEITFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RslrgndIAMIFQEPmtSLNPVFTVGEQIVETLREHELLskneaYKKAIELIRKVGI-ARADEIVHSYphelSGGMLQRI 164
Cdd:cd03268 73 R------IGALIEAP--GFYPNLTARENLRLLARLLGIR-----KKRIDEVLDVVGLkDSAKKKVKGF----SLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGIT-VLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-235 |
1.59e-28 |
|
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: 107.90 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESGsvvgGDILYEGKsllgmkeke 84
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKS-TLMKILsGLYKPDS----GEILVDGK--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 lrslrgndiamifqepmtslnpvftvgeqivetlrEHELLSKNEAYKKAIELIrkvgiaradeivhsypHELSGGMLQRI 164
Cdd:cd03216 63 -----------------------------------EVSFASPRDARRAGIAMV----------------YQLSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-247 |
3.24e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.48 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHF-QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVVGGDI--------LYEG 74
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIQVGDIyigdkknnHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 75 KSLLGMKEKELRSLRgNDIAMIFQEPMTslnpvftvgeQIVETLREHELL--------SKNEAYKKAIELIRKVGIAraD 146
Cdd:PRK13631 101 TNPYSKKIKNFKELR-RRVSMVFQFPEY----------QLFKDTIEKDIMfgpvalgvKKSEAKKLAKFYLNKMGLD--D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 147 EIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYV 226
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLEVADEV 246
|
250 260
....*....|....*....|.
gi 1355713525 227 VVMYGGKVIEEAPVLEIFQNP 247
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-248 |
7.76e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSL-LGMKEKELRSLRgNDIAMIFQEPM 101
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS----GTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TSLnpvFtvgEQIVetLREHELLSKN------EAYKKAIELIRKVGIAraDEIVHSYPHELSGGMLQRIMIAVALSCNPK 175
Cdd:PRK13641 96 AQL---F---ENTV--LKDVEFGPKNfgfsedEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPK 248
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVI-LVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-246 |
8.25e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 8.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFQ-TEEGTVK-AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGksLLG 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE----GKVYVDG--LDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSLRgNDIAMIFQEPMTSLnpVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGG 159
Cdd:PRK13633 75 SDEENLWDIR-NKAGMVFQNPDNQI--VATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMY---EYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEmADYVVVMYGGKVIEEAP 239
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
....*..
gi 1355713525 240 VLEIFQN 246
Cdd:PRK13633 228 PKEIFKE 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-236 |
1.47e-27 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 112.19 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVvGGDILYEGKsllgmkEKELRSLRGND---IAMIFQ 98
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKS-TLMKVLSGVYPHGSY-EGEILFDGE------VCRFKDIRDSEalgIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 EpmTSLNPVFTVGEQIV---ETLReHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPK 175
Cdd:NF040905 86 E--LALIPYLSIAENIFlgnERAK-RGVIDWNETNRRARELLAKVGL---DESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEMADYVVVMYGGKVIE 236
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSI-IISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-257 |
1.50e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFQTEEgtvkavNHVSFSVREGETVCVVGESGCGKSvTALS-IMGLIAESGsvvgGDILYEGKSLLGMkEKEL 85
Cdd:COG3840 3 RLDDLTYRYGDFP------LRFDLTIAAGERVAILGPSGAGKS-TLLNlIAGFLPPDS----GRILWNGQDLTAL-PPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSlrgndIAMIFQEpmTSLNPVFTVGEQIVETLREHelLSKNEAYKKAIE-LIRKVGIAradEIVHSYPHELSGGMLQRI 164
Cdd:COG3840 71 RP-----VSMLFQE--NNLFPHLTVAQNIGLGLRPG--LKLTAEQRAQVEqALERVGLA---GLLDRLPGQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
250
....*....|...
gi 1355713525 245 QNPKHPYTKGLLK 257
Cdd:COG3840 219 DGEPPPALAAYLG 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
1.51e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.01 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEgTVKAVNhvsFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSV-VGGDILYEGKSLLGMKEKE 84
Cdd:PRK14267 5 IETVNLRVYYGSNH-VIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEArVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRgnDIAMIFQEPmtslNPV--FTVGEQIVETLREHELLSKNEAYKKAIELIRKVGiARADEI---VHSYPHELSGG 159
Cdd:PRK14267 81 IEVRR--EVGMVFQYP----NPFphLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKA-ALWDEVkdrLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFktSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
250
....*....|....
gi 1355713525 240 VLEIFQNPKHPYTK 253
Cdd:PRK14267 232 TRKVFENPEHELTE 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-239 |
1.76e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.94 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVvGGDILYEGKSLlgm 80
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKS-TLMKVLSGVYPHGTY-EGEIIFEGEEL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNDIAMIFQEPMtsLNPVFTVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSG 158
Cdd:PRK13549 72 QASNIRDTERAGIAIIHQELA--LVKELSVLENIFlgNEITPGGIMDYDAMYLRAQKLLAQLKL---DINPATPVGNLGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACI-YISHKLNEVKAISDTICVIRDGRHIGTR 225
|
.
gi 1355713525 239 P 239
Cdd:PRK13549 226 P 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-257 |
6.00e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 6.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQtEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDilyeGKSLLGMKEKE 84
Cdd:PRK13642 4 ILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID----GELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRslrgNDIAMIFQEPMTSLnpVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRI 164
Cdd:PRK13642 79 LR----RKIGMVFQNPDNQF--VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML---DFKTREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEmADYVVVMYGGKVIEEAPVLEIF 244
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
250 260
....*....|....*....|.
gi 1355713525 245 QNPKH--------PYTKGLLK 257
Cdd:PRK13642 229 ATSEDmveigldvPFSSNLMK 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-243 |
1.89e-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: 109.12 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHF-QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDIlyeGKSLLGMK 81
Cdd:TIGR03269 277 EPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRV---GDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EK--ELRSLRGNDIAMIFQEpmTSLNPVFTVGEQIVETLREHelLSKNEAYKKAIELIRKVGIA--RADEIVHSYPHELS 157
Cdd:TIGR03269 354 KPgpDGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDeeKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*.
gi 1355713525 238 APVLEI 243
Cdd:TIGR03269 510 GDPEEI 515
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-251 |
2.09e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.12 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSVTALSIMGLI--AESGSVVGGDILYEGKSLLGMKEKELRslrgndIAMIFQEpmTSLN 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrpDEGEIVLNGRTLFDSRKGIFLPPEKRR------IGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 106 PVFTVGEQIVETLREHELLSKNEAYKKAIELIrkvGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTA 185
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELL---GI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 186 LDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPY 251
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-234 |
3.15e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 102.51 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHfqteegtvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKE 82
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR----PPASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLRgndIAMIFQEPM-TSLNPVFTVGEQIveTLREHellskneaykkaielirkvgiaradeivhsypheLSGGML 161
Cdd:cd03215 70 RDAIRAG---IAYVPEDRKrEGLVLDLSVAENI--ALSSL----------------------------------LSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGK-AVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-229 |
5.20e-26 |
|
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: 107.76 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 19 EGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSLrgndIAMIFQ 98
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKS----TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ----IAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 EPmtslnpvftvgeQIVE-TLREHELLSKNEAykKAIELIRKVGIARADEIVHSYP-----------HELSGGMLQRIMI 166
Cdd:TIGR02857 404 HP------------FLFAgTIAENIRLARPDA--SDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 167 AVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLgVVAEMADYVVVM 229
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-248 |
5.30e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.14 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLLGMKeKELR 86
Cdd:COG0410 5 EVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLP-PHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGndIAM------IFqepmTSLnpvfTVgeqivetlREHELLSkneAY-KKAIELIRkvgiARADEIVHSYP--HE-- 155
Cdd:COG0410 76 ARLG--IGYvpegrrIF----PSL----TV--------EENLLLG---AYaRRDRAEVR----ADLERVYELFPrlKErr 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 ------LSGGmlQRIMIAV--ALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVV 227
Cdd:COG0410 131 rqragtLSGG--EQQMLAIgrALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAY 207
|
250 260
....*....|....*....|.
gi 1355713525 228 VMYGGKVIEEAPVLEIFQNPK 248
Cdd:COG0410 208 VLERGRIVLEGTAAELLADPE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-239 |
5.47e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQThfqTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLLGMKE 82
Cdd:COG3845 255 EVVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLRgndIAMIFQEPM-TSLNPVFTVGEQIVetLREHE--------LLSKNEAYKKAIELIRKVGI--ARADEIVHS 151
Cdd:COG3845 328 RERRRLG---VAYIPEDRLgRGLVPDMSVAENLI--LGRYRrppfsrggFLDRKAIRAFAEELIEEFDVrtPGPDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 152 ypheLSGGMLQRIMIAVALSCNPKLLIADEPTTALDV----TIQAQILDLLRQikkefKTSILLITHDLGVVAEMADYVV 227
Cdd:COG3845 403 ----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLELRDA-----GAAVLLISEDLDEILALSDRIA 473
|
250
....*....|..
gi 1355713525 228 VMYGGKVIEEAP 239
Cdd:COG3845 474 VMYEGRIVGEVP 485
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
14-281 |
9.80e-26 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 105.46 E-value: 9.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 14 HFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvVGGDILYEGKSLLGMKEKElrslRGndI 93
Cdd:TIGR03258 10 HLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG--LTGRIAIADRDLTHAPPHK----RG--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 94 AMIFQEpmTSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIARAdeiVHSYPHELSGGMLQRIMIAVALSCN 173
Cdd:TIGR03258 82 ALLFQN--YALFPHLKVEDNVAFGLRAQKM-PKADIAERVADALKLVGLGDA---AAHLPAQLSGGMQQRIAIARAIAIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 174 PKLLIADEPTTALDVTIQAQILDLLRQIKKEF-KTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYT 252
Cdd:TIGR03258 156 PDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFA 235
|
250 260
....*....|....*....|....*....
gi 1355713525 253 KGLLKSKPVMGKRIDKLYSIPGQVPNLVG 281
Cdd:TIGR03258 236 AEFLGAANILPAIALGITEAPGLVDVSCG 264
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
1.24e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLqtHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlGM 80
Cdd:PRK13636 1 MEDYILKVEEL--NYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS----GRILFDGKPI-DY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNdIAMIFQEPMtslNPVFTVG-EQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGG 159
Cdd:PRK13636 73 SRKGLMKLRES-VGMVFQDPD---NQLFSASvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE---HLKDKPTHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*
gi 1355713525 240 VLEIF 244
Cdd:PRK13636 226 PKEVF 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-235 |
1.25e-25 |
|
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: 101.59 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlgmkekel 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS----GEVLFDGKPL-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVGIA-RADEIVHsyphELSGGMLQRI 164
Cdd:cd03269 65 DIAARNRIGYLPEE--RGLYPKMKVIDQLVYLAQLKGL-KKEEARRRIDEWLERLELSeYANKRVE----ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-252 |
1.91e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAE--SGSVVGGDILYEGKSLLGMKEK-ELRslrgNDIAMIFQEPm 101
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKT-TFLRTLNRMNDkvSGYRYSGDVLLGGRSIFNYRDVlEFR----RRVGMLFQRP- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 tslNPV-FTVGEQIVETLREHELLSKNEAYKKAIELIRKVGI--ARADEIVHSyPHELSGGMLQRIMIAVALSCNPKLLI 178
Cdd:PRK14271 111 ---NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdAVKDRLSDS-PFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 179 ADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYT 252
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-239 |
2.13e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKEL 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL----TPTAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 rslrGNDIAMIFQEpmTSLNPVFTVgEQIVETLReHELLSK----NEAYKKAIE-LIRKVGIAR-ADEIVHSypheLSGG 159
Cdd:PRK09536 76 ----SRRVASVPQD--TSLSFEFDV-RQVVEMGR-TPHRSRfdtwTETDRAAVErAMERTGVAQfADRPVTS----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLItHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-245 |
2.14e-25 |
|
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: 101.53 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 12 QTHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESgsvvGGDILYEGKSLLGMKEKELRSLrgn 91
Cdd:cd03254 7 NVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ----KGQILIDGIDIRDISRKSLRSM--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 92 dIAMIFQEPMtslnpVFTvgeqivETLREHELLSKNEAYKKAIELIRKvgIARADEIVHSYP-----------HELSGGM 160
Cdd:cd03254 79 -IGVVLQDTF-----LFS------GTIMENIRLGRPNATDEEVIEAAK--EAGAHDFIMKLPngydtvlgengGNLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSIlLITHDLGVVAEmADYVVVMYGGKVIEEAPV 240
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKG-RTSI-IIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
....*
gi 1355713525 241 LEIFQ 245
Cdd:cd03254 222 DELLA 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-237 |
2.36e-25 |
|
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: 101.29 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLgmkeKEL 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA----GFATVDGFDVV----KEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNdiaMIFQEPMTSLNPVFTVGEQIVETLREHELlsKNEAYKKAIE-LIRKVGIAradEIVHSYPHELSGGMLQRI 164
Cdd:cd03266 74 AEARRR---LGFVSDSTGLYDRLTARENLEYFAGLYGL--KGDELTARLEeLADRLGME---ELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-244 |
5.55e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEEgTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGsvvggDILYEGKSLlgmK 81
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQ-EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESG-----QIIIDGDLL---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLRgNDIAMIFQEPMTSLNPVfTVGEQIVETLrEHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGML 161
Cdd:PRK13650 73 EENVWDIR-HKIGMVFQNPDNQFVGA-TVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQ---DFKEREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAeMADYVVVMYGGKVIEEAPVL 241
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPR 225
|
...
gi 1355713525 242 EIF 244
Cdd:PRK13650 226 ELF 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-239 |
7.15e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.19 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEK 83
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPTS---GTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGNDIAMIFQEpmTSLNPVFTvGEQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQR 163
Cdd:PRK10535 79 ALAQLRREHFGFIFQR--YHLLSHLT-AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLE---DRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEmADYVVVMYGGKVIEEAP 239
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVI-IVTHDPQVAAQ-AERVIEIRDGEIVRNPP 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-245 |
1.88e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.58 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAES-GSVVGGDILYEGKSllgmKEKELRSLRgNDIAMIFQEPM 101
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTeGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TSLnpvftVGEQIVETLR---EHELLSKNEAYKKAIELIRKVGIARadEIVHSYPHELSGGMLQRIMIAVALSCNPKLLI 178
Cdd:PRK13643 95 SQL-----FEETVLKDVAfgpQNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 179 ADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQ 245
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
2.08e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLqtHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVVggdilYEGKSLLGMKEK 83
Cdd:PRK13647 4 IIEVEDL--HFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVK-----VMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGndiaMIFQEPMtslNPVF--TVGEQIVETLREHELlSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGML 161
Cdd:PRK13647 76 WVRSKVG----LVFQDPD---DQVFssTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRM---WDFRDKPPYHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPVl 241
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAEGDK- 222
|
....*..
gi 1355713525 242 EIFQNPK 248
Cdd:PRK13647 223 SLLTDED 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-237 |
3.72e-24 |
|
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: 98.46 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQthFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmKEKEL 85
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDV---RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRgNDIAMIFQEPMtslnpVFTvgeqivETLREHELLSKNEAYKKAIEliRKVGIARADEIVHSYPH----------- 154
Cdd:cd03251 72 ASLR-RQIGLVSQDVF-----LFN------DTVAENIAYGRPGATREEVE--EAARAANAHEFIMELPEgydtvigergv 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSIlLITHDLGVVaEMADYVVVMYGGKV 234
Cdd:cd03251 138 KLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTF-VIAHRLSTI-ENADRIVVLEDGKI 214
|
...
gi 1355713525 235 IEE 237
Cdd:cd03251 215 VER 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-236 |
4.96e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMK 81
Cdd:PRK11160 335 DQVSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSlrgndiAMifqepmtslnpvfTVGEQIVE----TLREHELLSKNEAY-KKAIELIRKVGIAR---ADEIVHSYP 153
Cdd:PRK11160 409 EAALRQ------AI-------------SVVSQRVHlfsaTLRDNLLLAAPNASdEALIEVLQQVGLEKlleDDKGLNAWL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 HE----LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLGVVAEMaDYVVVM 229
Cdd:PRK11160 470 GEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-KT-VLMITHRLTGLEQF-DRICVM 546
|
....*..
gi 1355713525 230 YGGKVIE 236
Cdd:PRK11160 547 DNGQIIE 553
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-237 |
9.08e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHfqteegtvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLlgmkekE 84
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPV------R 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLR---GNDIAMIfqeP----MTSLNPVFTVGEQIV----ETLREHELLSKNEAYKKAIELIRKVGI--ARADEIVHS 151
Cdd:COG1129 318 IRSPRdaiRAGIAYV---PedrkGEGLVLDLSIRENITlaslDRLSRGGLLDRRRERALAEEYIKRLRIktPSPEQPVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 152 ypheLSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:COG1129 395 ----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
....*.
gi 1355713525 232 GKVIEE 237
Cdd:COG1129 470 GRIVGE 475
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
235-299 |
9.93e-24 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 92.08 E-value: 9.93e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 235 IEEAPVLEIFQNPKHPYTKGLLKSKPVMGKRIDKLYSIPGQVPNLVGLDEFCYFSGRCEHCMEIC 299
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-248 |
1.10e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.41 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGm 80
Cdd:PRK11432 2 TQKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLVAGLEKPTEGQIFIDGEDVTH- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 kekelRSLRGNDIAMIFQEpmTSLNPVFTVGEQIVETLREHELlSKNEA---YKKAIELIRKVGIAradeivHSYPHELS 157
Cdd:PRK11432 73 -----RSIQQRDICMVFQS--YALFPHMSLGENVGYGLKMLGV-PKEERkqrVKEALELVDLAGFE------DRYVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
250
....*....|.
gi 1355713525 238 APVLEIFQNPK 248
Cdd:PRK11432 219 GSPQELYRQPA 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-247 |
1.17e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.95 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLqTHfqTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKE 84
Cdd:PRK13652 3 LIETRDL-CY--SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS----GSVLIRGEPITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGndiaMIFQEPmtslnpvftvGEQIVETLREHEL--------LSKNEAYKKAIELIRKVGIaraDEIVHSYPHEL 156
Cdd:PRK13652 76 VRKFVG----LVFQNP----------DDQIFSPTVEQDIafgpinlgLDEETVAHRVSSALHMLGL---EELRDRVPHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 157 SGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIE 236
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
250
....*....|.
gi 1355713525 237 EAPVLEIFQNP 247
Cdd:PRK13652 219 YGTVEEIFLQP 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-245 |
1.25e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVVGGDILYEGKSllgmKEKELRSLRgNDIAMIFQEPM 101
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSVRVDDTLITSTS----KNKDIKQIR-KKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TSLnpvftVGEQIVETLR---EHELLSKNEAYKKAIELIRKVGIAraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLI 178
Cdd:PRK13649 96 SQL-----FEETVLKDVAfgpQNFGVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 179 ADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQ 245
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-237 |
3.38e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLqtHFQTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLiaESGSVVGGDILYEGKSLLGMKEKElR 86
Cdd:COG0396 2 EIKNL--HVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSILLDGEDILELSPDE-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGndIAMIFQEPM------------TSLNPVftvgeqivetlREhELLSKNEAYKKAIELIRKVGIarADEIVHSYPH 154
Cdd:COG0396 75 ARAG--IFLAFQYPVeipgvsvsnflrTALNAR-----------RG-EELSAREFLKLLKEKMKELGL--DEDFLDRYVN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 E-LSGGMLQRIMIAVALSCNPKLLIADEPTTALDV-TIQAqILDLLRQIKKEfKTSILLITH-----DLGVvaemADYVV 227
Cdd:COG0396 139 EgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVH 212
|
250
....*....|
gi 1355713525 228 VMYGGKVIEE 237
Cdd:COG0396 213 VLVDGRIVKS 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-237 |
5.02e-23 |
|
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: 95.37 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGtVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmKEKEL 85
Cdd:cd03253 1 IEFENV--TFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDI---REVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNdIAMIFQEpmtslNPVF--TVGEQIvetlrehellskneAYKKA----IELIRKVGIARADEIVHSYPH----- 154
Cdd:cd03253 71 DSLRRA-IGVVPQD-----TVLFndTIGYNI--------------RYGRPdatdEEVIEAAKAAQIHDKIMRFPDgydti 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ------ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSIlLITHDLGVVAEmADYVVV 228
Cdd:cd03253 131 vgerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTTI-VIAHRLSTIVN-ADKIIV 207
|
....*....
gi 1355713525 229 MYGGKVIEE 237
Cdd:cd03253 208 LKDGRIVER 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-235 |
5.65e-23 |
|
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: 95.03 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaESGSVVGGDILYEGKSllgMKEKE 84
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSGQILFNGQP---RKPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRS----LRGNDIamifqepmtsLNPVFTVGEQIVET--LREHELlsKNEAYKK---AIELIRKVGIARadeIVHSYPHE 155
Cdd:cd03234 79 FQKcvayVRQDDI----------LLPGLTVRETLTYTaiLRLPRK--SSDAIRKkrvEDVLLRDLALTR---IGGNLVKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03234 144 ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-256 |
6.19e-23 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 96.79 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 40 VVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLgMKEKELRSlrgndIAMIFQEpmTSLNPVFTVGEQIVETLR 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS----GSIMLDGEDVT-NVPPHLRH-----INMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 120 EHELlSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLR 199
Cdd:TIGR01187 69 MRKV-PRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 200 QIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLL 256
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
27-215 |
9.43e-23 |
|
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: 93.70 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 27 HVSFSVREGETVCVVGESGCGKSvTAL-SIMGLIaesgSVVGGDILYEGKSLlgmkeKELRSLRGNDIAMIFQEPMtsLN 105
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKT-TLLrILAGLL----PPSAGEVLWNGEPI-----RDAREDYRRRLAYLGHADG--LK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 106 PVFTVGEQivetLREHELLSKNEAYKKAI-ELIRKVGIARADeivHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTT 184
Cdd:COG4133 88 PELTVREN----LRFWAALYGLRADREAIdEALEAVGLAGLA---DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|.
gi 1355713525 185 ALDVTIQAQILDLLRQiKKEFKTSILLITHD 215
Cdd:COG4133 161 ALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-246 |
1.11e-22 |
|
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: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 8 LKDLqthFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIA-ESGSV-VGGDILYEgksllgmKEKE 84
Cdd:COG4586 24 LKGL---FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLtGILVpTSGEVrVLGYVPFK-------RRKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSlrgnDIAMIF-QEpmTSLN---PVftvgeqiVETLReheLLSK-----NEAYKKAI-ELIRKVGIaraDEIVHSYPH 154
Cdd:COG4586 93 FAR----RIGVVFgQR--SQLWwdlPA-------IDSFR---LLKAiyripDAEYKKRLdELVELLDL---GELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGmlQRiM---IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:COG4586 154 QLSLG--QR-MrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
250
....*....|....*
gi 1355713525 232 GKVIEEAPVLEIFQN 246
Cdd:COG4586 231 GRIIYDGSLEELKER 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-229 |
1.12e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 94.04 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHF---QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLI-----AESGSVV----GGDIl 71
Cdd:COG4778 3 TLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIygnylPDSGSILvrhdGGWV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 72 yegkSLLGMKEKELRSLRGNDIAMIFQepmtSLNPVFTVG-EQIV-ETLREHELlSKNEAYKKAIELIRKVGIARadEIV 149
Cdd:COG4778 78 ----DLAQASPREILALRRRTIGYVSQ----FLRVIPRVSaLDVVaEPLLERGV-DREEARARARELLARLNLPE--RLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 150 HSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVM 229
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-238 |
1.20e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLiaESGSvvGGDILYEGKSLLGMKEKELRslrgndIAMIFQE 99
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL--EHQT--SGHIRFHGTDVSRLHARDRK------VGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmTSLNPVFTVGEQI---VETLREHELLSKNEAYKKAIELIRKVGIARadeIVHSYPHELSGGMLQRIMIAVALSCNPKL 176
Cdd:PRK10851 83 --YALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAH---LADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 177 LIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKvIEEA 238
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQA 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-236 |
1.28e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.11 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKekeLRSLRGNdIAMIFQE 99
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPQS---GRILIDGTDIRTVT---RASLRRN-IAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 PMtslnpVF--TVGEQIV---ETLREHELLSKNEAyKKAIELIRKvGIARADEIVHSYPHELSGGMLQRIMIAVALSCNP 174
Cdd:PRK13657 418 AG-----LFnrSIEDNIRvgrPDATDEEMRAAAER-AQAHDFIER-KPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 175 KLLIADEPTTALDVTIQAQI---LDLLRQIKKEFktsilLITHDLGVVAEmADYVVVMYGGKVIE 236
Cdd:PRK13657 491 PILILDEATSALDVETEAKVkaaLDELMKGRTTF-----IIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-239 |
1.76e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.38 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 13 THFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGmkekelrslRGND 92
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGSITLDGKPVEG---------PGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 93 IAMIFQEpmTSLNPVFTVGEQIVETLrehEL--LSKNEAYKKAIELIRKVGIARADeivHSYPHELSGGMLQRIMIAVAL 170
Cdd:PRK11248 72 RGVVFQN--EGLLPWRNVQDNVAFGL---QLagVEKMQRLEIAHQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 171 SCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMY--GGKVIEEAP 239
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLP 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-248 |
1.83e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.15 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTV-KAVNHVSFSVREGETVCVVGESGCGKS-----VTALsimgLIAESGSVVggdILYEGKSLL- 78
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNAL----LLPDTGTIE---WIFKDEKNKk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 --GMKEKELRSL-----RGNDIAMIfQEPMTSLNPVFTVGE-QIVETLREHELL--------SKNEAYKKAIELIRKVGI 142
Cdd:PRK13651 76 ktKEKEKVLEKLviqktRFKKIKKI-KEIRRRVGVVFQFAEyQLFEQTIEKDIIfgpvsmgvSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 143 AraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEM 222
Cdd:PRK13651 155 D--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEW 231
|
250 260
....*....|....*....|....*.
gi 1355713525 223 ADYVVVMYGGKVIEEAPVLEIFQNPK 248
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-258 |
4.81e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKElrslrgNDIAMIFQEpmTS 103
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMFQS--YA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVFTVGEQIVETLREHELlSKNEAYKKAIELIrkvGIARADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKL-PKAEIASRVNEML---GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 184 TALDVTI----QAQILDLLRQIkkefKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPKHPYTKGLLKS 258
Cdd:PRK11607 178 GALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-252 |
1.56e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.86 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGM 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGFETPDSGRIMLDGQDITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KeKELRslrgnDIAMIFQEpmTSLNPVFTVGEQIVETLREHELlSKNEAYKKAIELIRKVgiaRADEIVHSYPHELSGGM 160
Cdd:PRK09452 82 P-AENR-----HVNTVFQS--YALFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMV---QLEEFAQRKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
250
....*....|..
gi 1355713525 241 LEIFQNPKHPYT 252
Cdd:PRK09452 230 REIYEEPKNLFV 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-235 |
2.55e-21 |
|
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: 90.34 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEgtVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVvggdiLYEGkslLGMKEKE 84
Cdd:cd03245 3 IEFRNVSFSYPNQE--IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSV-----LLDG---TDIRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSLRGNdIAMIFQEPMTslnpvftvgeqIVETLREHELLSKNEAykKAIELIRKVGIARADEIVHSYPH---------- 154
Cdd:cd03245 73 PADLRRN-IGYVPQDVTL-----------FYGTLRDNITLGAPLA--DDERILRAAELAGVTDFVNKHPNgldlqigerg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 -ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLGVVaEMADYVVVMYGGK 233
Cdd:cd03245 139 rGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KT-LIIITHRPSLL-DLVDRIIVMDSGR 215
|
..
gi 1355713525 234 VI 235
Cdd:cd03245 216 IV 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-239 |
5.36e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.22 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSLRgndiAMIFQEpmTSL 104
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR----AVLPQH--SSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPVFTVgEQIVETLREHELLSKneayKKAIELIRKVgIARADeIVH----SYPhELSGGMLQRIMIAVAL------SCNP 174
Cdd:PRK13548 88 SFPFTV-EEVVAMGRAPHGLSR----AEDDALVAAA-LAQVD-LAHlagrDYP-QLSGGEQQRVQLARVLaqlwepDGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 175 KLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-247 |
5.45e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGm 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG----GTILLRGQHIEG- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 kekelrsLRGNDIAM-----------IFQEpMTSLNPVFTVGEQIVETLREHELL-------SKNEAYKKAIELIRKVGI 142
Cdd:PRK11300 72 -------LPGHQIARmgvvrtfqhvrLFRE-MTVIENLLVAQHQQLKTGLFSGLLktpafrrAESEALDRAATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 143 AradEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEM 222
Cdd:PRK11300 144 L---EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGI 220
|
250 260
....*....|....*....|....*
gi 1355713525 223 ADYVVVMYGGKVIEEAPVLEIFQNP 247
Cdd:PRK11300 221 SDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-237 |
1.09e-20 |
|
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: 89.08 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVV--GGDILYEGKSLLG------MKEKEL--RSLRGNd 92
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLvdGHDLALADPAWLRrqvgvvLQENVLfnRSIRDN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 93 IAMifQEPMTSLnpvftvgEQIVETLR---EHELLSK-NEAYkkaielirkvgiaraDEIVHSYPHELSGGMLQRIMIAV 168
Cdd:cd03252 96 IAL--ADPGMSM-------ERVIEAAKlagAHDFISElPEGY---------------DTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 169 ALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVaEMADYVVVMYGGKVIEE 237
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQ 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-247 |
1.24e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.06 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQthfQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGLiaESgsVVGGDILYEGKSLLGMKE 82
Cdd:PRK11650 2 AGLKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKS-TLLrMVAGL--ER--ITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KElrslRgnDIAMIFQEpmTSLNPVFTVGEQIVETLrehellsKNEAYKKAiELIRKVG-IARADEI---VHSYPHELSG 158
Cdd:PRK11650 74 AD----R--DIAMVFQN--YALYPHMSVRENMAYGL-------KIRGMPKA-EIEERVAeAARILELeplLDRKPRELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLgvVAEM--ADYVVVMYGGkVIE 236
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ--VEAMtlADRVVVMNGG-VAE 214
|
250
....*....|...
gi 1355713525 237 E--APvLEIFQNP 247
Cdd:PRK11650 215 QigTP-VEVYEKP 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-244 |
1.83e-20 |
|
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: 88.60 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGliAESGSVVGGDIlyegkSLLGmKEK------ELRSLRG--- 90
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKS-TLLSLIT--GDLPPTYGNDV-----RLFG-ERRggedvwELRKRIGlvs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 91 NDIAMIFQEPMTSLNPVFTVGEQIVETLREHEllskNEAYKKAIELIRKVGIA-RADeivHSYpHELSGGMLQRIMIAVA 169
Cdd:COG1119 85 PALQLRFPRDETVLDVVLSGFFDSIGLYREPT----DEQRERARELLELLGLAhLAD---RPF-GTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 170 LSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-248 |
1.94e-20 |
|
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: 87.98 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVV--GGDIlyegkSLLGMKEkelRSLRGndIAMI 96
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILldGQDI-----TKLPMHK---RARLG--IGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 97 FQEPmtSLNPVFTVGEQIVETLREHElLSKNEAYKKAIELIRKVGIARadeIVHSYPHELSGGMLQRIMIAVALSCNPKL 176
Cdd:cd03218 81 PQEA--SIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITH---LRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 177 LIADEPTTALD----VTIQAQILDLlrqikKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNPK 248
Cdd:cd03218 155 LLLDEPFAGVDpiavQDIQKIIKIL-----KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-234 |
3.59e-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: 87.53 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKE 82
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLrgndIAMIFQEPMTSLNpvfTVGEQIVETLREHELLSKNEAYKKAielirkvgiaRADEIVHSYPHE------- 155
Cdd:cd03248 84 KYLHSK----VSLVGQEPVLFAR---SLQDNIAYGLQSCSFECVKEAAQKA----------HAHSFISELASGydtevge 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 ----LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVaEMADYVVVMYG 231
Cdd:cd03248 147 kgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTV-ERADQILVLDG 223
|
...
gi 1355713525 232 GKV 234
Cdd:cd03248 224 GRI 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-253 |
3.94e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.17 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAV--VELKDLQTHFQTEegtvKAVNHVSFSVREGETVCVVGESGCGKS--VTALSIMGLIaESGSVVGGDILYEGKS 76
Cdd:PRK14258 1 MSKLIpaIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNEL-ESEVRVEGRVEFFNQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 77 LLgMKEKELRSLRgNDIAMIFQEP----MTSLNPVfTVGEQIVETLREHELLSKNEAYKKAIELirkvgiarADEI---V 149
Cdd:PRK14258 76 IY-ERRVNLNRLR-RQVSMVHPKPnlfpMSVYDNV-AYGVKIVGWRPKLEIDDIVESALKDADL--------WDEIkhkI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 150 HSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVM 229
Cdd:PRK14258 145 HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFF 224
|
250 260
....*....|....*....|....*....
gi 1355713525 230 YG-----GKVIEEAPVLEIFQNPKHPYTK 253
Cdd:PRK14258 225 KGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-258 |
3.97e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVT--ALSIMgLIAESGSvvggdILYEGKSLLGMKEKELrslrGNDIAMIF 97
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLlkCFARL-LTPQSGT-----VFLGDKPISMLSSRQL----ARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 98 QEPMTslnPVFTVGEQIVETLREHEL-----LSKNEAYK--KAIElirKVGIaraDEIVHSYPHELSGGMLQRIMIAVAL 170
Cdd:PRK11231 83 QHHLT---PEGITVRELVAYGRSPWLslwgrLSAEDNARvnQAME---QTRI---NHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 171 SCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLItHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFqnpkhp 250
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL-HDLNQASRYCDHLVVLANGHVMAQGTPEEVM------ 226
|
....*...
gi 1355713525 251 yTKGLLKS 258
Cdd:PRK11231 227 -TPGLLRT 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-215 |
4.41e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.77 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVVGGDILYEGKSLLGMKeKELRSlrgndIAMIFQEPMtsL 104
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIAGTLSPAFSASGEVLLNGRRLTALP-AEQRR-----IGILFQDDL--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPVFTVGEQIVETLREHelLSKNEAYKKAIELIRKVGIA-RADeivhSYPHELSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:COG4136 88 FPHLSVGENLAFALPPT--IGRAQRRARVEQALEEAGLAgFAD----RDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|..
gi 1355713525 184 TALDVTIQAQILDLLRQIKKEFKTSILLITHD 215
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-236 |
4.98e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFQTEEgtVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmK 81
Cdd:PRK11176 338 AKGDIEFRNVTFTYPGKE--VPALRNINFKIPAGKTVALVGRSGSGKS----TIANLLTRFYDIDEGEILLDGHDL---R 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLRgNDIAMIFQEPMtslnpVF--TVGEQIVetlrehelLSKNEAYKKAiELIRKVGIARADEIVHSYPH----- 154
Cdd:PRK11176 409 DYTLASLR-NQVALVSQNVH-----LFndTIANNIA--------YARTEQYSRE-QIEEAARMAYAMDFINKMDNgldtv 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ------ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSiLLITHDLGVVaEMADYVVV 228
Cdd:PRK11176 474 igengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTS-LVIAHRLSTI-EKADEILV 550
|
....*...
gi 1355713525 229 MYGGKVIE 236
Cdd:PRK11176 551 VEDGEIVE 558
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-244 |
5.41e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDIlyegkSLLGMKEKelRSLRGNDIAMIFQ-EPMT 102
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKI-----SILGQPTR--QALQKNLVAYVPQsEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 103 SLNPVFTvgEQIVETLREHEL--LSKNEAYKKAIElirKVGIARAD--EIVHSYPHELSGGMLQRIMIAVALSCNPKLLI 178
Cdd:PRK15056 91 WSFPVLV--EDVVMMGRYGHMgwLRRAKKRDRQIV---TAALARVDmvEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 179 ADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYvVVMYGGKVIEEAPVLEIF 244
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKT-MLVSTHNLGSVTEFCDY-TVMVKGTVLASGPTETTF 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-243 |
6.41e-20 |
|
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: 90.25 E-value: 6.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL--------------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 59 -IAESGSVVGGDILYEGKSLLGMKEKELRSLRgNDIAMIFQEPMtSLNPVFTVGEQIVETLREHELLSKnEAYKKAIELI 137
Cdd:TIGR03269 77 kVGEPCPVCGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEALEEIGYEGK-EAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 138 RKVGIARadEIVHsYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLG 217
Cdd:TIGR03269 154 EMVQLSH--RITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 1355713525 218 VVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-234 |
7.17e-20 |
|
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: 84.96 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 15 FQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKELRslrgndia 94
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL----RPTSGRVRLDGADISQWDPNELG-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 95 mifqepmtslnpvftvgeQIVETL-REHELLSKneaykkAIelirkvgiarADEIvhsypheLSGGMLQRIMIAVALSCN 173
Cdd:cd03246 76 ------------------DHVGYLpQDDELFSG------SI----------AENI-------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 174 PKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAeMADYVVVMYGGKV 234
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRI-VIAHRPETLA-SADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-216 |
7.41e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.11 E-value: 7.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqteEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKEL 85
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLrgndIAMIFQEPMtslnpVFTVgeqiveTLREHELLSKNEAYKKAI-ELIRKVGIAR--------ADEIVHSYPHEL 156
Cdd:TIGR02868 408 RRR----VSVCAQDAH-----LFDT------TVRENLRLARPDATDEELwAALERVGLADwlralpdgLDTVLGEGGARL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 157 SGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfkTSILLITHDL 216
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-234 |
8.43e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 8 LKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESGsvvgGDILyEGKSLLGmkekELR 86
Cdd:PRK11247 15 LNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLaGLETPSA----GELL-AGTAPLA----EAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 slrgNDIAMIFQEpmTSLNPVFTVGEQIVETLREHellskneAYKKAIELIRKVGIA-RADEivhsYPHELSGGMLQRIM 165
Cdd:PRK11247 81 ----EDTRLMFQD--ARLLPWKKVIDNVGLGLKGQ-------WRDAALQALAAVGLAdRANE----WPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-235 |
1.10e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.68 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqtEEGTV---KAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKE 82
Cdd:COG1101 2 LELKNLSKTF--NPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKS----TLLNAIAGSLPPDSGSILIDGKDVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KElrslRGNDIAMIFQEPMTSLNPVFTVGEQIVETLREHE-------LLSKN-EAYKKAIELIR---------KVGIara 145
Cdd:COG1101 76 YK----RAKYIGRVFQDPMMGTAPSMTIEENLALAYRRGKrrglrrgLTKKRrELFRELLATLGlglenrldtKVGL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 146 deivhsypheLSGGmlQR-----IMiavALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVA 220
Cdd:COG1101 149 ----------LSGG--QRqalslLM---ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAL 213
|
250
....*....|....*
gi 1355713525 221 EMADYVVVMYGGKVI 235
Cdd:COG1101 214 DYGNRLIMMHEGRII 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-235 |
1.20e-19 |
|
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: 86.23 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 11 LQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSV-VGGDILYEGKsllgmkeKELRSl 88
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVrVAGLVPWKRR-------KKFLR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 89 rgnDIAMIFQE---------PMTSLNpvftvgeqiveTLREHELLSKNEAYKKAIELIRKVGIARadeIVHSYPHELSGG 159
Cdd:cd03267 95 ---RIGVVFGQktqlwwdlpVIDSFY-----------LLAAIYDLPPARFKKRLDELSELLDLEE---LLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-247 |
1.26e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 29 SFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmKEKELRSLRgNDIAMIFQEPMtslnpVF 108
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLH-RQVALVGQEPV-----LF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 109 --TVGEQIVETLREHELLSKNEAYKKAielirkvgiaRADEIVHSYPH-----------ELSGGMLQRIMIAVALSCNPK 175
Cdd:TIGR00958 568 sgSVRENIAYGLTDTPDEEIMAAAKAA----------NAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 176 LLIADEPTTALDVTIQAqildLLRQIKKEFKTSILLITHDLGVVaEMADYVVVMYGGKVIEEAPVLEIFQNP 247
Cdd:TIGR00958 638 VLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-240 |
1.46e-19 |
|
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: 84.89 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 7 ELKDLqtHFQTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLiaESGSVVGGDILYEGKSLLGMkEKELR 86
Cdd:cd03217 2 EIKDL--HVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDL-PPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGndIAMIFQEPMTslnpvftvgeqiVETLrehellskneaykKAIELIRKVGIAradeivhsypheLSGGMLQRIMI 166
Cdd:cd03217 75 ARLG--IFLAFQYPPE------------IPGV-------------KNADFLRYVNEG------------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 167 AVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHdLGVVAEM--ADYVVVMYGGKVIEEAPV 240
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-235 |
1.73e-19 |
|
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: 85.24 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 27 HVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKElrslrgNDIAMIFQEpmTSLNP 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS----TLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQE--NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 107 VFTVGEQIveTLREHELLSKNEAYKKAIELI-RKVGIAradEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTA 185
Cdd:cd03298 84 HLTVEQNV--GLGLSPGLKLTAEDRQAIEVAlARVGLA---GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1355713525 186 LDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-234 |
2.35e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 27 HVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsVVGGDILYEGKSLLGMKEK-----------ELR--------- 86
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRP----ARGGRIMLNGKEINALSTAqrlarglvylpEDRqssglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGNDIAMIFQEPMTSLNPVftvgeqivetlREHELLsknEAYKKAIelirkvGI--ARADEIVHSypheLSGGMLQRI 164
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPA-----------RENAVL---ERYRRAL------NIkfNHAEQAART----LSGGNQQKV 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
23-237 |
2.53e-19 |
|
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: 84.55 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVcVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMKEKeLRSLrgndIAMIFQEPMT 102
Cdd:cd03264 14 RALDGVSLTLGPGMYG-LLGPNGAGKT-TLMRILATLTPPSS---GTIRIDGQDVLKQPQK-LRRR----IGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 103 SlnPVFTVGEQI--VETLREhelLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIAD 180
Cdd:cd03264 84 Y--PNFTVREFLdyIAWLKG---IPSKEVKARVDEVLELVNLG---DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 181 EPTTALDVTIQAQILDLLRQIKKEfkTSILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-245 |
3.73e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 16 QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMG--LIAESGSV-VGGDIlyegKSLLGMkekelrslrgnd 92
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIAgiLEPTSGRVeVNGRV----SALLEL------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 93 iamifqepMTSLNPVFTVGEQIVetlreheL------LSKNEaykkaielIRkvgiARADEI-------------VHSYp 153
Cdd:COG1134 96 --------GAGFHPELTGRENIY-------LngrllgLSRKE--------ID----EKFDEIvefaelgdfidqpVKTY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 helSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|..
gi 1355713525 234 VIEEAPVLEIFQ 245
Cdd:COG1134 224 LVMDGDPEEVIA 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-235 |
4.72e-19 |
|
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: 87.57 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVvGGDILYEGKSLlgmKEKELRSLRGNDIAMIFQE 99
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKS-TLMKILSGVYPHGTW-DGEIYWSGSPL---KASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 PMtsLNPVFTVGEQIV---ETLREHELLSKNEAYKKAIELIRKVgiaRADEIVHSYP-HELSGGMLQRIMIAVALSCNPK 175
Cdd:TIGR02633 87 LT--LVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLREL---QLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-239 |
9.55e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 9.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 27 HVSFSVREGETVCVVGESGCGKSvTALSIMG--LIAESGSVvggdilyegksllgmkekelrSLRGND----------IA 94
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKS-TLLNLIAgfLTPASGSL---------------------TLNGQDhtttppsrrpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 95 MIFQEpmTSLNPVFTVGEQIveTLREHELLSKNEAYKKAIELI-RKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCN 173
Cdd:PRK10771 75 MLFQE--NNLFSHLTVAQNI--GLGLNPGLKLNAAQREKLHAIaRQMGI---EDLLARLPGQLSGGQRQRVALARCLVRE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 174 PKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-235 |
1.71e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESGSvvggdILYEGKSLLGMKEKELRSLRgndiAMIFQEPMTSLN- 105
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGE-----ILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 106 PVFtvgeqivETLREHelLSKNEAYKKAIELIRKvgIARADEIVHSYP---HELSGGMLQRIMIAVAL-----SCNP--K 175
Cdd:COG4138 85 PVF-------QYLALH--QPAGASSEAVEQLLAQ--LAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPegQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIkKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-249 |
2.94e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.95 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKS----VTALSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSLRgndiAMIFQEP 100
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKStllkALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 101 mtslNPVFTVgeqiveTLREHELLSKNEAYKKAIELIRKVG--------IARADEIVHSYPHELSGGMLQRIMIAVALS- 171
Cdd:PRK13547 93 ----QPAFAF------SAREIVLLGRYPHARRAGALTHRDGeiawqalaLAGATALVGRDVTTLSGGELARVQFARVLAq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 172 --------CNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:PRK13547 163 lwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
....*.
gi 1355713525 244 FQnPKH 249
Cdd:PRK13547 243 LT-PAH 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-237 |
3.01e-18 |
|
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: 80.82 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMkEKEL 85
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPVSDL-EKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLrgndIAMIFQEPMtslnpVFTVgeqiveTLREHellskneaykkaielirkVGIaradeivhsyphELSGGMLQRIM 165
Cdd:cd03247 74 SSL----ISVLNQRPY-----LFDT------TLRNN------------------LGR------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTsILLITHDLGVVAEMaDYVVVMYGGKVIEE 237
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KT-LIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-248 |
3.53e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVV--GGDIlyegkSLLGMKEkelRSLRGndIAMIFQE 99
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGRIFldGEDI-----THLPMHK---RARLG--IGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 PmtSlnpVF---TVGEQIVETLREHELlSKNEAYKKAIELIRKVGIARadeIVHSYPHELSGGMLQRIMIAVALSCNPKL 176
Cdd:COG1137 87 A--S---IFrklTVEDNILAVLELRKL-SKKEREERLEELLEEFGITH---LRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 177 LIADEPTTALD---VT-IQAQILDLlrqikKEFKTSIlLIT-HD----LGVVaemaDYVVVMYGGKVIEEAPVLEIFQNP 247
Cdd:COG1137 158 ILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGV-LITdHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 1355713525 248 K 248
Cdd:COG1137 228 L 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-234 |
4.01e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKELRSLRgNDIAMIFQE 99
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA----GKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmtslnpvftvgeqivetlreHELLSKNEAYKK-AIELI----------RKVGIArADEI-----VHSYPHELSGGMLQR 163
Cdd:PRK10908 88 ---------------------HHLLMDRTVYDNvAIPLIiagasgddirRRVSAA-LDKVglldkAKNFPIQLSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKeFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-235 |
4.13e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 26 NHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVVGGDILYEGKSLlGMKEKELRSlrgndiAMIFQEPMtsLN 105
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKT-TLMNALAFRSPKGVKGSGSVLLNGMPI-DAKEMRAIS------AYVQQDDL--FI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 106 PVFTVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIARADEIVHSYPHE---LSGGMLQRIMIAVALSCNPKLLIAD 180
Cdd:TIGR00955 112 PTLTVREHLMfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 181 EPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-245 |
6.39e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 20 GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMG-LIAESGsvvgGDILYEGKSLLGMKEKEL-RSLrgndiAMIF 97
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPDS----GEVLVDGLDVATTPSRELaKRL-----AILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 98 QEPmtSLNPVFTVgEQIVE-----------TLREHELLskNEAykkaielirkvgIARAD--EIVHSYPHELSGGMLQRI 164
Cdd:COG4604 82 QEN--HINSRLTV-RELVAfgrfpyskgrlTAEDREII--DEA------------IAYLDleDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
.
gi 1355713525 245 Q 245
Cdd:COG4604 225 T 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-247 |
8.53e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvTALSIMG--LIAESGsvvggDILYEGKSLLGMKEKELRSLRgNDIAMIFQEP--MTS 103
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKT-TLLRLIGgqIAPDHG-----EILFDGENIPAMSRSRLYTVR-KRMSMLFQSGalFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNpVFtvgEQIVETLREHELLSKNEAYKKAIELIRKVGIARADEIVhsyPHELSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:PRK11831 99 MN-VF---DNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 184 TALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQNP 247
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-237 |
9.27e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 80.65 E-value: 9.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 9 KDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-GLIA-ESGSVvggdilyegksllgmkekelr 86
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS-TLLRLLaGIYPpDSGTV--------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 87 SLRGNDIAMIfqEPMTSLNPVFTVGEQIVETLREHElLSKNEAYKKAIELIRKVGI-ARADEIVHSYphelSGGMLQRIM 165
Cdd:cd03220 80 TVRGRVSSLL--GLGGGFNPELTGRENIYLNGRLLG-LSRKEIDEKIDEIIEFSELgDFIDLPVKTY----SSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 166 IAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLiTHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILV-SHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-236 |
1.49e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.36 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvtalSIMGLIAesgsvvgGDILYEGkSLL--GMkekELRSL-----RGNdIAMIFQEP 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKT----SLLNALL-------GFLPYQG-SLKinGI---ELRELdpeswRKH-LSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 101 mtslnpvftvgeQIVE-TLREHELLSKNEAYKKAIE-LIRKvgiARADEIVHSYPH-----------ELSGGMLQRIMIA 167
Cdd:PRK11174 433 ------------QLPHgTLRDNVLLGNPDASDEQLQqALEN---AWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 168 VALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVAEMaDYVVVMYGGKVIE 236
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-236 |
1.67e-17 |
|
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: 79.85 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqtEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKEL 85
Cdd:cd03244 3 IEFKNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV----ELSSGSILIDGVDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLrgndIAMIFQEPMtslnpVFTvGeqiveTLREHeLLSKNEAYKKAI-ELIRKVGIARA--------DEIVHSYPHEL 156
Cdd:cd03244 77 RSR----ISIIPQDPV-----LFS-G-----TIRSN-LDPFGEYSDEELwQALERVGLKEFveslpgglDTVVEEGGENL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 157 SGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQikkEFK-TSILLITHDLGVVAEMaDYVVVMYGGKVI 235
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFKdCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
.
gi 1355713525 236 E 236
Cdd:cd03244 217 E 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-262 |
1.89e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSllgMKEK 83
Cdd:PRK11000 2 ASVTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGDLFIGEKR---MNDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ElRSLRGndIAMIFQEpmTSLNPVFTVGEQIVETLRehelLS---KNEAYKKAIELIRkvgIARADEIVHSYPHELSGGM 160
Cdd:PRK11000 71 P-PAERG--VGMVFQS--YALYPHLSVAENMSFGLK----LAgakKEEINQRVNQVAE---VLQLAHLLDRKPKALSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:PRK11000 139 RQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
250 260
....*....|....*....|..
gi 1355713525 241 LEIFQNPKHPYTKGLLKSkPVM 262
Cdd:PRK11000 219 LELYHYPANRFVAGFIGS-PKM 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-215 |
3.59e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLqtHFQTeeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSImglIAESGSVVGGDILYEGKSLLGMK 81
Cdd:PRK10247 4 NSPLLQLQNV--GYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKS-TLLKI---VASLISPTSGTLLFEGEDISTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRslrgNDIAMIFQEPMtslnpVFtvGEQIVETLREHELLSKNEAYKKAIelirKVGIAR---ADEIVHSYPHELSG 158
Cdd:PRK10247 76 PEIYR----QQVSYCAQTPT-----LF--GDTVYDNLIFPWQIRNQQPDPAIF----LDDLERfalPDTILTKNIAELSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHD 215
Cdd:PRK10247 141 GEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-244 |
6.64e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDIlyegkSLLGM 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA----GKI-----TVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNDIAMIFQepMTSLNPVFTVGEQIVETLREHELLSKN-EAYKKAIelirkVGIARADEIVHSYPHELSGG 159
Cdd:PRK13536 104 PVPARARLARARIGVVPQ--FDNLDLEFTVRENLLVFGRYFGMSTREiEAVIPSL-----LEFARLESKADARVSDLSGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEA- 238
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGRKIAEGr 255
|
250
....*....|....*..
gi 1355713525 239 -----------PVLEIF 244
Cdd:PRK13536 256 phalidehigcQVIEIY 272
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-247 |
1.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESgsvvGGDILYEGKSLLGM-KEKELRSLRGndiaMIFQEPMT 102
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ----KGKVLVSGIDTGDFsKLQGIRKLVG----IVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 103 SLnpvftVGEQIVETLR---EHELLSKNEAYKKAIELIRKVGIARADeivHSYPHELSGGMLQRIMIAVALSCNPKLLIA 179
Cdd:PRK13644 89 QF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEKYR---HRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 180 DEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVaEMADYVVVMYGGKVIEEAPVLEIFQNP 247
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
1.23e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIA-ESGSVvggdilyegkSLLG 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSI----------SLCG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSLRGNDIAMIFQepMTSLNPVFTVGEQIVETLReHELLSKNEAYKKAIELIRkvgIARADEIVHSYPHELSGG 159
Cdd:PRK13537 69 EPVPSRARHARQRVGVVPQ--FDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLE---FAKLENKADAKVGELSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGG-KVIEEA 238
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGrKIAEGA 221
|
.
gi 1355713525 239 P 239
Cdd:PRK13537 222 P 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-235 |
1.23e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvTALSIM-GLIAESGSvvggdILYEGKSLLGMKEKELRSLRGndiAMIFQEPMTSLNP 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARMaGLLPGSGS-----IQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 107 VFtvgeQIVeTLREHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVAL-----SCNP--KLLIA 179
Cdd:PRK03695 86 VF----QYL-TLHQPDKTRTEAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 180 DEPTTALDVTIQAqildLLRQIKKEFKT---SILLITHDLGVVAEMADYVVVMYGGKVI 235
Cdd:PRK03695 158 DEPMNSLDVAQQA----ALDRLLSELCQqgiAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-235 |
1.50e-16 |
|
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: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSvTALSI-MGLIAESGsvVGGDILYEGKSLlgmKEKELRSLrgndIAMIFQEPMts 103
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKS-TLLNAlAGRRTGLG--VSGEVLINGRPL---DKRSFRKI----IGYVPQDDI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVFTVgeqiVETLREHELLSKneaykkaielirkvgiaradeivhsypheLSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:cd03213 93 LHPTLTV----RETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 184 TALDVTIQAQILDLLRQIKKEFKTsILLITHDL-GVVAEMADYVVVMYGGKVI 235
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRT-IICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-236 |
1.62e-16 |
|
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: 76.68 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEegTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSvvggdILYEGKSLLGMKEKE 84
Cdd:cd03369 7 IEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGK-----IEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSlrgnDIAMIFQEPM-------TSLNPV--FTvGEQIVETLRehellskneaykkaielirkvgiaradeiVHSYPHE 155
Cdd:cd03369 80 LRS----SLTIIPQDPTlfsgtirSNLDPFdeYS-DEEIYGALR-----------------------------VSEGGLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQIldlLRQIKKEFK-TSILLITHDLGVVAEMaDYVVVMYGGKV 234
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI---QKTIREEFTnSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
..
gi 1355713525 235 IE 236
Cdd:cd03369 202 KE 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-244 |
2.78e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 40 VVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlGMKEKELRSLRgNDIAMIFQEPMTSLnpVFT-VGEQIVETL 118
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQK----GAVLWQGKPL-DYSKRGLLALR-QQVATVFQDPEQQI--FYTdIDSDIAFSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 119 REhelLSKNEAykkaiELIRKVGIARADEIVHSYPHE----LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQI 194
Cdd:PRK13638 104 RN---LGVPEA-----EITRRVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1355713525 195 LDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIF 244
Cdd:PRK13638 176 IAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-235 |
2.88e-16 |
|
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: 76.15 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 12 QTHFQTEEGTVKA--VNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVvGGDILYEGKSLLGMKEKELRslr 89
Cdd:cd03233 8 NISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV-EGDIHYNGIPYKEFAEKYPG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 90 gnDIAMIFQEpmTSLNPVFTVGEqivetlrehellskneaykkaieLIRKVGIARADEIVHSypheLSGGMLQRIMIAVA 169
Cdd:cd03233 84 --EIIYVSEE--DVHFPTLTVRE-----------------------TLDFALRCKGNEFVRG----ISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 170 LSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVA-EMADYVVVMYGGKVI 235
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQI 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-253 |
2.95e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 11 LQTHFQTEE-----GTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMG----LIaeSGSVVGGDILYEGKSLLG-- 79
Cdd:PRK14243 7 TETVLRTENlnvyyGSFLAVKNVWLDIPKNQITAFIGPSGCGKS-TILRCFNrlndLI--PGFRVEGKVTFHGKNLYApd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 MKEKELRSlrgnDIAMIFQEPmtslNPVftvGEQIVEtlrehellskNEAYKKAI--------ELIRKvGIARA---DEI 148
Cdd:PRK14243 84 VDPVEVRR----RIGMVFQKP----NPF---PKSIYD----------NIAYGARIngykgdmdELVER-SLRQAalwDEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 149 ---VHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFktSILLITHDLGVVAEMADY 225
Cdd:PRK14243 142 kdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 1355713525 226 V------VVMYGGKV---IEEAPVLEIFQNPKHPYTK 253
Cdd:PRK14243 220 TaffnveLTEGGGRYgylVEFDRTEKIFNSPQQQATR 256
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-229 |
3.10e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIA-ESGSVVGGdilyegksllgmkekelrslRGNDIAMIFQEpmT 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRA--------------------GGARVAYVPQR--S 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 103 SLNPVF--TVgEQIVE--TLREHELLSKNEAYKKAI--ELIRKVGIAradEIVHSYPHELSGGMLQRIMIAVALSCNPKL 176
Cdd:NF040873 65 EVPDSLplTV-RDLVAmgRWARRGLWRRLTRDDRAAvdDALERVGLA---DLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 177 LIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEmADYVVVM 229
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-237 |
4.03e-16 |
|
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: 79.09 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 26 NHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLlgmKEKELRSLRGnDIAMIFQEpmTSL- 104
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY----DVTSGRILIDGQDI---RDVTQASLRA-AIGIVPQD--TVLf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NpvftvgeqivETLREhellskNEAYKKA----IELIRKVGIARADEIVHSYPH-----------ELSGGMLQRIMIAVA 169
Cdd:COG5265 445 N----------DTIAY------NIAYGRPdaseEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 170 LSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSiLLITHDLGVVAEmADYVVVMYGGKVIEE 237
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTT-LVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-237 |
6.44e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 78.63 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKELRSLrgndIAMIFQEPmt 102
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS----GEILLNGFSLKDIDRHTLRQF----INYLPQEP-- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 103 slnpvFTVGEQIVETLreheLLSKNEAYKKAiELIRKVGIARADEIVHSYPH-----------ELSGGMLQRIMIAVALS 171
Cdd:TIGR01193 558 -----YIFSGSILENL----LLGAKENVSQD-EIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 172 CNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTsILLITHDLGvVAEMADYVVVMYGGKVIEE 237
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KT-IIFVAHRLS-VAKQSDKIIVLDHGKIIEQ 689
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-215 |
1.00e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 26 NHVSFSVREGETVCVVGESGCGKSvTALSIM-GLI-AESGSVVggdilyegksllgmKEKELRslrgndIAMIFQEPmtS 103
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKS-TLLKILaGELePDSGEVS--------------IPKGLR------IGYLPQEP--P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVFTVGEQIVETLRE--------HELLSKNEAYKKAIELIRKVGI-----------ARADEIVH-----SYPH----- 154
Cdd:COG0488 72 LDDDLTVLDTVLDGDAElraleaelEELEAKLAEPDEDLERLAELQEefealggweaeARAEEILSglgfpEEDLdrpvs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV-TIQaqildLLRQIKKEFKTSILLITHD 215
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-247 |
1.49e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 16 QTEEGTVKAVNHVSFSVrEGET-------------VC-VVGESGCGKSvTALSIMGliaESGSVVGGDILYEGKSLLGMK 81
Cdd:PRK10575 5 TNHSDTTFALRNVSFRV-PGRTllhplsltfpagkVTgLIGHNGSGKS-TLLKMLG---RHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELrslrGNDIAMIFQ-----EPMTSlnpvftvgEQIVETLRE--HELLSK--NEAYKKAIELIRKVGIAR-ADEIVHS 151
Cdd:PRK10575 80 SKAF----ARKVAYLPQqlpaaEGMTV--------RELVAIGRYpwHGALGRfgAADREKVEEAISLVGLKPlAHRLVDS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 152 ypheLSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:PRK10575 148 ----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
250
....*....|....*.
gi 1355713525 232 GKVIEEAPVLEIFQNP 247
Cdd:PRK10575 224 GEMIAQGTPAELMRGE 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-231 |
1.56e-15 |
|
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: 77.13 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 33 REGETVCVVGESGCGKSvTALSIMgliaeSGSVvggdilyegKSLLGMKEKE------LRSLRGNDIAMIFQ-----EPM 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKS-TALKIL-----SGEL---------KPNLGDYDEEpswdevLKRFRGTELQDYFKklangEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TSLNPvftvgeQIVETLREH------ELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPK 175
Cdd:COG1245 162 VAHKP------QYVDLIPKVfkgtvrELLEKVDERGKLDELAEKLGL---ENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYG 231
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDLAILDYLADYVHILYG 287
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
3.08e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGM 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKelRSLRgNDIAMIFQEpmtslNPVFTvGEQIVETLREHELLSKNEAYKKAIELIRKVgIARADEIVHSYPHELSGGM 160
Cdd:PRK11614 73 QTA--KIMR-EAVAIVPEG-----RRVFS-RMTVEENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEE 237
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-234 |
3.18e-15 |
|
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: 76.33 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVV--GGDI--------------------LYEGksllgmk 81
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWpPTAGSVRldGADLsqwdreelgrhigylpqdveLFDG------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 ekelrSLRGNdIAMiFQEPmtslNPvftvgEQIVETLRE---HEL-LSKNEAYkkaielirkvgiaraDEIVHSYPHELS 157
Cdd:COG4618 421 -----TIAEN-IAR-FGDA----DP-----EKVVAAAKLagvHEMiLRLPDGY---------------DTRIGEGGARLS 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 158 GGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEmADYVVVMYGGKV 234
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRV 544
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-237 |
3.71e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETV--------------CVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKELRslr 89
Cdd:PRK10790 342 DIDNVSFAYRDDNLVlqninlsvpsrgfvALVGHTGSGKSTLASLLMGYY----PLTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 90 gNDIAMIFQEPMTSLNPVF---TVGEQIVEtlrehellsknEAYKKAIELIRKVGIARA-DEIVHSYPHE----LSGGML 161
Cdd:PRK10790 415 -QGVAMVQQDPVVLADTFLanvTLGRDISE-----------EQVWQALETVQLAELARSlPDGLYTPLGEqgnnLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVAEmADYVVVMYGGKVIEE 237
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
152-247 |
4.67e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 152 YPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:PRK11144 125 YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
90
....*....|....*.
gi 1355713525 232 GKVIEEAPVLEIFQNP 247
Cdd:PRK11144 205 GKVKAFGPLEEVWASS 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-233 |
5.82e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.69 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 16 QTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaeSGSVVGGDILYEGKSLLGMKEKELRSLRGNDIam 95
Cdd:PLN03211 77 QIQERTI--LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI--QGNNFTGTILANNRKPTKQILKRTGFVTQDDI-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 96 ifqepmtsLNPVFTVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIARADEIV--HSYPHELSGGMLQRIMIAVALS 171
Cdd:PLN03211 151 --------LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEML 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 172 CNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-243 |
8.06e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGM 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM----TPAHGHVWLDGEHIQHY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELrslrGNDIAMIFQEPMTSLNpvFTVGEQIVETLREHELL------SKNEAYKKAIeliRKVGIAR-ADEIVHSyp 153
Cdd:PRK10253 75 ASKEV----ARRIGLLAQNATTPGD--ITVQELVARGRYPHQPLftrwrkEDEEAVTKAM---QATGITHlADQSVDT-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 heLSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGK 233
Cdd:PRK10253 144 --LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
250
....*....|
gi 1355713525 234 VIEEAPVLEI 243
Cdd:PRK10253 222 IVAQGAPKEI 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-243 |
2.22e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGK--SLLGMKEKELRSlrgndIAMIFQE 99
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKS----TMMKVLTGIYTRDAGSILYLGKevTFNGPKSSQEAG-----IGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 100 pmtsLN--PVFTVGEQIV---ETLREHELLSKNEAYKKAIELIRKVGIARADeivHSYPHELSGGMLQRIMIAVALSCNP 174
Cdd:PRK10762 88 ----LNliPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSS---DKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 175 KLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEI 243
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-246 |
4.01e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 27 HVSFSVREGETVCVVGESGCGKSvTALSIMG---------------LI----------AESGSVVggDILYEGKSLLGMK 81
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKS-TLMKILNgevllddgriiyeqdLIvarlqqdpprNVEGTVY--DFVAEGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLrGNDIAmifQEPMTS-LNPVFTVGEQIvetlrEHELLSKNEAykKAIELIRKVGIArADEIVHsyphELSGGM 160
Cdd:PRK11147 98 LKRYHDI-SHLVE---TDPSEKnLNELAKLQEQL-----DHHNLWQLEN--RINEVLAQLGLD-PDAALS----SLSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 161 LQRIMIAVALSCNPKLLIADEPTTALDV-TIqaqilDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKVI---- 235
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIeTI-----EWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVsypg 236
|
250 260
....*....|....*....|
gi 1355713525 236 ---------EEAPVLEIFQN 246
Cdd:PRK11147 237 nydqyllekEEALRVEELQN 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-238 |
5.02e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSL--------------------------L 78
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALPRTSGYVTLDGHEVvtrspqdglangivyisedrkrdglvL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 79 GMKEKELRSLrgndiamifqepmTSLNPVFTVGEQIvetlrehellsKNEAYKKAIE-LIRKVGIA--RADEIVHsyphE 155
Cdd:PRK10762 344 GMSVKENMSL-------------TALRYFSRAGGSL-----------KHADEQQAVSdFIRLFNIKtpSMEQAIG----L 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKV- 234
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIs 474
|
....*...
gi 1355713525 235 ----IEEA 238
Cdd:PRK10762 475 geftREQA 482
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-246 |
6.32e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIA-ESGSVVGGDilyEGKSLLGMKEkelRSLRGndIAMIFQEPm 101
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDD---EDISLLPLHA---RARRG--IGYLPQEA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 tSLNPVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGIAradEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADE 181
Cdd:PRK10895 88 -SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE---HLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 182 PTTALDvtiQAQILDLLRQIK--KEFKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQN 246
Cdd:PRK10895 164 PFAGVD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-227 |
7.23e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKE 84
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE----GVIKRNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LrslrgndiamifqepmtSLNPVFTVgeqiveTLREHELLSKNEAYKKAIELIRKVgiaRADEIVHSYPHELSGGMLQRI 164
Cdd:PRK09544 76 L-----------------YLDTTLPL------TVNRFLRLRPGTKKEDILPALKRV---QAGHLIDAPMQKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVV 227
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-231 |
7.85e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 32 VREGETVCVVGESGCGKSvTALSIMgliaeSGSVVG--GDilYEGKsllGMKEKELRSLRGNDIAMIFQ-----EPMTSL 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKT-TAVKIL-----SGELIPnlGD--YEEE---PSWDEVLKRFRGTELQNYFKklyngEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 NPvftvgeQIVETLREH------ELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLI 178
Cdd:PRK13409 165 KP------QYVDLIPKVfkgkvrELLKKVDERGKLDEVVERLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 179 ADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAYG 286
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-232 |
8.08e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGM 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPTK---GTITINNINYNKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLrgnDIAMIFQE-----PMTSLNPVFtVGEQIVETLREHELLSKNEAYKKAIELIRKVGIARA-DEIVHsyph 154
Cdd:PRK09700 73 DHKLAAQL---GIGIIYQElsvidELTVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDlDEKVA---- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYGG 232
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-214 |
9.35e-14 |
|
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: 67.95 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQthFQTEEGTVKaVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDIlyegksllgmkekel 85
Cdd:cd03223 1 IELENLS--LATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKS----SLFRALAGLWPWGSGRI--------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGNDIAMIFQEPMtslnpvFTVGeqiveTLREhellskneaykkaiELIrkvgiaradeivhsYP--HELSGGMLQR 163
Cdd:cd03223 59 GMPEGEDLLFLPQRPY------LPLG-----TLRE--------------QLI--------------YPwdDVLSGGEQQR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 164 IMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLrqikKEFKTSILLITH 214
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-234 |
9.73e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGliAESGSvvggdilYEGKSLLGMKEKELRSLR---GNDIAMIFQ 98
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGK-------FEGNVFINGKPVDIRNPAqaiRAGIAMVPE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 E-PMTSLNPVFTVGEQIveTLREHELLSKNEAYKKAIEL-IRKVGIARAdEIVHSYPH----ELSGGMLQRIMIAVALSC 172
Cdd:TIGR02633 344 DrKRHGIVPILGVGKNI--TLSVLKSFCFKMRIDAAAELqIIGSAIQRL-KVKTASPFlpigRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 173 NPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-236 |
1.17e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 1 MSKAVVELKDLQTHFQTEEgTVKAVNhvsFSVREGETVCVVGESGCGKSVTALSIMGliAESGSVVGGDILYEGKSLLGM 80
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE-ILKGLN---LSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 kEKELRSLRGndIAMIFQepmtslNPVFTVGEQIVETLRehelLSKNEAYKKA----------IELIR-KVGIARADEI- 148
Cdd:CHL00131 77 -EPEERAHLG--IFLAFQ------YPIEIPGVSNADFLR----LAYNSKRKFQglpeldplefLEIINeKLKLVGMDPSf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 149 VHSYPHE-LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVtiqaqilDLLRQIKKEFKT------SILLITHD---LGV 218
Cdd:CHL00131 144 LSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDI-------DALKIIAEGINKlmtsenSIILITHYqrlLDY 216
|
250
....*....|....*...
gi 1355713525 219 VaeMADYVVVMYGGKVIE 236
Cdd:CHL00131 217 I--KPDYVHVMQNGKIIK 232
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-234 |
1.87e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 70.84 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIA-ESGSVV--GGDIL-----YEGKSLlGMKEKELRSLRGN---DI 93
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPpTSGSVRldGADLKqwdreTFGKHI-GYLPQDVELFPGTvaeNI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 94 AMiFQEPMTSlnpvftvgEQIVETLR---EHEL-LSKNEAYKKAIelirkvGIARADeivhsypheLSGGMLQRIMIAVA 169
Cdd:TIGR01842 413 AR-FGENADP--------EKIIEAAKlagVHELiLRLPDGYDTVI------GPGGAT---------LSGGQRQRIALARA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 170 LSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVaEMADYVVVMYGGKV 234
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGRI 531
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-237 |
2.94e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEGTVK--AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLI---AESGSV-VGGDILYEGKSLLg 79
Cdd:COG2401 25 ERVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgtPVAGCVdVPDNQFGREASLI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 mkekelrslrgndiamifqepmtslnpvftvgeqivetlrehELLSKNEAYKKAIELIRKVGIARADEIVHSYpHELSGG 159
Cdd:COG2401 104 ------------------------------------------DAIGRKGDFKDAVELLNAVGLSDAVLWLRRF-KELSTG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 160 MLQRIMIAVALSCNPKLLIADEPTTALDVTiQAQILDL-LRQIKKEFKTSILLITHDLGVVAEMADYVVVM--YGGKVIE 236
Cdd:COG2401 141 QKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPEE 219
|
.
gi 1355713525 237 E 237
Cdd:COG2401 220 K 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-219 |
3.40e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQTEEgTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSllGMKEKEL 85
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIINDSH--NLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRgNDIAMIFQEPMT--------------SLNPVFTVGEQ----------------------------IVETLREHEL 123
Cdd:PTZ00265 456 KWWR-SKIGVVSQDPLLfsnsiknnikyslySLKDLEALSNYynedgndsqenknkrnscrakcagdlndMSNTTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 124 LSKNEAYK-----KAIELIRKVGIA--------RADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTI 190
Cdd:PTZ00265 535 IEMRKNYQtikdsEVVDVSKKVLIHdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260
....*....|....*....|....*....
gi 1355713525 191 QAQILDLLRQIKKEFKTSILLITHDLGVV 219
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
6.02e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEegtvKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAeSGSVVGGDILYEGKSLL--GM 80
Cdd:PRK09984 2 QTIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT-GDKSAGSHIELLGRTVQreGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 KEKELRSLRGNdIAMIFQEpmTSLNPVFTVGEQIV-----------ETLREHELLSKNEAYKKaielIRKVGIAradEIV 149
Cdd:PRK09984 77 LARDIRKSRAN-TGYIFQQ--FNLVNRLSVLENVLigalgstpfwrTCFSWFTREQKQRALQA----LTRVGMV---HFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 150 HSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVM 229
Cdd:PRK09984 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
....*
gi 1355713525 230 YGGKV 234
Cdd:PRK09984 227 RQGHV 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-234 |
1.33e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGliAESGSvvggdilYEGKSLLGMKEKELRSLR---GNDIAMIFQ 98
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGR-------WEGEIFIDGKPVKIRNPQqaiAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 E-PMTSLNPVFTVGEQIveTLREHELLSKNEAYKKAIEL--IR------KVGIARADEIVHSypheLSGGMLQRIMIAVA 169
Cdd:PRK13549 346 DrKRDGIVPVMGVGKNI--TLAALDRFTGGSRIDDAAELktILesiqrlKVKTASPELAIAR----LSGGNQQKAVLAKC 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 170 LSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-248 |
2.32e-12 |
|
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: 65.85 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 31 SVREGETVCVVGESGCGKSvTALSIMgliaeSGSVvggdilyegKSLLGMKEKE------LRSLRGNDIAMIFQEPMT-S 103
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKS-TALKIL-----AGKL---------KPNLGKFDDPpdwdeiLDEFRGSELQNYFTKLLEgD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVftVGEQIVETL------REHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLL 177
Cdd:cd03236 87 VKVI--VKPQYVDLIpkavkgKVGELLKKKDERGKLDELVDQLEL---RHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 178 IADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYGgkvieEAPVLEIFQNPK 248
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYG-----EPGAYGVVTLPK 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-214 |
2.49e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQthFQTEEGTVKaVNHVSFSVREGETVCVVGESGCGKSvTAL-SIMGL-IAESGSVV---GGDILYegksL--- 77
Cdd:COG4178 363 LALEDLT--LRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKS-TLLrAIAGLwPYGSGRIArpaGARVLF----Lpqr 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 ----LGmkekelrSLRGndiAMIFQEPMTSLNPvftvgEQIVETLRehellskneaykkaielirKVG----IARADEiV 149
Cdd:COG4178 435 pylpLG-------TLRE---ALLYPATAEAFSD-----AELREALE-------------------AVGlghlAERLDE-E 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 150 HSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfkTSILLITH 214
Cdd:COG4178 480 ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG--TTVISVGH 542
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-247 |
2.55e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 14 HFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSlrgnDI 93
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS----RL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 94 AMIFQEPMtslnpVF--TVGEQIVetlrehelLSKNEAYKKAIELIRKVGIARAD--EIVHSYPHE-------LSGGMLQ 162
Cdd:PRK10789 392 AVVSQTPF-----LFsdTVANNIA--------LGRPDATQQEIEHVARLASVHDDilRLPQGYDTEvgergvmLSGGQKQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 163 RIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKefKTSILLITHDLGVVAEmADYVVVMYGGKVIEEAPVLE 242
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQ 535
|
....*
gi 1355713525 243 IFQNP 247
Cdd:PRK10789 536 LAQQS 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-233 |
4.08e-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: 64.41 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 16 QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMG-LIAESGSV-VGGDILYegksllgmkekelrslrgndi 93
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVsVPGSIAY--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 94 amIFQEP--MTslnpvftvgeqivETLREHELLSK---NEAYKKAIE---LIRKVGI-ARAD--EIvhsypHE----LSG 158
Cdd:cd03250 71 --VSQEPwiQN-------------GTIRENILFGKpfdEERYEKVIKacaLEPDLEIlPDGDltEI-----GEkginLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILD-LLRQIKKEFKTsILLITHDLGVVAEmADYVVVMYGGK 233
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
142-215 |
6.24e-12 |
|
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: 62.47 E-value: 6.24e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 142 IARADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLrqikKEFKTSILLITHD 215
Cdd:cd03221 57 VTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHD 126
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-237 |
7.26e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHfqteegTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgMKE 82
Cdd:PRK09700 263 ETVFEVRNVTSR------DRKKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKDI--SPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 83 KELRSLRgNDIAMIFQEPM-TSLNPVFTVGEQ--IVETLrehellsKNEAYKKAIELIRKVGIARADE-----------I 148
Cdd:PRK09700 331 SPLDAVK-KGMAYITESRRdNGFFPNFSIAQNmaISRSL-------KDGGYKGAMGLFHEVDEQRTAEnqrellalkchS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 149 VHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVV 228
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAV 481
|
....*....
gi 1355713525 229 MYGGKVIEE 237
Cdd:PRK09700 482 FCEGRLTQI 490
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-236 |
1.09e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGliaesgsvvGGDILYEGKSLLGMKEKELRSLR---GNDIAMIFQ 98
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKS-TLLKILS---------GNYQPDAGSILIDGQEMRFASTTaalAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 EpmTSLNPVFTVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIaradEIVHSYP-HELSGGMLQRIMIAVALSCNPK 175
Cdd:PRK11288 87 E--LHLVPEMTVAENLYlgQLPHKGGIVNRRLLNYEAREQLEHLGV----DIDPDTPlKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIE 236
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-283 |
1.19e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.76 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSimgliaesGSVVGGDIlyegksllGMK 81
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP--------AHV*GPDA--------GRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLRGNDIAMifqepmtslnpVFTVG-EQIVETLREHELLSKNEAYK--KAIELIRKVGIARADEIVHSYP----- 153
Cdd:NF000106 70 PWRF*TWCANRRAL-----------RRTIG*HRPVR*GRRESFSGRENLYMigR*LDLSRKDARARADELLERFSlteaa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 ----HELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVM 229
Cdd:NF000106 139 graaAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVI 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 230 YGGKVIEEAPVLEIfqnpKHPYTKGLLKSKPVMGKRIDKLYSIPGQvpnlVGLD 283
Cdd:NF000106 218 DRGRVIADGKVDEL----KTKVGGRTLQIRPAHAAELDRMVGAIAQ----AGLD 263
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-228 |
2.75e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLQTHFQTEEgTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIM-------------------------- 56
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRP-NVPIYKDLTFSCDSKKTTAIVGETGSGKS-TVMSLLmrfydlkndhhivfknehtndmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 57 -----------------------GLIAESGSVV--GGDILYEGKSLLGMKEKELRSLrgndIAMIFQEPMtslnpVFTVg 111
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeGGSGEDSTVFknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPM-----LFNM- 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 112 eQIVETLRehelLSKNEAYKKAIEliRKVGIARADEIVHSYPHE-----------LSGGMLQRIMIAVALSCNPKLLIAD 180
Cdd:PTZ00265 1311 -SIYENIK----FGKEDATREDVK--RACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLD 1383
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1355713525 181 EPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVaEMADYVVV 228
Cdd:PTZ00265 1384 EATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVV 1430
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-236 |
2.90e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALS-IMGLIA-ESGSVVGG------------DI 70
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-TLLKlLAGELEpDSGTVKLGetvkigyfdqhqEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 71 LYEGKSLL--------GMKEKELRSLRGNdiamifqepmtslnpvFtvgeqivetlreheLLSKNEAYKKAielirkvgi 142
Cdd:COG0488 390 LDPDKTVLdelrdgapGGTEQEVRGYLGR----------------F--------------LFSGDDAFKPV--------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 143 aradeivhsypHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV-TIQAqILDLLrqikKEFKTSILLITHDLGVVAE 221
Cdd:COG0488 431 -----------GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEAL----DDFPGTVLLVSHDRYFLDR 494
|
250
....*....|....*
gi 1355713525 222 MADYVVVMYGGKVIE 236
Cdd:COG0488 495 VATRILEFEDGGVRE 509
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-232 |
3.15e-10 |
|
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: 59.27 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKELRSLRGNDIAMIFQEPM 101
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 TsLNPvfTVGEQIVetlreHELLSKNEAYKKAIEL------IRKVGIARADEIVHSYPHeLSGGMLQRIMIAVALSCNPK 175
Cdd:cd03290 90 L-LNA--TVEENIT-----FGSPFNKQRYKAVTDAcslqpdIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 176 LLIADEPTTALDV-----TIQAQILDLLRQIKKefktSILLITHDLGVVAEmADYVVVMYGG 232
Cdd:cd03290 161 IVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-234 |
4.77e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESgsvvGGDILYEGKSLLGMKEKELRSLrgnDIAMIFQEPM 101
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD----SGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 tsLNPVFTVGEQIVETLREHEllsknEAYKKAIELIRKVGiaradeiVHSYPHeLSGGML-----QRIMIAVALSCNPKL 176
Cdd:PRK15439 97 --LFPNLSVKENILFGLPKRQ-----ASMQKMKQLLAALG-------CQLDLD-SSAGSLevadrQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 177 LIADEPTTALdvtIQAQILDLLRQIKKEFKT--SILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK15439 162 LILDEPTASL---TPAETERLFSRIRELLAQgvGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-245 |
1.06e-09 |
|
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: 59.57 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 25 VNHVSFSVREGETVCVVGESGCGKSvTALSimGLIAESGSVvggdilyEGKSllgmkekelrSLRGNdIAMIFQEPMTSl 104
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKS-SLLS--ALLAEMDKV-------EGHV----------HMKGS-VAYVPQQAWIQ- 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 105 npvftvgeqiVETLREHELLSK--NEAYKKAIelIRKVGIARADEIVHSYPH--------ELSGGMLQRIMIAVALSCNP 174
Cdd:TIGR00957 712 ----------NDSLRENILFGKalNEKYYQQV--LEACALLPDLEILPSGDRteigekgvNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 175 KLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSI-LLITHDLGVVAEMaDYVVVMYGGKVIEEAPVLEIFQ 245
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTrILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-223 |
1.08e-09 |
|
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: 56.23 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 35 GETVCVVGESGCGKSVTALSIMGLIAESGSVVggdilyegksllgmkekelrslrgndiamifqepmtslnpVFTVGEQI 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------IYIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 115 VETLREhellskneaykkaielirkvgiARADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQI 194
Cdd:smart00382 42 LEEVLD----------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
170 180 190
....*....|....*....|....*....|....
gi 1355713525 195 LDLLR-----QIKKEFKTSILLITHDLGVVAEMA 223
Cdd:smart00382 100 LLLEElrlllLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
135-231 |
1.59e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 135 ELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITH 214
Cdd:PRK13409 436 EIIKPLQL---ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH 512
|
90
....*....|....*..
gi 1355713525 215 DLGVVAEMADYVVVMYG 231
Cdd:PRK13409 513 DIYMIDYISDRLMVFEG 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-231 |
2.70e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.26 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 31 SVREGETVCVVGESGCGKSVTALSIMGLI-AESGSVVGG-DILYegksllgmKEKELRSlrgnDIAMIFQEPMTSLNPVf 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDlKISY--------KPQYISP----DYDGTVEEFLRSANTD- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 109 TVGEQIVETlrehellskneaykkaiELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV 188
Cdd:COG1245 429 DFGSSYYKT-----------------EIIKPLGL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1355713525 189 TIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-269 |
2.86e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLqtHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAEsgsVVGGDILYEGKSLLGMK 81
Cdd:PLN03232 1231 SRGSIKFEDV--HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKS-SMLNALFRIVE---LEKGRIMIDDCDVAKFG 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLrgndIAMIFQEPMTSLNPV-FTVgeqivETLREHELLSKNEAYKKA--IELIRKVGIArADEIVHSYPHELSG 158
Cdd:PLN03232 1305 LTDLRRV----LSIIPQSPVLFSGTVrFNI-----DPFSEHNDADLWEALERAhiKDVIDRNPFG-LDAEVSEGGENFSV 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQIldlLRQIKKEFKT-SILLITHDLGVVAEmADYVVVMYGGKVIEE 237
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI---QRTIREEFKScTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
250 260 270
....*....|....*....|....*....|..
gi 1355713525 238 APVLEIFQNPKHPYTKGLLKSKPVMGKRIDKL 269
Cdd:PLN03232 1451 DSPQELLSRDTSAFFRMVHSTGPANAQYLSNL 1482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-246 |
3.20e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLqtHFQTEEGTVK-AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVggDIlyEGKSLLgm 80
Cdd:PRK13545 18 NKPFDKLKDL--FFRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--DI--KGSAAL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 kekelrslrgndIAMifqepMTSLNPVFTVGEQIvetlrEHELLSKNEAYKKAIELIRKVgIARAD--EIVHSYPHELSG 158
Cdd:PRK13545 90 ------------IAI-----SSGLNGQLTGIENI-----ELKGLMMGLTKEKIKEIIPEI-IEFADigKFIYQPVKTYSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIEEA 238
Cdd:PRK13545 147 GMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
....*...
gi 1355713525 239 PVLEIFQN 246
Cdd:PRK13545 226 DIKEVVDH 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-187 |
3.64e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTalsiM----GLIAESgsvvggdilyEGK-SLLG 79
Cdd:NF033858 266 AIEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTT----MkmltGLLPAS----------EGEaWLFG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 80 mkekelRSLRGNDIAM---------IFqepmtSLnpvftVGEQiveTLREH-EL------LSKNEAYKKAIELIRKVGIA 143
Cdd:NF033858 328 ------QPVDAGDIATrrrvgymsqAF-----SL-----YGEL---TVRQNlELharlfhLPAAEIAARVAEMLERFDLA 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1355713525 144 radEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALD 187
Cdd:NF033858 389 ---DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-248 |
4.86e-09 |
|
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: 54.89 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYGgkv 234
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG--- 147
|
90
....*....|....
gi 1355713525 235 ieEAPVLEIFQNPK 248
Cdd:cd03222 148 --EPGVYGIASQPK 159
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-236 |
7.74e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFQTEEgTVKAVNhvsFSVREGETVCVVGESGCGKSVTALSIMGliAESGSVVGGDILYEGKSLLGMkEKE 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKA-ILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLEL-SPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 85 LRSlrGNDIAMIFQEPM------------TSLNPVftvgeqivETLREHELLSK---NEAYKKAIELIRkvgiARADEIV 149
Cdd:PRK09580 74 DRA--GEGIFMAFQYPVeipgvsnqfflqTALNAV--------RSYRGQEPLDRfdfQDLMEEKIALLK----MPEDLLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 150 HSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV---TIQAQILDLLRQIKKEFktsiLLITHDLGVVAEMA-DY 225
Cdd:PRK09580 140 RSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKRSF----IIVTHYQRILDYIKpDY 215
|
250
....*....|.
gi 1355713525 226 VVVMYGGKVIE 236
Cdd:PRK09580 216 VHVLYQGRIVK 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-201 |
9.74e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 4 AVVELKDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVVGGDILYEGKSLLGMKEK 83
Cdd:TIGR00956 758 DIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKT-TLLNVLAERVTTGVITGGDRLVNGRPLDSSFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 ELRSLRGNDIAMifqepmtslnPVFTVGE--QIVETLREHELLSKNEAYKKAIELIRKVGIAR-ADEIVHSYPHELSGGM 160
Cdd:TIGR00956 837 SIGYVQQQDLHL----------PTSTVREslRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESyADAVVGVPGEGLNVEQ 906
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1355713525 161 LQRIMIAVALSCNPKLLI-ADEPTTALDVTIQAQILDLLRQI 201
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-231 |
1.06e-08 |
|
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: 55.11 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 31 SVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLlGMKEKELRSlrgnDIAMIFQEPMTSLNPVFTv 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDE----GDIEIELDTV-SYKPQYIKA----DYEGTVRDLLSSITKDFY- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 111 geqivetlrehellskNEAYKKAiELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTI 190
Cdd:cd03237 91 ----------------THPYFKT-EIAKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1355713525 191 QAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMYG 231
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-235 |
2.56e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 9 KDLQTHFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGsVVGGDILYEGKSLlgmkEKELRSL 88
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT-TLLDVLAGRKTAG-VITGEILINGRPL----DKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 89 RGndiamiFQEPMTSLNPVFTVgeqiVETLREHELLskneaykkaielirkvgiaradeivhsypHELSGGMLQRIMIAV 168
Cdd:cd03232 81 TG------YVEQQDVHSPNLTV----REALRFSALL-----------------------------RGLSVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355713525 169 ALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVMY-GGKVI 235
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKrGGKTV 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-234 |
2.63e-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: 55.40 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTaLSIM-GLIAESGsvvgGDILYEGKSLlgmkEKELRSLRgNDIAMIFQEpmt 102
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTT-LSILtGLLPPTS----GTVLVGGKDI----ETNLDAVR-QSLGMCPQH--- 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 103 slNPVF---TVGEQIVeTLREHELLSKNEAYKKAIELIRKVGI--ARADEivhsyPHELSGGMLQRIMIAVALSCNPKLL 177
Cdd:TIGR01257 1012 --NILFhhlTVAEHIL-FYAQLKGRSWEEAQLEMEAMLEDTGLhhKRNEE-----AQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 178 IADEPTTALDVTIQAQILDLLrqIKKEFKTSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
156-237 |
2.92e-08 |
|
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: 52.71 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPK--LLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVaEMADYVVVM---- 229
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVL-SSADWIIDFgpgs 165
|
90
....*....|
gi 1355713525 230 --YGGKVIEE 237
Cdd:cd03238 166 gkSGGKVVFS 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-236 |
3.39e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFQTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSvvgGDILYEGKSLLGMK 81
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKS-SMLNALFRIVELER---GRILIDGCDISKFG 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 ekeLRSLRGNdIAMIFQEPMT-------SLNPvftvgeqivetLREHELLSKNEAYKKA--IELIRK--VGIaraDEIVH 150
Cdd:PLN03130 1308 ---LMDLRKV-LGIIPQAPVLfsgtvrfNLDP-----------FNEHNDADLWESLERAhlKDVIRRnsLGL---DAEVS 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 151 SYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQIldlLRQIKKEFKT-SILLITHDLGVVAEmADYVVVM 229
Cdd:PLN03130 1370 EAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI---QKTIREEFKScTMLIIAHRLNTIID-CDRILVL 1445
|
....*..
gi 1355713525 230 YGGKVIE 236
Cdd:PLN03130 1446 DAGRVVE 1452
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-232 |
4.45e-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: 54.63 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 24 AVNHVSFSVREGETVCVVGESGCGKSVTALSIMGliaeSGSVVGGDILYEGKSLLgmkekelrslrgNDIAMIFQEpmTS 103
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG----DTTVTSGDATVAGKSIL------------TNISDVHQN--MG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVFTVGEQIVeTLREHELL-------SKNEAYKKAIELIRKVGIA-RADEIVHSYphelSGGMLQRIMIAVALSCNPK 175
Cdd:TIGR01257 2016 YCPQFDAIDDLL-TGREHLYLyarlrgvPAEEIEKVANWSIQSLGLSlYADRLAGTY----SGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 176 LLIADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYGG 232
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-219 |
5.68e-08 |
|
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: 52.36 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmkeKELRSLRGNDIAMIFQEPmtSLNPV 107
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKT----TLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLP--GLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 108 FTVgeqiVETLR-EHELLSknEAYKKAIELIRKVGI-ARADEIVHSypheLSGGMLQRIMIAVALSCNPKLLIADEPTTA 185
Cdd:TIGR01189 88 LSA----LENLHfWAAIHG--GAQRTIEDALAAVGLtGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1355713525 186 LDVTIQAQILDLLRQiKKEFKTSILLITH-DLGVV 219
Cdd:TIGR01189 158 LDKAGVALLAGLLRA-HLARGGIVLLTTHqDLGLV 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-235 |
1.15e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIA-----ESGS--VVGGDilyegksl 77
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKS----SLLSLIAgarkiQQGRveVLGGD-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 78 lgMKEKELRSLRGNDIAMIFQEPMTSLNPVFTVGEQIVETLReheLLSKNEAYKKA-I-ELIRKVGIAR-ADEivhsyPH 154
Cdd:NF033858 65 --MADARHRRAVCPRIAYMPQGLGKNLYPTLSVFENLDFFGR---LFGQDAAERRRrIdELLRATGLAPfADR-----PA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 -ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfktsilliTHDLGVV--------AEMADY 225
Cdd:NF033858 135 gKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE--------RPGMSVLvataymeeAERFDW 206
|
250
....*....|
gi 1355713525 226 VVVMYGGKVI 235
Cdd:NF033858 207 LVAMDAGRVL 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-246 |
1.30e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 17 TEEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGSVVGGDILYEGKSLLGMKekelRSLRGnDIAMI 96
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIK----KHYRG-DVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 97 FQepmTSLN-PVFTVGEQIVETLR------EHELLSKNEAYKKAIELI-----------RKVGiaraDEIVHSypheLSG 158
Cdd:TIGR00956 144 AE---TDVHfPHLTVGETLDFAARcktpqnRPDGVSREEYAKHIADVYmatyglshtrnTKVG----NDFVRG----VSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 159 GMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVA-EMADYVVVMYGGKVIEE 237
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAyELFDKVIVLYEGYQIYF 292
|
250
....*....|..
gi 1355713525 238 AP---VLEIFQN 246
Cdd:TIGR00956 293 GPadkAKQYFEK 304
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-245 |
1.33e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 23 KAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGliaES-GSVVGGDILYEGKsllgmkEKELRSLR---GNDIAMIFQ 98
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSyGRNISGTVFKDGK------EVDVSTVSdaiDAGLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 99 EPMTS-LNPVFTVGEQIV----ETLREHELLSKNEAYKKAIELIRKVGIaRA---DEIVHSypheLSGGMLQRIMIAVAL 170
Cdd:NF040905 345 DRKGYgLNLIDDIKRNITlanlGKVSRRGVIDENEEIKVAEEYRKKMNI-KTpsvFQKVGN----LSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 171 SCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYGGKVIEEAPVLEIFQ 245
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQ 493
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-240 |
2.53e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 22 VKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAESGsvvgGDILYEGKSLLGMKEKELRSlrgNDIAMIFQEpm 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS----GSILFQGKEIDFKSSKEALE---NGISMVHQE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 tsLNPVF--TVGEQIV--ETLREHELLSKNEAYKKAIELIRKVGIaraDEIVHSYPHELSGGMLQRIMIAVALSCNPKLL 177
Cdd:PRK10982 82 --LNLVLqrSVMDNMWlgRYPTKGMFVDQDKMYRDTKAIFDELDI---DIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 178 IADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAPV 240
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-219 |
2.57e-07 |
|
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: 50.18 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmkeKELRSLRGNDIAMIFQEPmtSLNPV 107
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKT----TLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAP--GIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 108 FTVgeqiVETLREHELLSKNEAYKKAIElirKVGIARADeivHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALD 187
Cdd:cd03231 88 LSV----LENLRFWHADHSDEQVEEALA---RVGLNGFE---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|...
gi 1355713525 188 VTIQAQILDLLRQiKKEFKTSILLITH-DLGVV 219
Cdd:cd03231 158 KAGVARFAEAMAG-HCARGGMVVLTTHqDLGLS 189
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-214 |
2.94e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 17 TEEGTVkAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGdILY---EGKsLLGMKEK---ELRSLRG 90
Cdd:TIGR00954 461 TPNGDV-LIESLSFEVPSGNNLLICGPNGCGKS----SLFRILGELWPVYGG-RLTkpaKGK-LFYVPQRpymTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 91 NDIAmifqePMTSLNpVFTVG------EQIVETLREHELLSKNEAYkkaielirkvgiaradEIVHSYPHELSGGMLQRI 164
Cdd:TIGR00954 534 QIIY-----PDSSED-MKRRGlsdkdlEQILDNVQLTHILEREGGW----------------SAVQDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1355713525 165 MIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRqikkEFKTSILLITH 214
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-215 |
4.07e-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: 51.47 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvTALSIMGliaesgsvvGGDILYEGksllgmkekELRSLRGNDIAMIFQEPmtSLNPV 107
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKS-TLLRIMA---------GVDKDFNG---------EARPQPGIKVGYLPQEP--QLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 108 FTVGEQIVETLRE-HELLSK-NEAYKK--------------------------AIELIRKVGIA----RA---DEIVHsy 152
Cdd:TIGR03719 83 KTVRENVEEGVAEiKDALDRfNEISAKyaepdadfdklaaeqaelqeiidaadAWDLDSQLEIAmdalRCppwDADVT-- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355713525 153 phELSGGMLQRIMIAVALSCNPKLLIADEPTTALDvtiqAQILDLLRQIKKEFKTSILLITHD 215
Cdd:TIGR03719 161 --KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-239 |
5.35e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGKSLlgmkekELRSLRGNDIAMIFQEP----MTS 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRS----ELMKLLYGATRRTAGQVYLDGKPI------DIRSPRDAIRAGIMLCPedrkAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 104 LNPVFTVGEQIVETLREHELL------SKNEAyKKAIELIRKVGI---ARADEIVHsypheLSGGMLQRIMIAVALSCNP 174
Cdd:PRK11288 342 IIPVHSVADNINISARRHHLRagclinNRWEA-ENADRFIRSLNIktpSREQLIMN-----LSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355713525 175 KLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVMYGGKVIEEAP 239
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-215 |
8.09e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 3 KAVVELKDLqtHFQTEEGTVkaVNHVSFSVREGETVCVVGESGCGKSvTALSIM--GLIAESGSVVGGDILyegksllgm 80
Cdd:PRK11147 317 KIVFEMENV--NYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKT-TLLKLMlgQLQADSGRIHCGTKL--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 81 kekelrslrgnDIAMiFQEPMTSLNPVFTV------GEQIVETL-REHELLSkneaY--------KKAIELIRKvgiara 145
Cdd:PRK11147 383 -----------EVAY-FDQHRAELDPEKTVmdnlaeGKQEVMVNgRPRHVLG----YlqdflfhpKRAMTPVKA------ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 146 deivhsypheLSGGMLQRIMIAVALSCNPKLLIADEPTTALDVtiqaQILDLLRQIKKEFKTSILLITHD 215
Cdd:PRK11147 441 ----------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-199 |
1.53e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.95 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvTAL-SIMGLIAesgsVVGGDILYEGKsllgmkEKELRSLRGndiAMIFQEPMTSLNP 106
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKT-TLLrLIAGLLP----PAAGTIKLDGG------DIDDPDVAE---ACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 107 VFTVGEQIV---ETLREHELlskneaykKAIELIRKVGIARadeIVHSYPHELSGGMLQRIMIAVALSCNPKLLIADEPT 183
Cdd:PRK13539 87 ALTVAENLEfwaAFLGGEEL--------DIAAALEAVGLAP---LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170
....*....|....*.
gi 1355713525 184 TALDVTIQAQILDLLR 199
Cdd:PRK13539 156 AALDAAAVALFAELIR 171
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-235 |
2.00e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.24 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALS---CNPKLLIADEPTTAL---DVtiqAQILDLLRQIKKEFKTsILLITHDLGVVaEMADYVVVM 229
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNT-VVVIEHNLDVI-KTADYIIDL 904
|
90
....*....|..
gi 1355713525 230 ------YGGKVI 235
Cdd:TIGR00630 905 gpeggdGGGTVV 916
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-236 |
3.17e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 21 TVKAVNHVSFSVREGETVCVVGESGCGKSvtalSIMGLIAESGSVVGGDILYEGksllgmkekelrslrgnDIAMIFQEp 100
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKS----TLSNIIGGSLSPTVGKVDRNG-----------------EVSVIAIS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 101 mTSLNPVFTVGEQIvetlrEHELLSKNEAYKKAIELIRK-VGIARADEIVHSYPHELSGGMLQRIMIAVALSCNPKLLIA 179
Cdd:PRK13546 94 -AGLSGQLTGIENI-----EFKMLCMGFKRKEIKAMTPKiIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 180 DEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEMADYVVVMYGGKVIE 236
Cdd:PRK13546 168 DEALSVGDQTFAQKCLDKIYEFKEQNKT-IFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-247 |
3.97e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFQteEGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIaesgSVVGGDILYEGKSLLGMKEKEL 85
Cdd:PTZ00243 1309 LVFEGVQMRYR--EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV----EVCGGEIRVNGREIGAYGLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLrgndIAMIFQEPMtslnpVF--TVgEQIVETLREhelLSKNEAYkKAIELirkVG----IARADEIVHSYPHE---- 155
Cdd:PTZ00243 1383 RRQ----FSMIPQDPV-----LFdgTV-RQNVDPFLE---ASSAEVW-AALEL---VGlrerVASESEGIDSRVLEggsn 1445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVA-LSCNPKLLIADEPTT----ALDVTIQAQILDLLRQIkkefktSILLITHDLGVVAEMaDYVVVMY 230
Cdd:PTZ00243 1446 YSVGQRQLMCMARAlLKKGSGFILMDEATAnidpALDRQIQATVMSAFSAY------TVITIAHRLHTVAQY-DKIIVMD 1518
|
250
....*....|....*..
gi 1355713525 231 GGKVIEEAPVLEIFQNP 247
Cdd:PTZ00243 1519 HGAVAEMGSPRELVMNR 1535
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
156-246 |
1.14e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAEMaDYVVVMYGGKVI 235
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRV-LVTNQLHFLPLM-DRIILVSEGMIK 818
|
90
....*....|.
gi 1355713525 236 EEAPVLEIFQN 246
Cdd:PLN03232 819 EEGTFAELSKS 829
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
38-235 |
1.95e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.94 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 38 VCVVGESGCGKSvtALSIMGLIAEsgsvvgGDILY-EGKS-----LLGMKEK-ELRSLRGNDIAMIFQEPMTSLNPVFTV 110
Cdd:cd03270 24 VVITGVSGSGKS--SLAFDTIYAE------GQRRYvESLSayarqFLGQMDKpDVDSIEGLSPAIAIDQKTTSRNPRSTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 111 GE--QIVETLReheLLSKNEAYKKAIELIRKVGIA--RADEIVHSypheLSGGMLQRIMIAVALSCNPK--LLIADEPTT 184
Cdd:cd03270 96 GTvtEIYDYLR---LLFARVGIRERLGFLVDVGLGylTLSRSAPT----LSGGEAQRIRLATQIGSGLTgvLYVLDEPSI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 185 ALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEmADYVVVM------YGGKVI 235
Cdd:cd03270 169 GLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIV 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
156-234 |
2.45e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 2.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKtSILLITHDLGVVAEMADYVVVMYGGKV 234
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-239 |
3.73e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 155 ELSGGMLQRIMIAVALS---CNPKLLIADEPTTALDVTIQAQILDLLRQIkKEFKTSILLITHDLGVVAeMADYVVVM-- 229
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK-CADWIIDLgp 246
|
90
....*....|....
gi 1355713525 230 ----YGGKVIEEAP 239
Cdd:cd03271 247 eggdGGGQVVASGT 260
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-228 |
5.82e-05 |
|
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: 44.07 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 6 VELKDLQTHFqTEEGTVkAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGLIAesgsvVGGDILYEGKSLLGMKEKEL 85
Cdd:cd03289 3 MTVKDLTAKY-TEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-----TEGDIQIDGVSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 86 RSLRGndiaMIFQEpmtslnpVFTVGEQIVETLREHELLSKNEAYKKAIELIRKVGI----ARADEIVHSYPHELSGGML 161
Cdd:cd03289 76 RKAFG----VIPQK-------VFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIeqfpGQLDFVLVDGGCVLSHGHK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 162 QRIMIAVALSCNPKLLIADEPTTALD-VTIQAqildLLRQIKKEFKT-SILLITHDLGVVAEMADYVVV 228
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDpITYQV----IRKTLKQAFADcTVILSEHRIEAMLECQRFLVI 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
156-246 |
9.51e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDllRQIKKEF--KTSIlLITHDLGVVAEMaDYVVVMYGGK 233
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrgKTRV-LVTNQLHFLSQV-DRIILVHEGM 816
|
90
....*....|...
gi 1355713525 234 VIEEAPVLEIFQN 246
Cdd:PLN03130 817 IKEEGTYEELSNN 829
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
156-229 |
1.05e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEfKTSILLITHDLGVVAEMADYVVVM 229
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-215 |
1.26e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 16 QTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMG--LIAESGSVvggdilyegksllgmkekelrSLRGN-D 92
Cdd:PRK10636 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKS-TLLALLKneISADGGSY---------------------TFPGNwQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 93 IAMIFQEPMTSLNPVFtvgEQIVETLREHELL--------SKNEAYKKA-----IELIRKVGI-ARADEIVH----SYPH 154
Cdd:PRK10636 66 LAWVNQETPALPQPAL---EYVIDGDREYRQLeaqlhdanERNDGHAIAtihgkLDAIDAWTIrSRAASLLHglgfSNEQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355713525 155 ------ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDvtIQAQIldLLRQIKKEFKTSILLITHD 215
Cdd:PRK10636 143 lerpvsDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI--WLEKWLKSYQGTLILISHD 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-245 |
1.46e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 28 VSFSVREGETVCVVGESGCGKSvtalSIMGLIA--ESGSVVGGDILYEGkslLGMKEKELRSLRG----NDIAmifqepm 101
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKT----TLMDVLAgrKTGGYIEGDIRISG---FPKKQETFARISGyceqNDIH------- 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 102 tslNPVFTVGEQIVET--LREHELLSKNEAYKKAIELIRKVGIARADEIVHSYP--HELSGGMLQRIMIAVALSCNPKLL 177
Cdd:PLN03140 965 ---SPQVTVRESLIYSafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 178 IADEPTTALDVTIQAQILDLLRQIKKEFKTSILLITHDLGVVAEMADYVVVM-YGGKVIEEAP-------VLEIFQ 245
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMkRGGQVIYSGPlgrnshkIIEYFE 1117
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-215 |
1.67e-04 |
|
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: 43.00 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 5 VVELKDLQTHFqteeGTVKAVNHVSFSVREGETVCVVGESGCGKSVTALSIMGL-IAESGSVVGGDILyegksllgmkek 83
Cdd:TIGR03719 322 VIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEIGETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 84 elrslrgnDIAMIFQEpMTSLNPVFTVGEQIVETLrEHELLSKNE----AYK-----KAIELIRKVGiaradeivhsyph 154
Cdd:TIGR03719 386 --------KLAYVDQS-RDALDPNKTVWEEISGGL-DIIKLGKREipsrAYVgrfnfKGSDQQKKVG------------- 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355713525 155 ELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV-TIQAqildlLRQIKKEFKTSILLITHD 215
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
156-227 |
2.05e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 156 LSGGMLQRIMIAVAL---SCNPKLLIADEPTTALDV-TIQAQILDLLRQIKKefKTSILLITHDLGVVaEMADYVV 227
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQ--GHTVVIIEHNMHVV-KVADYVL 882
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-228 |
2.47e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 2 SKAVVELKDLQTHFqTEEGTvKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESgsvvGGDILYEGKSLLGMK 81
Cdd:TIGR01271 1214 SGGQMDVQGLTAKY-TEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKS-TLLSALLRLLST----EGEIQIDGVSWNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 82 EKELRSLRGndiaMIFQEpmtslnpVFTVGEQIVETLREHELLSKNEAYKKAIElirkVGIAradEIVHSYPHE------ 155
Cdd:TIGR01271 1287 LQTWRKAFG----VIPQK-------VFIFSGTFRKNLDPYEQWSDEEIWKVAEE----VGLK---SVIEQFPDKldfvlv 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 -----LSGGMLQRIMIAVALSCNPKLLIADEPTTALD-VTIQAqildLLRQIKKEFKT-SILLITHDLGVVAEMADYVVV 228
Cdd:TIGR01271 1349 dggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQI----IRKTLKQSFSNcTVILSEHRVEALLECQQFLVI 1424
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-215 |
3.91e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 40 VVGESGCGKSvTALSIMGliaesgsvvGGDILYEGksllgmkekELRSLRGNDIAMIFQEPmtSLNPVFTVGEQIVETLR 119
Cdd:PRK11819 38 VLGLNGAGKS-TLLRIMA---------GVDKEFEG---------EARPAPGIKVGYLPQEP--QLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 120 E-HELLSK-NEAYKK--------------------------AIELIRKVGIA----R---ADEIVHSypheLSGGMLQRi 164
Cdd:PRK11819 97 EvKAALDRfNEIYAAyaepdadfdalaaeqgelqeiidaadAWDLDSQLEIAmdalRcppWDAKVTK----LSGGERRR- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1355713525 165 miaVALsC-----NPKLLIADEPTTALDvtiqAQILDLLRQIKKEFKTSILLITHD 215
Cdd:PRK11819 172 ---VAL-CrllleKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
156-234 |
4.68e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 4.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1355713525 156 LSGGMLQRIMIAVALSCNPKLLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGVVAeMADYVVVMYGGKV 234
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRV-LATHQVHVVP-RADYVVALGDGRV 859
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
154-230 |
4.73e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 154 HELSGGMLQRIMIAVAL---SCNPK-LLIADEPTTALDVTIQAQILDLLRQIKKEFKTSIlLITHDLGvVAEMADYVVVM 229
Cdd:cd03227 76 LQLSGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVI-VITHLPE-LAELADKLIHI 153
|
.
gi 1355713525 230 Y 230
Cdd:cd03227 154 K 154
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
156-257 |
6.71e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALScnpK------LLIADEPTTAL---DVtiqAQILDLLRQIkKEFKTSILLITHDLGVVaEMADYV 226
Cdd:PRK00349 831 LSGGEAQRVKLAKELS---KrstgktLYILDEPTTGLhfeDI---RKLLEVLHRL-VDKGNTVVVIEHNLDVI-KTADWI 902
|
90 100 110
....*....|....*....|....*....|....*..
gi 1355713525 227 VVM------YGGKVIEEAPVLEIFQNPKhPYTKGLLK 257
Cdd:PRK00349 903 IDLgpeggdGGGEIVATGTPEEVAKVEA-SYTGRYLK 938
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
129-224 |
8.02e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 129 AYKKAIELIRKVGIaraDEIVHSYP-HELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV-TIQaqildLLRQIKKEFK 206
Cdd:PRK15064 131 AEARAGELLLGVGI---PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDVLNERN 202
|
90 100
....*....|....*....|..
gi 1355713525 207 TSILLITHDL----GVVAEMAD 224
Cdd:PRK15064 203 STMIIISHDRhflnSVCTHMAD 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-188 |
1.32e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 14 HFQTEEGTVKAVNHVSFSVREGETVCVVGESGCGKSvTALSIMGLIAESGSVVGGDILYEGKSLLGMKEKELRSLRGNDI 93
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT-TFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTTALQCVLNTDI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 94 ---------AMIFQEPMTSLNPVFT---------------VGEQIVETLREHELLSKNEAYKKAIELIrkVGIARADEIV 149
Cdd:PLN03073 261 ertqlleeeAQLVAQQRELEFETETgkgkgankdgvdkdaVSQRLEEIYKRLELIDAYTAEARAASIL--AGLSFTPEMQ 338
|
170 180 190
....*....|....*....|....*....|....*....
gi 1355713525 150 HSYPHELSGGMLQRIMIAVALSCNPKLLIADEPTTALDV 188
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
156-260 |
2.26e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALS---CNPKLLIADEPTTAL---DVtiqAQILDLLRQIkKEFKTSILLITHDLGVVAeMADYVVVM 229
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDI---RKLLEVLHRL-VDKGNTVVVIEHNLDVIK-TADWIIDL 901
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1355713525 230 ------YGGKVIEEAPVLEIFQNPKhPYT----KGLLKSKP 260
Cdd:COG0178 902 gpeggdGGGEIVAEGTPEEVAKVKA-SYTgrylKEYLEAAR 941
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-248 |
6.62e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355713525 156 LSGGMLQRIMIAVALSCNPK--LLIADEPTTALDVTIQAQILDLLRQIKKEFKTsILLITHDLGVVAEmADYVVVM---- 229
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNT-LIVVEHDEDTIRA-ADYVIDIgpga 566
|
90 100
....*....|....*....|.
gi 1355713525 230 --YGGKVIEEAPVLEIFQNPK 248
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANPD 587
|
|
| |
