|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-317 |
9.81e-173 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 481.92 E-value: 9.81e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPW-RPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRID 79
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGGLFgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 80 RLTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQR 159
Cdd:COG4608 84 GLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 160 QRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTA 239
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 240 DVFAAPRHPYTRALLDAVPRLVPTGEPRR-LLAGDPPSPLAPPSGCVFRTRCPHAIAACAEVMPPLEADADGHAAACIR 317
Cdd:COG4608 244 ELYARPLHPYTQALLSAVPVPDPERRRERiVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQVACHL 322
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-321 |
6.99e-164 |
|
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: 459.13 E-value: 6.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPpwrpplVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP---ISSGEVHFAGRRIDR 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRG------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVR-RRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGL--PRGTAQNYPGALSGG 157
Cdd:COG0444 75 LSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 158 QRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGR 237
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 238 TADVFAAPRHPYTRALLDAVPRLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAACAEVMPPLEADADGHAAACIR 317
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHL 314
|
....
gi 2075269590 318 QHEV 321
Cdd:COG0444 315 YEEE 318
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-263 |
1.11e-129 |
|
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: 379.25 E-value: 1.11e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 2 TALLDVNDLGVEFRLKSPPWRpplvlHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRL 81
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKGGV-----RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 82 TGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQR 161
Cdd:COG1123 333 SRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 162 VGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
250 260
....*....|....*....|..
gi 2075269590 242 FAAPRHPYTRALLDAVPRLVPT 263
Cdd:COG1123 493 FANPQHPYTRALLAAVPSLDPA 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-260 |
3.13e-129 |
|
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: 379.03 E-value: 3.13e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPPW-RPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPiSSGEVHFAGRRIDRLT 82
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 83 GRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIG-TRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQR 161
Cdd:COG4172 354 RRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 162 VGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|....*....
gi 2075269590 242 FAAPRHPYTRALLDAVPRL 260
Cdd:COG4172 514 FDAPQHPYTRALLAAAPLL 532
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-317 |
1.75e-128 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 369.81 E-value: 1.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSP---PWRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDR 80
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIG-TRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQR 159
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 160 QRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTA 239
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 240 DVFAAPRHPYTRALLDAVPrlVPTGEPRR-----LLAGDPPSPLAPPSGCVFRTRCPHAIAACAEVMPPLEADaDGHAAA 314
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVP--IPDPDLERnktiqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGS-FRHAVS 324
|
...
gi 2075269590 315 CIR 317
Cdd:PRK15079 325 CLK 327
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-321 |
5.47e-120 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 348.11 E-value: 5.47e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPWRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI-- 78
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 79 -DRLTGRQLgpvRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGG 157
Cdd:PRK11308 82 aDPEAQKLL---RQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 158 QRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGR 237
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 238 TADVFAAPRHPYTRALLDAVPRLVPTGEPRRL-LAGDPPSPLAPPSGCVFRTRCPHAIAACAEVMPPLEaDADGHAAACI 316
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPDDRRERIkLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLR-DYDGRLVACF 317
|
....*
gi 2075269590 317 RQHEV 321
Cdd:PRK11308 318 AVEQD 322
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-236 |
3.61e-107 |
|
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: 311.75 E-value: 3.61e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSppwrppLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTG 83
Cdd:cd03257 1 LLEVKNLSVSFPTGG------GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 84 RQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTR-ADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRV 162
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKkEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 163 GIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-261 |
1.31e-103 |
|
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: 303.26 E-value: 1.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPpwrpplVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrlTG 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGR------RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 84 RQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGtraDRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVG 163
Cdd:COG1124 72 RRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 164 IARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*...
gi 2075269590 244 APRHPYTRALLDAVPRLV 261
Cdd:COG1124 229 GPKHPYTRELLAASLAFE 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-275 |
2.23e-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: 2.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRlksppwRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP----ISSGEVHFAGR 76
Cdd:COG4172 3 SMPLLSVEDLSVAFG------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 77 RIDRLTGRQLGPVR-RRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGL--PRGTAQNYPGA 153
Cdd:COG4172 77 DLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpdPERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVM 233
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2075269590 234 ETGRTADVFAAPRHPYTRALLDAVPRlvptGEPRRLLAGDPP 275
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLLAAEPR----GDPRPVPPDAPP 274
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-320 |
3.21e-95 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 285.08 E-value: 3.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRlksppwRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP---ISSGEVHFAGRR 77
Cdd:PRK09473 9 ADALLDVKDLRVTFS------TPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 78 IDRLTGRQLGPVR-RRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLP--RGTAQNYPGAL 154
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPeaRKRMKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 155 SGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVME 234
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 235 TGRTADVFAAPRHPYTRALLDAVPRLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAACAEvMPPLEADADGHAAA 314
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSS-APPLEEFGPGRLRA 321
|
....*.
gi 2075269590 315 CIRQHE 320
Cdd:PRK09473 322 CFKPVE 327
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-254 |
3.99e-81 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 255.40 E-value: 3.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 2 TALLDVNDLGVEFRLKSPPWRPPLVLH-AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPiSSGEVHFAGRRIDR 80
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILKRTVDHNvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIG-TRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQR 159
Cdd:PRK15134 352 LNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 160 QRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTA 239
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE 511
|
250
....*....|....*
gi 2075269590 240 DVFAAPRHPYTRALL 254
Cdd:PRK15134 512 RVFAAPQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-273 |
1.07e-79 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 254.01 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPPW-RPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT 82
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLnRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 83 GRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRV 162
Cdd:PRK10261 393 PGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 163 GIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
250 260 270
....*....|....*....|....*....|..
gi 2075269590 243 AAPRHPYTRALLDAVPRLVPT-GEPRRLLAGD 273
Cdd:PRK10261 553 ENPQHPYTRKLMAAVPVADPSrQRPQRVLLSD 584
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-254 |
1.00e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 240.89 E-value: 1.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPWRPPlVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdr 80
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLFRRQ-QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 ltgrQLGPVRRRMQ---AVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGG 157
Cdd:COG4167 78 ----EYGDYKYRCKhirMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 158 QRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGR 237
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*..
gi 2075269590 238 TADVFAAPRHPYTRALL 254
Cdd:COG4167 234 TAEVFANPQHEVTKRLI 250
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-275 |
1.32e-75 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 240.58 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPwrpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIS---SGEVHFAGRR 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVP--------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 78 IDRLTGRQLGpvrRRMQAVFQDPTSSLNPTmTVGAAVGEGLGVHRIgTRADRAERVAAMLDRVGLPRGTAQnYPGALSGG 157
Cdd:COG1123 73 LLELSEALRG---RRIGMVFQDPMTQLNPV-TVGDQIAEALENLGL-SRAEARARVLELLEAVGLERRLDR-YPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 158 QRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGR 237
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 2075269590 238 TADVFAAPRhpytraLLDAVPRLVPTGEPRRLLAGDPP 275
Cdd:COG1123 227 PEEILAAPQ------ALAAVPRLGAARGRAAPAAAAAE 258
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-315 |
1.71e-72 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 226.93 E-value: 1.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 3 ALLDVNDLGVEFRLKSPPWRpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP----ISSGEVHFAGRRI 78
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFR------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 79 DRLTG---RQLgpVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQ--NYPGA 153
Cdd:PRK11022 76 QRISEkerRNL--VGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVM 233
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 234 ETGRTADVFAAPRHPYTRALLDAVPRLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAACAEVMPPLEADAdGHAA 313
Cdd:PRK11022 234 ETGKAHDIFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA-GRQS 312
|
..
gi 2075269590 314 AC 315
Cdd:PRK11022 313 KC 314
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
28-276 |
7.44e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 223.03 E-value: 7.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDptSSLNPT 107
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQH--FNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVG---EGLGVhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:COG1135 97 RTVAENVAlplEIAGV----PKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 185 DVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAVPRLVPTG 264
Cdd:COG1135 172 DPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPE 251
|
250
....*....|..
gi 2075269590 265 EPRRLLAGDPPS 276
Cdd:COG1135 252 ELLARLREAAGG 263
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-275 |
4.87e-68 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 221.50 E-value: 4.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 2 TALLDVNDLGVEFRlksppwRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIS-----SGEVHFAGR 76
Cdd:PRK15134 3 QPLLAIENLSVAFR------QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 77 RIDRLTGRQLGPVR-RRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHR-IGTRADRAERVAAmLDRVGL--PRGTAQNYPG 152
Cdd:PRK15134 77 SLLHASEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNC-LDRVGIrqAAKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 153 ALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2075269590 233 METGRTADVFAAPRHPYTRALLDAvprlVPTGEPRRLLAGDPP 275
Cdd:PRK15134 236 VEQNRAATLFSAPTHPYTQKLLNS----EPSGDPVPLPEPASP 274
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
27-246 |
1.89e-64 |
|
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: 203.20 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDptSSLNP 106
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH--FNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:cd03258 96 SRTVFENVALPLEIAGVP-KAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 187 SVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPR 246
Cdd:cd03258 174 ETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-257 |
4.56e-62 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 198.11 E-value: 4.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 3 ALLDVNDLGVEFR----LKSPPWRPplVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRtgglFGAKQRAP--VLT---NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 79 DRLTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQ 158
Cdd:TIGR02769 76 YQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRT 238
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
250
....*....|....*....
gi 2075269590 239 ADVFAApRHPYTRALLDAV 257
Cdd:TIGR02769 236 AQLLSF-KHPAGRNLQSAV 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
30-275 |
5.02e-62 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 197.99 E-value: 5.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDPTSSLNPTMT 109
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEGLGvHRIG-TRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSV 188
Cdd:PRK10419 108 VREIIREPLR-HLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 189 QAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAApRHPYTRALLDAVprlVPTgEPRR 268
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGRVLQNAV---LPA-FPVR 261
|
....*..
gi 2075269590 269 LLAGDPP 275
Cdd:PRK10419 262 RRTTEKV 268
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-315 |
1.91e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 193.58 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 3 ALLDVNDLGVEfrLKSPPWRpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP----ISSGEVHFAGRRI 78
Cdd:COG4170 2 PLLDIRNLTIE--IDTPQGR----VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 79 DRLTGRQlgpvRRR-----MQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTR-----ADRAERVAAMLDRVGL--PRGT 146
Cdd:COG4170 76 LKLSPRE----RRKiigreIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIkdHKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 147 AQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMV 226
Cdd:COG4170 152 MNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 227 LYLGRVMETGRTADVFAAPRHPYTRALLDAVP---RLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAACAEvMPP 303
Cdd:COG4170 232 LYCGQTVESGPTEQILKSPHHPYTKALLRSMPdfrQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVE-TPR 310
|
330
....*....|..
gi 2075269590 304 LEADaDGHAAAC 315
Cdd:COG4170 311 LRKI-KGHEFAC 321
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
28-257 |
1.29e-58 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 189.25 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQA------VFQDPT 101
Cdd:COG4107 26 VACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDGGPRDLFALSEAERRRLRrtdwgmVYQNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 SSLNPTMTVGAAVGEGL---GVHRIGTRADRAERvaaMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:COG4107 106 DGLRMDVSAGGNIAERLmaaGERHYGDIRARALE---WLERVEIPLERIDDLPRTFSGGMQQRVQIARALVTNPRLLFLD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAV 257
Cdd:COG4107 183 EPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
31-254 |
4.85e-56 |
|
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: 181.72 E-value: 4.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDP---TSslnpt 107
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQGGalfDS----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD-V 186
Cdd:COG1127 97 LTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 187 SVQAgIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPrHPYTRALL 254
Cdd:COG1127 176 TSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
27-257 |
6.55e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 184.62 E-value: 6.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQ--DPTSSl 104
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQhfNLLSS- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 nptMTVGAAVGEGL---GVhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:PRK11153 97 ---RTVFDNVALPLelaGT----PKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAV 257
Cdd:PRK11153 169 SALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQST 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-254 |
1.13e-55 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 181.91 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPWRPPLVlHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRidr 80
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRRQTV-EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQ 160
Cdd:PRK15112 77 LHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 161 RVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTAD 240
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....
gi 2075269590 241 VFAAPRHPYTRALL 254
Cdd:PRK15112 237 VLASPLHELTKRLI 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-282 |
6.58e-55 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 188.53 E-value: 6.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPPwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAG---RRIDR 80
Cdd:PRK10261 12 VLAVENLNIAFMQEQQK------IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllRRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 -------LTGRQLGPVR-RRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTA--QNY 150
Cdd:PRK10261 86 qvielseQSAAQMRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 151 PGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLG 230
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 231 RVMETGRTADVFAAPRHPYTRALLDAVPRLVP---TGEPRR--LLAGDPPSPLAPPS 282
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTRALLAAVPQLGAmkgLDYPRRfpLISLEHPAKQEPPI 302
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
31-251 |
6.83e-55 |
|
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: 178.46 E-value: 6.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDptSSLNPTMTV 110
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS--GALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 GAAVGEGLGVHRIGTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:cd03261 95 FENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 191 GIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGrTADVFAAPRHPYTR 251
Cdd:cd03261 174 VIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG-TPEELRASDDPLVR 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-257 |
2.45e-51 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 170.11 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGvefRLKSPpwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDR 80
Cdd:PRK11701 3 DQPLLSVRGLT---KLYGP-------RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRRMQA------VFQDPTSSLNPTMTVGAAVGE---GLGVHRIGTRADRAervAAMLDRVGLPRGTAQNYP 151
Cdd:PRK11701 73 RDLYALSEAERRRLLrtewgfVHQHPRDGLRMQVSAGGNIGErlmAVGARHYGDIRATA---GDWLERVEIDAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 152 GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGR 231
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|....*.
gi 2075269590 232 VMETGRTADVFAAPRHPYTRALLDAV 257
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-227 |
5.20e-51 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 168.03 E-value: 5.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRLKSPPwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgr 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGA------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 qlgpVRRRMQAVFQDPtsSLNPTMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGI 164
Cdd:cd03293 71 ----PGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVP-KAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 165 ARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-260 |
6.88e-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: 169.36 E-value: 6.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRR-RMQAVFQdpTSSLNPT 107
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQ--SFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03294 117 RTVLENVAFGLEVQGVP-RAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAVPRL 260
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRA 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
27-257 |
3.84e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 166.32 E-value: 3.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrLTGRQLGPVRRRMQAVFQdptsSLN- 105
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKVGMVFQ----QFNl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 -PTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:COG1126 89 fPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 185 DVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAV 257
Cdd:COG1126 168 DPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-237 |
5.60e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.60 E-value: 5.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLgravLRLL----PISSGEVHFAGR 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGE------VTALRGVSLSIEAGEFVAIVGPSGSGKSTL----LNILggldRPTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 77 RIDRLTGRQLGPVRRRMQA-VFQDPTssLNPTMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLPrGTAQNYPGALS 155
Cdd:COG1136 71 DISSLSERELARLRRRHIGfVFQFFN--LLPELTALENVALPLLLAGVS-RKERRERARELLERVGLG-DRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 156 GGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMET 235
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
..
gi 2075269590 236 GR 237
Cdd:COG1136 226 ER 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
28-241 |
7.22e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 166.00 E-value: 7.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDPtsSLNPT 107
Cdd:COG3638 17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIFQQF--NLVPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLgVHRIGT------RADRAERVAAM--LDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:COG3638 95 LSVLTNVLAGR-LGRTSTwrsllgLFPPEDRERALeaLERVGLA-DKAYQRADQLSGGQQQRVAIARALVQEPKLILADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG3638 173 PVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
28-249 |
6.63e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.81 E-value: 6.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDPtsSLNPT 107
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-----PEKRNVGMVFQDY--ALFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:COG3842 92 LTVAENVAFGLRMRGVP-KAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPY 249
Cdd:COG3842 170 LREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
28-321 |
7.57e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 166.48 E-value: 7.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgrQLGPVRRRMQAVFQDPtsSLNPT 107
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPPRERRVGFVFQHY--ALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVhRIGTRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:COG1118 90 MTVAENIAFGLRV-RPPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAVPRLVPTGEPR 267
Cdd:COG1118 168 VRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRGRVIGG 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 268 RLLAGDPPSPLAPPSgcvfrtrcphaiaacaevmppleadADGHAAACIRQHEV 321
Cdd:COG1118 248 QLEADGLTLPVAEPL-------------------------PDGPAVAGVRPHDI 276
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
1.98e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 162.95 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDR 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGG------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRqlgpvrRRMqaVFQDPTssLNPTMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQ 160
Cdd:COG1116 78 PGPD------RGV--VFQEPA--LLPWLTVLDNVALGLELRGVP-KAERRERARELLELVGL-AGFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 161 RVGIARALIVAPDLLIADEAVSALDV----SVQagivNLLLDLREEMGLAMLFIAHDLD-VVRhFCDRVMVL 227
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVL 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
27-232 |
2.84e-48 |
|
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: 161.12 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRR-MQAVFQDPTssLN 105
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSFN--LL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03255 95 PDLTALENVELPLLLAGVP-KKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRV 232
Cdd:cd03255 173 SETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-315 |
3.87e-48 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 164.21 E-value: 3.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPPwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRL----LPISSGEVHFAGRRID 79
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGW------VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 80 RLTGRQlgpvRRR-----MQAVFQDPTSSLNPTMTVGAAVGE--------GLGVHRIGTRADRAervAAMLDRVGL--PR 144
Cdd:PRK15093 77 RLSPRE----RRKlvghnVSMIFQEPQSCLDPSERVGRQLMQnipgwtykGRWWQRFGWRKRRA---IELLHRVGIkdHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 145 GTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRV 224
Cdd:PRK15093 150 DAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 225 MVLYLGRVMETGRTADVFAAPRHPYTRALLDAVP---RLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAACAEVm 301
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTPHHPYTQALIRAIPdfgSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET- 308
|
330
....*....|....
gi 2075269590 302 PPLEAdADGHAAAC 315
Cdd:PRK15093 309 PRLTG-AKNHLYAC 321
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
29-234 |
6.99e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.22 E-value: 6.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDptSSLNPTM 108
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIgTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSV 188
Cdd:COG2884 95 TVYENVALPLRVTGK-SRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2075269590 189 QAGIVNLLLDLReEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVME 234
Cdd:COG2884 173 SWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-246 |
4.04e-47 |
|
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: 158.26 E-value: 4.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTSSL-NP 106
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---RRKVGLVFQNPDDQLfAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TmtVGA--AVG-EGLGVhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:COG1122 92 T--VEEdvAFGpENLGL----PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 184 LDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPR 246
Cdd:COG1122 165 LDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
28-236 |
5.87e-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: 157.30 E-value: 5.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDPtsSLNPT 107
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERRNIGMVFQDY--ALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03259 87 LTVAENIAFGLKLRGVP-KAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
28-231 |
4.38e-46 |
|
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: 153.88 E-value: 4.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtGRQLGPVRRRMQAVFQDPtsSLNPT 107
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVgaavgeglgvhrigtradraervaamLDRVGLPrgtaqnypgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03229 91 LTV--------------------------LENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGR 231
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
4.63e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.02 E-value: 4.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKsppwrpplvlHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDR 80
Cdd:COG1121 3 MMPAIELENLTVSYGGR----------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 ltgrqlgpVRRRMQAVFQDPTSSLNPTMTVGAAVGEGL----GVHRIGTRADRaERVAAMLDRVGLpRGTAQNYPGALSG 156
Cdd:COG1121 73 --------ARRRIGYVPQRAEVDWDFPITVRDVVLMGRygrrGLFRRPSRADR-EAVDEALERVGL-EDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 157 GQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLyLGRVMETG 236
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHG 220
|
....*....
gi 2075269590 237 RTADVFAAP 245
Cdd:COG1121 221 PPEEVLTPE 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-241 |
4.80e-46 |
|
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: 156.19 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDPtsSLNPT 107
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEG-LGVHRIG-------TRADRaERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:cd03256 93 LSVLENVLSGrLGRRSTWrslfglfPKEEK-QRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-257 |
1.19e-45 |
|
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: 155.37 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQA------VFQDPTS 102
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLMrtewgfVHQNPRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTMTVGAAVGEGLgvHRIGTRADRAERVAAM--LDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:TIGR02323 98 GLRMRVSAGANIGERL--MAIGARHYGNIRATAQdwLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAV 257
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
28-241 |
1.31e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.84 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgrQLGPVRRRMQAVFQDPtsSLNPT 107
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVRRRIGYVPQEP--ALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIgTRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:COG1131 88 LTVRENLRFFARLYGL-PRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 188 VQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG1131 166 ARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
30-257 |
2.95e-45 |
|
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: 154.43 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTSSLNptMT 109
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARRIAYVPQEPPAPFG--LT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEG----LGVHRIGTRADRaERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:COG1120 92 VRELVALGryphLGLFGRPSAEDR-EAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFaaprhpyTRALLDAV 257
Cdd:COG1120 170 LAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-------TPELLEEV 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
29-231 |
4.05e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 152.62 E-value: 4.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTSSL-NPT 107
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKVGLVFQNPDDQFfGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVG-EGLGVhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:cd03225 93 VEEEVAFGlENLGL----PEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2075269590 187 SVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGR 231
Cdd:cd03225 168 AGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-246 |
5.79e-44 |
|
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: 150.28 E-value: 5.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpVRRRMQAVFQDPtsSLNP 106
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGIGRTFQIP--RLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTV------GAAVGEGLGVHRIGTRADRA---ERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIA 177
Cdd:cd03219 89 ELTVlenvmvAAQARTGSGLLLARARREERearERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 178 DEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPR 246
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
28-241 |
1.04e-42 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 147.44 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDptSSLNPT 107
Cdd:TIGR02315 16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIGMIFQH--YNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEG-LGVH----RIGTRADRAERVAAM--LDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:TIGR02315 94 LTVLENVLHGrLGYKptwrSLLGRFSEEDKERALsaLERVGL-ADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:TIGR02315 173 IASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-227 |
3.74e-41 |
|
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: 142.29 E-value: 3.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgrqlgpVRRRMQAVFQdpTSSLNPT 107
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--------ERKRIGYVPQ--RRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 M--TVGAAVGEGL----GVHRIGTRADRaERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:cd03235 83 FpiSVRDVVLMGLyghkGLFRRLSKADK-AKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-254 |
4.40e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.97 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 34 SFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDptSSLNPTMTVGAA 113
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PAERPVSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 114 VGegLGVH---RIgTRADRAeRVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:COG3840 92 IG--LGLRpglKL-TAEQRA-QVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 191 GIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALL 254
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
28-238 |
2.94e-40 |
|
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: 140.39 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPI-----SSGEVHFAGRRIDRLTGRQLGpVRRRMQAVFQDPts 102
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLE-LRRRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 slNP-TMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQN-YPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRT 238
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
29-256 |
4.67e-40 |
|
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: 140.51 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrltgRQLGPV--RRRMQAVFQDptSSLNP 106
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-----REQDPVelRRKIGYVIQQ--IGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVG---AAVGEGLGVhrigTRADRAERVAAMLDRVGL-PRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:cd03295 89 HMTVEeniALVPKLLKW----PKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDA 256
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
31-232 |
6.74e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.18 E-value: 6.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTssLnPTMTV 110
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQVAYVPQEPA--L-WGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 GAAVGEGLgvhRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:COG4619 91 RDNLPFPF---QLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2075269590 191 GIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
27-232 |
4.26e-39 |
|
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: 137.28 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrLTGRQLGPVRRRMQAVFQDPTssLNP 106
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVGMVFQQFN--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLgVHRIGTRADRAERVA-AMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03262 90 HLTVLENITLAP-IKVKGMSKAEAEERAlELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2075269590 186 VSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:cd03262 168 PELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-256 |
4.59e-38 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 135.60 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP----ISSGEVHFAGRRIdrltgrQLGPVRRRMQA-VFQDPTSSL 104
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPV------APCALRGRKIAtIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVGAAVGEGLgvhRIGTRADRAERVAAMLDRVGL--PRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:PRK10418 93 NPLHTMHTHARETC---LALGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDA 256
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-245 |
5.38e-38 |
|
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: 138.31 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI-DRLTGRQLGPVRRRMQAVFQDPtsSLNPTMTVG 111
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQEA--RLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGEGLGVHRIGTRADRAERVAAM------LDRvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:COG4148 96 GNLLYGRKRAPRAERRISFDEVVELlgighlLDR----------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-247 |
7.93e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.51 E-value: 7.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDPtsSLNPT 107
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP-----PKDRNIAMVFQSY--ALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIgTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:COG3839 90 MTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRH 247
Cdd:COG3839 168 LRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
27-239 |
3.18e-37 |
|
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: 132.94 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLgravLRLL-----PiSSGEVHFAGRRIDRLTGRQLGPVRRR-MQAVFQDp 100
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTL----LGLLagldrP-TSGTVRLAGQDLFALDEDARARLRARhVGFVFQS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 tSSLNPTMTVGAAVG---EGLGvhrigtRADRAERVAAMLDRVGL-PRgtAQNYPGALSGGQRQRVGIARALIVAPDLLI 176
Cdd:COG4181 99 -FQLLPTLTALENVMlplELAG------RRDARARARALLERVGLgHR--LDHYPAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 177 ADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTA 239
Cdd:COG4181 170 ADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-249 |
3.37e-37 |
|
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: 136.01 E-value: 3.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI-DRLTGRQLGPVRRRMQAVFQDptSSLNPTMTVG 111
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGEGLGVHRIGTRADRAERVAAMLDRVGLprgtAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAG 191
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERVIELLGIGHL----LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 192 IVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPY 249
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
28-231 |
4.33e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.06 E-value: 4.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQdptsslnpt 107
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 mtvgaavgeglgvhrigtradraervaamldrvglprgtaqnypgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2075269590 188 VQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGR 231
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
30-236 |
5.92e-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: 130.25 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQdptsslnptmt 109
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 vgaavgeglgvhrigtradraervaaMLDRVGLPRGTAQNYpGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPF-NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2075269590 190 AGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-243 |
1.17e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.83 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqLGPVRRRMQAVFQDPTSSLnptm 108
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET---VWDVRRQVGMVFQNPDNQF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 tVGAAVGE--GLGVHRIGT-RADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:PRK13635 95 -VGATVQDdvAFGLENIGVpREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRhFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
28-245 |
1.20e-36 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 131.21 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrltgRQLGPVRRRMQAVFQDptSSLNPT 107
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPVNTVFQN--YALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03300 87 LTVFENIAFGLRLKKLP-KAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-231 |
2.06e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 128.65 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 22 RPPLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPT 101
Cdd:cd03228 13 RPKPVLK---DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKNIAYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 sslnptmtvgaavgeglgvhrigtradraervaamldrvgLPRGT-AQNYpgaLSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:cd03228 87 ----------------------------------------LFSGTiRENI---LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHfCDRVMVLYLGR 231
Cdd:cd03228 124 TSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-180 |
2.35e-36 |
|
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: 127.76 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTssLNPTMT 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 110 VGAAVGEGLGVHRIGTRA--DRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREkdARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
29-249 |
3.90e-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: 130.15 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQlgpvrRRMQAVFQDptSSLNPTM 108
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFVFQH--YALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGTRADRAE---RVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03296 90 TVFDNVAFGLRVKPRSERPPEAEiraKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPY 249
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-243 |
1.06e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 129.86 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrrIDRLTGRQLGPVRRRMQAVFQDPTSSLnptm 108
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVFQNPDNQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 tVGAAV------G-EGLGVHRIGTRadraERVAAMLDRVGLprgtaQNY----PGALSGGQRQRVGIARALIVAPDLLIA 177
Cdd:TIGR04520 91 -VGATVeddvafGlENLGVPREEMR----KRVDEALKLVGM-----EDFrdrePHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 178 DEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVrHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
28-232 |
2.77e-35 |
|
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: 125.97 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrltGRQLGPVRRRMQAVFQDPtsSLNPT 107
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIGYLPEEP--SLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVgaavgeglgvhrigtradraervAAMLDrvglprgtaqnypgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03230 88 LTV-----------------------RENLK---------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2075269590 188 VQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
29-249 |
3.95e-34 |
|
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: 131.88 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrltgRQLGP--VRRRMQAVFQDPT---SS 103
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-----RQIDPasLRRQIGVVLQDVFlfsGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 L-------NPTMTVGAavgeglgVHRIGTRADRAERVAAM---LDRVGLPRGTAqnypgaLSGGQRQRVGIARALIVAPD 173
Cdd:COG2274 565 IrenitlgDPDATDEE-------IIEAARLAGLHDFIEALpmgYDTVVGEGGSN------LSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 174 LLIADEAVSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAAPRHPY 249
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-250 |
4.77e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.03 E-value: 4.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLL-----PISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTSSl 104
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIEL---RRRVQMVFQIPNPI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 nPTMTVGAAVGEGLGVHRI-GTRADRAERVAAML----------DRVGLPrgtaqnyPGALSGGQRQRVGIARALIVAPD 173
Cdd:PRK14247 95 -PNLSIFENVALGLKLNRLvKSKKELQERVRWALekaqlwdevkDRLDAP-------AGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 174 LLIADEAVSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYT 250
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-241 |
2.01e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 122.54 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpVRRRMQAVFQDPtsSLNP 106
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGR--RIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTvgaaVGEGLgvhRIGTRADRAERVAAMLDRV-GL-PR-GTAQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:cd03224 89 ELT----VEENL---LLGAYARRRAKRKARLERVyELfPRlKERRKQLaGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-232 |
2.21e-33 |
|
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: 122.02 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVaPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI-DRLTGRQLGPVRRRMQAVFQDptSSLNPTMTVG 111
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQRKIGLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGEGLGVHRigtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAG 191
Cdd:cd03297 94 ENLAFGLKRKR---NREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2075269590 192 IVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-255 |
2.87e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 26 VLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRID--RLTGRQLGPVRRRMQA---VFQDp 100
Cdd:PRK11264 18 VLH---GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtaRSLSQQKGLIRQLRQHvgfVFQN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 tSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:PRK11264 94 -FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMgLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLD 255
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
4.03e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 123.05 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 3 ALLDVNDLGVEFrlksPPWRPPLvlHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrlt 82
Cdd:COG4525 2 SMLTVRHVSVRY----PGGGQPQ--PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 83 grqlGPVRRRmQAVFQDptSSLNPTMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRV 162
Cdd:COG4525 73 ----GPGADR-GVVFQK--DALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 163 GIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLD 215
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
28-241 |
4.37e-33 |
|
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: 122.27 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRqlgpVRRRMQAVFQDPtsSLNPT 107
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARRQIGVLPDER--GLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTV-------GAAVGEglgvhrigTRADRAERVAAMLDRVGLPRGTAQNYpGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:COG4555 89 LTVreniryfAELYGL--------FDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
30-254 |
4.39e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.77 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTG----------RQLGPVRRRMQAVFQD 99
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 100 ptSSLNPTMTVGAAVGEGlGVHRIG-TRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:PRK10619 101 --FNLWSHMTVLENVMEA-PIQVLGlSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALL 254
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-245 |
9.60e-33 |
|
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: 121.29 E-value: 9.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDptSSLNPTMT 109
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-----PEKRDISYVPQN--YALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEGLgVHRIGTRADRAERVAAMLDRVG----LPRgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03299 88 VYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGidhlLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-252 |
1.60e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLR---LLPIS--SGEVHFAGRRIdrlTGRQLGPV--RRRMQAVFQDP 100
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGArvEGEILLDGEDI---YDPDVDVVelRRRVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 tsslNP-TMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLP---------RGTAqnypgaLSGGQRQRVGIARALIV 170
Cdd:COG1117 102 ----NPfPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWdevkdrlkkSALG------LSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 171 APDLLIADEAVSALD-VSVQAgIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPY 249
Cdd:COG1117 172 EPEVLLMDEPTSALDpISTAK-IEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKR 248
|
...
gi 2075269590 250 TRA 252
Cdd:COG1117 249 TED 251
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-241 |
2.31e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.75 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLG--PVRRrmqavfqdptsSLN 105
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGylPEER-----------GLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMTVGAAV---GE--GLgvhrigTRADRAERVAAMLDRVGLprGTAQNYP-GALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:COG4152 84 PKMKVGEQLvylARlkGL------SKAEAKRRADEWLERLGL--GDRANKKvEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 180 AVSALD-VSVQAgIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG4152 156 PFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
33-245 |
8.64e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRaVLRLLPI-SSGEVHFAGRRID---RLTGRQLGPVRRRMQAVFQDptSSLNPTM 108
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLR-VLNLLETpDSGQLNIAGHQFDfsqKPSEKAIRLLRQKVGMVFQQ--YNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEG----LGVhrigTRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:COG4161 98 TVMENLIEApckvLGL----SKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 185 DVSVQAGIVNLLLDLrEEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGrTADVFAAP 245
Cdd:COG4161 173 DPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-242 |
9.39e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.06 E-value: 9.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGpvRRRmqAVF-QDptSSLNPTM 108
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA--RRR--AVLpQH--SSLAFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGTRADRaERVAAMLDRVGLPRGTAQNYPgALSGGQRQRVGIARAL--IVAPD-----LLIADEAV 181
Cdd:COG4559 91 TVEEVVALGRAPHGSSAAQDR-QIVREALALVGLAHLAGRSYQ-TLSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:COG4559 169 SALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
29-237 |
1.57e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 123.74 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPT--Sslnp 106
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFlfS---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 tMTVGAAVgeglgvhRIG-TRADRAE-----RVAAMLDRV-GLP---------RGTAqnypgaLSGGQRQRVGIARALIV 170
Cdd:COG1132 428 -GTIRENI-------RYGrPDATDEEveeaaKAAQAHEFIeALPdgydtvvgeRGVN------LSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 171 APDLLIADEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGR 237
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-224 |
1.63e-31 |
|
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: 117.54 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSppwRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGE--VHFAGRRI 78
Cdd:COG4778 1 MTTLLEVENLSKTFTLHL---QGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 79 D--RLTGRQLGPVRRR-MQAVFQdptsSLN-----PTMTVgaaVGEGLgVHRiGTRADRA-ERVAAMLDRVGLPRGTAQN 149
Cdd:COG4778 78 DlaQASPREILALRRRtIGYVSQ----FLRviprvSALDV---VAEPL-LER-GVDREEArARARELLARLNLPERLWDL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 150 YPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRV 224
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-232 |
1.71e-31 |
|
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: 117.12 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 23 PPLVLhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDptS 102
Cdd:cd03292 11 PNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTMTVGAAVGEGLGVHRIGTRaDRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:cd03292 88 RLLPDRNVYENVAFALEVTGVPPR-EIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2075269590 183 ALDVSVQAGIVNLLLDLrEEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:cd03292 166 NLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-236 |
4.53e-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: 116.32 E-value: 4.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRqlgpVRRRMQAVFQDPtsSLNPTM 108
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRIGIVFQDL--SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGaavgEGLGVH-RIG--TRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03265 89 TGW----ENLYIHaRLYgvPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-257 |
5.56e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.14 E-value: 5.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQA-VFQdpTSSLNPT 107
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAmVFQ--SFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGTrADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:PRK10070 121 MTVLDNTAFGMELAGINA-EERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYTRALLDAV 257
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-257 |
8.31e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKSPPWRPPLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI--DRLTGRQlgpV 89
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLH---NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERL---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 90 RRRMQAVFQDptSSLNPTMTVGAAVGEGlGVHRIGTRADRAERVA-AMLDRVGLpRGTAQNYPGALSGGQRQRVGIARAL 168
Cdd:PRK09493 76 RQEAGMVFQQ--FYLFPHLTALENVMFG-PLRVRGASKEEAEKQArELLAKVGL-AERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 169 IVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHP 248
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
....*....
gi 2075269590 249 YTRALLDAV 257
Cdd:PRK09493 231 RLQEFLQHV 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
28-236 |
9.73e-31 |
|
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: 115.04 E-value: 9.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrQLGPVRRRMQAVFQDptSSLNPT 107
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKDRDIAMVFQN--YALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGTRA--DRAERVAAMLDRVGLprgtAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEidERVREVAELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 186 VSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03301 163 AKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
33-245 |
1.30e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.88 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRaVLRLLPI-SSGEVHFAGRRIDRLT------GRQLgpvRRRMQAVFQDptSSLN 105
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMpRSGTLNIAGNHFDFSKtpsdkaIREL---RRNVGMVFQQ--YNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMTVGAAVGEG----LGVhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:PRK11124 95 PHLTVQQNLIEApcrvLGL----SKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 182 SALDVSVQAGIVNLLLDLReEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGrTADVFAAP 245
Cdd:PRK11124 170 AALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQP 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
28-246 |
1.40e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 115.46 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgrqlgPVRRRMQA----------VF 97
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL------PPHRIARLgigyvpegrrIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 98 qdptsslnPTMTV------GAAVGEGlgvhRIGTRADRAE------RVAAMLDRVGlprgtaqnypGALSGGQRQRVGIA 165
Cdd:COG0410 91 --------PSLTVeenlllGAYARRD----RAEVRADLERvyelfpRLKERRRQRA----------GTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 166 RALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
.
gi 2075269590 246 R 246
Cdd:COG0410 228 E 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
33-255 |
1.84e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.88 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQlgpvrRRMQAVFQDptSSLNPTMTVGA 112
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVGFVFQH--YALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 113 AVGEGLGVHRIGTRADRAE---RVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:PRK10851 94 NIAFGLTVLPRRERPNAAAikaKVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 190 AGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFaapRHPYTRALLD 255
Cdd:PRK10851 173 KELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW---REPATRFVLE 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-215 |
2.55e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.12 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP---ISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDPTssLNP 106
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALP-----AEQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLgVHRIGtRADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:COG4136 90 HLSVGENLAFAL-PPTIG-RAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*....
gi 2075269590 187 SVQAGIVNLLLDLREEMGLAMLFIAHDLD 215
Cdd:COG4136 167 ALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
31-237 |
3.67e-30 |
|
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: 114.25 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqLGPVRRRMQAVFQDpTSSLNPTM-- 108
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAIGVVPQD-TVLFNDTIgy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 -----TVGAAVGEglgVHRIGTRADRAERVAAMLD----RVGlPRGTAqnypgaLSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:cd03253 94 nirygRPDATDEE---VIEAAKAAQIHDKIMRFPDgydtIVG-ERGLK------LSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGR 237
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-245 |
9.41e-30 |
|
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: 115.28 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 45 VVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrQLGPVRRRMQAVFQdpTSSLNPTMTVGAAVGEGLGVHRIG 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQ--SYALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 125 tRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMG 204
Cdd:TIGR01187 74 -RAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2075269590 205 LAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-243 |
1.25e-29 |
|
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: 117.98 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 26 VLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHF--AGRRID----RLTGRqlGPVRRRMQAVFQD 99
Cdd:TIGR03269 296 VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDmtkpGPDGR--GRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 100 ptSSLNPTMTVGAAVGEGLGVHRIGTRADRaeRVAAMLDRVGLPRGTAQN----YPGALSGGQRQRVGIARALIVAPDLL 175
Cdd:TIGR03269 374 --YDLYPHRTVLDNLTEAIGLELPDELARM--KAVITLKMVGFDEEKAEEildkYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-244 |
1.30e-29 |
|
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: 112.96 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 11 GVEFRLKSPPwrpPLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvR 90
Cdd:cd03252 5 HVRFRYKPDG---PVILD---NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 91 RRMQAVFQDPTSsLNPTMTVGAAVG-EGLGVHRIGTRADRAERVAAMLDrvgLPRG--TAQNYPGA-LSGGQRQRVGIAR 166
Cdd:cd03252 76 RQVGVVLQENVL-FNRSIRDNIALAdPGMSMERVIEAAKLAGAHDFISE---LPEGydTIVGEQGAgLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 167 ALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-236 |
2.07e-29 |
|
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: 111.82 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKSPPWRPPLVLhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRR 91
Cdd:cd03244 3 IEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 92 RMQAVFQDPT-------SSLNPtmtvgaavgegLGVHrigtrADraERVAAMLDRVGLpRGTAQNYPGAL---------- 154
Cdd:cd03244 79 RISIIPQDPVlfsgtirSNLDP-----------FGEY-----SD--EELWQALERVGL-KEFVESLPGGLdtvveeggen 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 155 -SGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLlldLREEM-GLAMLFIAHDLDVVRHfCDRVMVLYLGRV 232
Cdd:cd03244 140 lSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
....
gi 2075269590 233 METG 236
Cdd:cd03244 216 VEFD 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-243 |
2.76e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLgvEFRLKSPPWRPPLvlhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrriDR 80
Cdd:PRK13650 1 MSNIIEVKNL--TFKYKEDQEKYTL-----NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRRMQAVFQDPTSSLnptmtVGAAVGE--GLGVHRIG-TRADRAERVAAMLDRVGLprgtaQNY----PGA 153
Cdd:PRK13650 71 LTEENVWDIRHKIGMVFQNPDNQF-----VGATVEDdvAFGLENKGiPHEEMKERVNEALELVGM-----QDFkerePAR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRhFCDRVMVLYLGRVM 233
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVE 219
|
250
....*....|
gi 2075269590 234 ETGRTADVFA 243
Cdd:PRK13650 220 STSTPRELFS 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-250 |
5.11e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.86 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIS-----SGEVHFAGRRIdrlTGRQLGP--VRRRMQAVFQDP 100
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI---YSPDVDPieVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 TSSlnPTMTVGAAVGEGLGVHR-IGTRADRAERV------AAMLDRVglpRGTAQNYPGALSGGQRQRVGIARALIVAPD 173
Cdd:PRK14267 95 NPF--PHLTIYDNVAIGVKLNGlVKSKKELDERVewalkkAALWDEV---KDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 174 LLIADEAVSALDVSVQAGIVNLLLDLREEmgLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYT 250
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
29-244 |
5.13e-29 |
|
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: 116.40 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTsslnptm 108
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPY------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLgvhRIGTRADRAERVAAMLDRVG-------LPRG-------TAQNypgaLSGGQRQRVGIARALIVAPDL 174
Cdd:COG4988 422 LFAGTIRENL---RLGRPDASDEELEAALEAAGldefvaaLPDGldtplgeGGRG----LSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 175 LIADEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
30-242 |
9.44e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGpvRRRmqAVF-QdpTSSLNPTM 108
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA--RRR--AVLpQ--HSSLSFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGTRADRAErVAAMLDRVGLPRGTAQNYPgALSGGQRQRVGIARAL--IVAPD----LLIADEAVS 182
Cdd:PRK13548 92 TVEEVVAMGRAPHGLSRAEDDAL-VAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13548 170 ALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
28-236 |
2.44e-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: 108.84 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDPtsSLNPT 107
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-----EALRRIGALIEAP--GFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGaavgEGLGVHR--IGTRADRAERVaamLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03268 87 LTAR----ENLRLLArlLGIRKKRIDEV---LDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 186 VSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03268 159 PDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-215 |
2.95e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.79 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrqlGPVRRRmQAVFQDptSSLNPTM 108
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-------GPGAER-GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSV 188
Cdd:PRK11248 86 NVQDNVAFGLQLAGVE-KMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*..
gi 2075269590 189 QAGIVNLLLDLREEMGLAMLFIAHDLD 215
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-232 |
5.25e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDPTSSLNPT 107
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 --------MTVGAAVGEglgvhrigtraDRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK10908 96 vydnvaipLIIAGASGD-----------DIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLrEEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
28-243 |
5.77e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrLTGRQLGPVRRRMQAVFQDPTSSLnpt 107
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPDNQL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 mtVGAAVGEGL--GVHRIGTRADRA-ERVAAMLDRVGLPRgtAQNYPG-ALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:PRK13636 96 --FSASVYQDVsfGAVNLKLPEDEVrKRVDNALKRTGIEH--LKDKPThCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 184 LDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-232 |
7.39e-28 |
|
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: 106.75 E-value: 7.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 26 VLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpVRRRMQAVFQDP-TSSL 104
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVPEDRkREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVGaavgeglgvhrigtradraervaamlDRVGLPRGtaqnypgaLSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:cd03215 90 VLDLSVA--------------------------ENIALSSL--------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2075269590 185 DVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:cd03215 136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-236 |
1.72e-27 |
|
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: 106.68 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPPwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrrIDrlTG 83
Cdd:cd03266 1 MITADALTKRFRDVKKT------VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FD--VV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 84 RQLGPVRRRMQAVFQdpTSSLNPTMTVGAAVGEGLGVHRIGTRADRAeRVAAMLDRVGLpRGTAQNYPGALSGGQRQRVG 163
Cdd:cd03266 71 KEPAEARRRLGFVSD--STGLYDRLTARENLEYFAGLYGLKGDELTA-RLEELADRLGM-EELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 164 IARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
28-241 |
2.04e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 106.84 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpVRRRMQAVFQDptSSLNPT 107
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAYVPQG--REIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGTRADRAERVA------AMLDRVGlprgtaqnypGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSRKIPDEIYElfpvlkEMLGRRG----------GDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-236 |
2.27e-27 |
|
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: 106.42 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 34 SFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrrIDRLTgrqLGPVRRRMQAVFQDptSSLNPTMTVGAA 113
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTA---APPADRPVSMLFQE--NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 114 VGEGLgVHRIGTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIV 193
Cdd:cd03298 91 VGLGL-SPGLKLTAEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2075269590 194 NLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-236 |
2.49e-27 |
|
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: 106.54 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPT------ 101
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMIGVVLQDTFlfsgti 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 ------SSLNPTMTVGAAVGEGLGVHRIGtradraERVAAMLDRVGLPRGtaqnypGALSGGQRQRVGIARALIVAPDLL 175
Cdd:cd03254 94 menirlGRPNATDEEVIEAAKEAGAHDFI------MKLPNGYDTVLGENG------GNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETG 236
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
231-315 |
3.12e-27 |
|
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: 102.06 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 231 RVMETGRTADVFAAPRHPYTRALLDAVPRLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAACAEVMPPLEADADG 310
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*
gi 2075269590 311 HAAAC 315
Cdd:TIGR01727 81 HRVAC 85
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-208 |
5.67e-27 |
|
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: 104.87 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 3 ALLDVNDLGVEFRlksppwRPPLVlhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrlt 82
Cdd:COG4133 1 MMLEAENLSCRRG------ERLLF----SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 83 gRQLGPVRRRMQAVFQDPtsSLNPTMTvgaaVGEGLGVH-RIGTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQR 161
Cdd:COG4133 68 -DAREDYRRRLAYLGHAD--GLKPELT----VRENLRFWaALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRR 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2075269590 162 VGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAML 208
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-236 |
7.52e-27 |
|
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: 105.70 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 11 GVEFRLKSPPWRPPLvlhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvR 90
Cdd:cd03249 5 NVSFRYPSRPDVPIL-----KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 91 RRMQAVFQDPTssLNPTmTVGAAVGEGLGvHRIGTRADRAERVAAMLD-----------RVGlPRGTAqnypgaLSGGQR 159
Cdd:cd03249 77 SQIGLVSQEPV--LFDG-TIAENIRYGKP-DATDEEVEEAAKKANIHDfimslpdgydtLVG-ERGSQ------LSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 160 QRVGIARALIVAPDLLIADEAVSALDVS----VQAGIVNLLldlreeMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMET 235
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAEseklVQEALDRAM------KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
.
gi 2075269590 236 G 236
Cdd:cd03249 219 G 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-227 |
8.14e-27 |
|
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: 104.65 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgRQLgpvRRRMQAVFQDPTSSLNpTMT 109
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KER---RKSIGYVMQDVDYQLF-TDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEGLGvhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:cd03226 89 VREELLLGLK-----ELDAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 2075269590 190 AGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:cd03226 163 ERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
35-241 |
9.84e-27 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 104.93 E-value: 9.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 35 FTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRiDRLTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAV 114
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-PGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 115 gegLGVHRIGTRADRAErVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVN 194
Cdd:TIGR03771 80 ---IGWLRRPCVADFAA-VRDALRRVGLTE-LADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2075269590 195 LLLDLREEmGLAMLFIAHDLDVVRHFCDRVmVLYLGRVMETGRTADV 241
Cdd:TIGR03771 155 LFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-247 |
1.10e-26 |
|
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: 104.86 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgrqlgPVRRRMqAVFQDptSSLNPTMT 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-------PGPDRM-VVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGegLGVHRIGTRADRAER---VAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:TIGR01184 71 VRENIA--LAVDRVLPDLSKSERraiVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 187 SVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV-FAAPRH 247
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-236 |
1.89e-26 |
|
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: 103.90 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLG--PVRRrmqavfqdptsSLNP 106
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylPEER-----------GLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGA-----AVGEGLGVHRIGTRADRaervaaMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:cd03269 84 KMKVIDqlvylAQLKGLKKEEARRRIDE------WLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-241 |
2.08e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT---GRQLGpvrrrMQAVFQDPtsSL 104
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAAG-----IAIIHQEL--NL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVGAAVGEGLGVHRIGTRADRA--ERVAAMLDRVGL---PRGTAqnypGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:COG1129 91 VPNLSVAENIFLGREPRRGGLIDWRAmrRRARELLARLGLdidPDTPV----GDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG1129 167 PTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-244 |
2.42e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.39 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPPWR------------PPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISS 68
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSRslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 69 GEVHfagrridrltgrqlgpVRRRMQAVFqDPTSSLNPTMTV------GAAVgegLGVhrigTRADRAERVAAMLDRVGL 142
Cdd:COG1134 81 GRVE----------------VNGRVSALL-ELGAGFHPELTGreniylNGRL---LGL----SRKEIDEKFDEIVEFAEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 143 prGTAQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFC 221
Cdd:COG1134 137 --GDFIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLC 213
|
250 260
....*....|....*....|...
gi 2075269590 222 DRVMVLYLGRVMETGRTADVFAA 244
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-241 |
3.99e-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: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVefrlksppwRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTG 83
Cdd:COG3845 257 VLEVENLSV---------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 84 RQlgpvRRRMQAVF--QDP-TSSLNPTMTV----------GAAVGEGlGVHRIGTRADRAERVAAMLD-RVGLPRGTAqn 149
Cdd:COG3845 328 RE----RRRLGVAYipEDRlGRGLVPDMSVaenlilgryrRPPFSRG-GFLDRKAIRAFAEELIEEFDvRTPGPDTPA-- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 150 ypGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYL 229
Cdd:COG3845 401 --RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYE 477
|
250
....*....|..
gi 2075269590 230 GRVMETGRTADV 241
Cdd:COG3845 478 GRIVGEVPAAEA 489
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-246 |
4.18e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.85 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRLKSppwrpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGR 84
Cdd:PRK09536 4 IDVSDLSVEFGDTT----------VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 QLGpvrRRMQAVFQDPTSSLNptMTVGAAVGEGLGVHR----IGTRADRAERVAAMlDRVGLPRGTAQNYPgALSGGQRQ 160
Cdd:PRK09536 74 AAS---RRVASVPQDTSLSFE--FDVRQVVEMGRTPHRsrfdTWTETDRAAVERAM-ERTGVAQFADRPVT-SLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 161 RVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTAD 240
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
....*.
gi 2075269590 241 VFAAPR 246
Cdd:PRK09536 226 VLTADT 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-243 |
4.60e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.40 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSPpwrpplvLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrriDR 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESD-------VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---EL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRRMQAVFQDPTSSLnptmtVGAAV---------GEGLGVHRIGTRADRAERVAAMLDrvglprgTAQNYP 151
Cdd:PRK13642 71 LTAENVWNLRRKIGMVFQNPDNQF-----VGATVeddvafgmeNQGIPREEMIKRVDEALLAVNMLD-------FKTREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 152 GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGR 231
Cdd:PRK13642 139 ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGE 217
|
250
....*....|..
gi 2075269590 232 VMETGRTADVFA 243
Cdd:PRK13642 218 IIKEAAPSELFA 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-244 |
6.25e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 107.88 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKSPPWrPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRR 91
Cdd:TIGR02203 331 VEFRNVTFRY-PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---RR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 92 RMQAVFQDPTSsLNPTMTVGAAVGEGLGVHRigTRADRAERVAAMLDRV-GLPRGTAQNY---PGALSGGQRQRVGIARA 167
Cdd:TIGR02203 407 QVALVSQDVVL-FNDTIANNIAYGRTEQADR--AEIERALAAAYAQDFVdKLPLGLDTPIgenGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 168 LIVAPDLLIADEAVSALDVS----VQAGIVNLLldlreeMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFA 243
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNEserlVQAALERLM------QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
.
gi 2075269590 244 A 244
Cdd:TIGR02203 557 R 557
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-242 |
9.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 9.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrlTGRQLGPVRRRMQAVFQDPTSSLNPTmTVGA 112
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQNPDNQFVGS-IVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 113 AVGEGLGVHRIGTRaDRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGI 192
Cdd:PRK13648 104 DVAFGLENHAVPYD-EMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2075269590 193 VNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13648 182 LDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-235 |
9.89e-26 |
|
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: 100.58 E-value: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQlgPVRRRMQAVFQdptsslnpt 107
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARRAGIAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 mtvgaavgeglgvhrigtradraervaamldrvglprgtaqnypgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03216 83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2075269590 188 VQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMET 235
Cdd:cd03216 117 EVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
12-243 |
1.22e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 107.14 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKspPWRPPLVlhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrRIDRLTGRQLGPV-- 89
Cdd:TIGR01846 461 IRFRYA--PDSPEVL----SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV-----LVDGVDLAIADPAwl 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 90 RRRMQAVFQDptsslnpTMTVGAAVGEGLGVHRIGTRADR---AERVAAMLDRV-GLPRGTAQ---NYPGALSGGQRQRV 162
Cdd:TIGR01846 530 RRQMGVVLQE-------NVLFSRSIRDNIALCNPGAPFEHvihAAKLAGAHDFIsELPQGYNTevgEKGANLSGGQRQRI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 163 GIARALIVAPDLLIADEAVSALDVSVQAGIVNlllDLRE-EMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADV 241
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDYESEALIMR---NMREiCRGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
..
gi 2075269590 242 FA 243
Cdd:TIGR01846 679 LA 680
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-250 |
2.62e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.05 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPI------SSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTSS 103
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 lnPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTAQ--NYPGA-LSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDrlNSPASqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYT 250
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-237 |
3.06e-25 |
|
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: 100.56 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRLKSPPwrpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgr 84
Cdd:cd03369 7 IEVENLSVRYAPDLPP--------VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 QLGPVRRRMQAVFQDPT-------SSLNPTmtvgaavgeglgvhrigTRADRAERVAAMldRVglpRGTAQNypgaLSGG 157
Cdd:cd03369 76 PLEDLRSSLTIIPQDPTlfsgtirSNLDPF-----------------DEYSDEEIYGAL--RV---SEGGLN----LSQG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 158 QRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLlldLREEM-GLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETG 236
Cdd:cd03369 130 QRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT---IREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
.
gi 2075269590 237 R 237
Cdd:cd03369 206 H 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-245 |
5.62e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.31 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrLTGRQLGPVRRRMQAVFQDPTSSL-NPT 107
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPDDQLfAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGE-GLGVhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:PRK13639 96 VEEDVAFGPlNLGL----SKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 187 SVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK13639 171 MGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
29-255 |
1.42e-24 |
|
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: 103.69 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDP----TSsl 104
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRRIAVVPQRPhlfdTT-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 nptmtvgaaVGEGLgvhRIGtrADRA--ERVAAMLDRVGLpRGTAQNYPG-----------ALSGGQRQRVGIARALIVA 171
Cdd:COG4987 425 ---------LRENL---RLA--RPDAtdEELWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 172 PDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLamLFIAHDLDVVRHFcDRVMVLYLGRVMETGRTADVFAapRHPYTR 251
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA--QNGRYR 564
|
....
gi 2075269590 252 ALLD 255
Cdd:COG4987 565 QLYQ 568
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-245 |
1.87e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.49 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRR-IDRLTGRQLGPVRRRMQAVFQDptSSLNPTMTVG 111
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQD--ARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGEGLgvhrigTRADRAE--RVAAML------DRvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:PRK11144 95 GNLRYGM------AKSMVAQfdKIVALLgiepllDR----------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 184 LDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-297 |
2.12e-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: 94.00 E-value: 2.12e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 233 METGRTADVFAAPRHPYTRALLDAVPRLVPTGEPRRLLAGDPPSPLAPPSGCVFRTRCPHAIAAC 297
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-232 |
4.37e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQ---LG----PVRRRMQAVFQDP 100
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGiayvPEDRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 TSSLNPTMTVGAAVGEGLGVHRigtradRAERVAA--MLDRVGL-PRGTAQNYpGALSGGQRQRVGIARALIVAPDLLIA 177
Cdd:COG1129 346 SIRENITLASLDRLSRGGLLDR------RRERALAeeYIKRLRIkTPSPEQPV-GNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 178 DEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-244 |
4.53e-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: 98.07 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDpTSSLNPTM 108
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---RRQIGLVSQD-VFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEglgvhRIGTRAD--RAERVAAMLDRV-GLPRGTAQNYP---GALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:cd03251 93 AENIAYGR-----PGATREEveEAARAANAHEFImELPEGYDTVIGergVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 183 ALDVS----VQAGIVNLLLDlReemglAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:cd03251 168 ALDTEserlVQAALERLMKN-R-----TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
30-218 |
5.58e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.96 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVR-RRMQAVFQdpTSSLNPTM 108
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLgvhRIG--TRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:PRK11629 103 TALENVAMPL---LIGkkKPAEINSRALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|..
gi 2075269590 187 SVQAGIVNLLLDLREEMGLAMLFIAHDLDVVR 218
Cdd:PRK11629 179 RNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-232 |
7.76e-24 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 95.75 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 11 GVEFRlksPPWRPPLVLhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrRIDRLTGRQLGPvr 90
Cdd:cd03246 5 NVSFR---YPGAEPPVL---RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLDGADISQWDP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 91 rrmqavfqdptsslnptmtvgaavgEGLGVHrigtradraerVAAMLDRVGLPRGT-AQNypgALSGGQRQRVGIARALI 169
Cdd:cd03246 72 -------------------------NELGDH-----------VGYLPQDDELFSGSiAEN---ILSGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 170 VAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHfCDRVMVLYLGRV 232
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
29-245 |
9.56e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 9.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSlgraVLRLLP----ISSGEVHFAGRRIDrltgrQLGPVRRRMQAVFQdpTSSL 104
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetPDSGRIMLDGQDIT-----HVPAENRHVNTVFQ--SYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVGAAVGEGLGVHRIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:PRK09452 98 FPHMTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 185 DVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-242 |
1.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrrIDrLTGRQ--LGPVRRRMQAVFQDPTSSL-N 105
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VD-ITDKKvkLSDIRKKVGLVFQYPEYQLfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMTVGAAVGE---GLGVHRIGTRADRAervaamLDRVGLPRGT-AQNYPGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:PRK13637 99 ETIEKDIAFGPinlGLSEEEIENRVKRA------MNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-242 |
2.51e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.98 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 23 PPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTS 102
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---RKKIGIIFQNPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLnptmtVGAAVGE----GLGVHRIgTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:PRK13632 95 QF-----IGATVEDdiafGLENKKV-PPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRhFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-237 |
2.62e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.04 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDP---TSSLN 105
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNIAVVFQDAglfNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMTVGAAVGEGLGVHRIGTRA---DRAERVAAMLDRVGLPRGtaqnypGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:PRK13657 427 DNIRVGRPDATDEEMRAAAERAqahDFIERKPDGYDTVVGERG------RQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 183 ALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGR 237
Cdd:PRK13657 501 ALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-250 |
2.78e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSppwrpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLR---LLP--ISSGEVHFAG 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPevTITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 76 RRI--DRLTGRQLgpvRRRMQAVFQDPtsslNP-TMTVGAAVGEGL---GV---HRIGTRADRAERVAAMLDRVglpRGT 146
Cdd:PRK14239 72 HNIysPRTDTVDL---RKEIGMVFQQP----NPfPMSIYENVVYGLrlkGIkdkQVLDEAVEKSLKGASIWDEV---KDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 147 AQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMV 226
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGF 219
|
250 260
....*....|....*....|....
gi 2075269590 227 LYLGRVMETGRTADVFAAPRHPYT 250
Cdd:PRK14239 220 FLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
28-251 |
2.88e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrQLGPVRRRMQAVFQdpTSSLNPT 107
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPINMMFQ--SYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIgTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:PRK11607 106 MTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFaapRHPYTR 251
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR 244
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
28-227 |
3.16e-23 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 94.99 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRR-RMQAVFQDptSSLNP 106
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRReKLGYLFQN--FALIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLgVHRIGTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:TIGR03608 90 NETVEENLDLGL-KYKKLSKKEKREKKKEALEKVGL-NLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2075269590 187 SVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHfCDRVMVL 227
Cdd:TIGR03608 168 KNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-244 |
3.86e-23 |
|
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: 99.44 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGP---------------VRRRMq 94
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhigylpqdvelfdgtIAENI- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 95 AVFQDPTSslnptmtvgAAVGEglgvhrigtrADRAERVAAMLDRvgLPRGtaqnY-------PGALSGGQRQRVGIARA 167
Cdd:COG4618 427 ARFGDADP---------EKVVA----------AAKLAGVHEMILR--LPDG----YdtrigegGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 168 LIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
24-236 |
4.30e-23 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 99.65 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLHavrGVSFTVAPREILGVVGESGSGKTSLgravLRLL-----PiSSGEVHFAGRRIDRLtgrQLGPVRRRMQAVFQ 98
Cdd:TIGR03797 466 PLILD---DVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfetP-ESGSVFYDGQDLAGL---DVQAVRRQLGVVLQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 99 DP---TSSLNPTMTVGAAVG--EGLGVHRigtRADRAERVAAMldRVGLPRGTAQNyPGALSGGQRQRVGIARALIVAPD 173
Cdd:TIGR03797 535 NGrlmSGSIFENIAGGAPLTldEAWEAAR---MAGLAEDIRAM--PMGMHTVISEG-GGTLSGGQRQRLLIARALVRKPR 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 174 LLIADEAVSALDVSVQAGIVNLLldlrEEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETG 236
Cdd:TIGR03797 609 ILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-245 |
5.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLR-LLPISSGEVHFAGRRIDrLTGRQLGPVRRRMQAVFQDPTSSLnpt 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKITVDGIT-LTAKTVWDIREKVGIVFQNPDNQF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 mtVGAAVGEGLGV---HRIGTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:PRK13640 98 --VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 185 DVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
45-245 |
5.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 45 VVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT-GRQLGPVRRRMQAVFQDPTSSL-NPTMTVGAAVG-EGLGVh 121
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKPLRKKVGIVFQFPEHQLfEETVEKDICFGpMNFGV- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 122 rigTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLRE 201
Cdd:PRK13634 117 ---SEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHK 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2075269590 202 EMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK13634 194 EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-245 |
7.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.05 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTG-RQLGPVRRRMQAVFQDPTSSLNPTmTVG 111
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLRKKVSLVFQFPEAQLFEN-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGegLGVHRIGTRADRAERVA-AMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:PRK13641 105 KDVE--FGPKNFGFSEDEAKEKAlKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 191 GIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK13641 183 EMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-242 |
8.41e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 8.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrrIDRLTGRQLGPVRRRMQAVFQDPTSSLNPTM 108
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TV-GAAVG-EGLGVHRIGTRadraERVAAMLDRVGLprgtaQNY----PGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:PRK13633 103 VEeDVAFGpENLGIPPEEIR----ERVDESLKKVGM-----YEYrrhaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-244 |
1.17e-22 |
|
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: 98.35 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDpTSSLNPTmtv 110
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQD-TVLFNDT--- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 gaaVGEGLGVHRIG-TRAD--RAERVAAMLDRV-GLP---------RGTAqnypgaLSGGQRQRVGIARALIVAPDLLIA 177
Cdd:COG5265 448 ---IAYNIAYGRPDaSEEEveAAARAAQIHDFIeSLPdgydtrvgeRGLK------LSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 178 DEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
28-236 |
1.52e-22 |
|
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: 93.34 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgRQLGPVRRRMQAVFQDPTssLNPT 107
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQSLGYCPQFDA--LFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTvgaaVGEGLGVH-RI--GTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:cd03263 90 LT----VREHLRFYaRLkgLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 185 DVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03263 165 DPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-250 |
2.64e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLL-PIS----SGEVHFAGRRIdrLTGRQLGPVRRRMQAVFQDPtsslNP- 106
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSgyrySGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRP----NPf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGL---PRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 184 LDVSVQAGIVNLLLDLREEmgLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPRHPYT 250
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-246 |
2.99e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.52 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRlksppwrpplVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDR 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFG----------GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQ---LGPVRrrmqaVFQDptSSLNPTMTVGaavgEGLGV--HR----------IGT----RADRA--ERVAAMLDR 139
Cdd:PRK11300 72 LPGHQiarMGVVR-----TFQH--VRLFREMTVI----ENLLVaqHQqlktglfsglLKTpafrRAESEalDRAATWLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 140 VGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRH 219
Cdd:PRK11300 141 VGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMG 219
|
250 260
....*....|....*....|....*..
gi 2075269590 220 FCDRVMVLYLGRVMETGRTADVFAAPR 246
Cdd:PRK11300 220 ISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-243 |
4.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 22 RPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGR--QLGPVRRRMQAVFQD 99
Cdd:PRK13645 19 KTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 100 PTSSL-NPTMTVGAAVGEglgVHRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:PRK13645 99 PEYQLfQETIEKDIAFGP---VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-236 |
4.31e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.71 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFR--LKSPPWRPPL-VLhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgp 88
Cdd:TIGR00958 479 IEFQdvSFSYPNRPDVpVL---KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL-- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 89 vRRRMQAVFQDPtssLNPTMTVGAAVGEGLgvhrigTRADRAE-RVAAMLDRV-----GLPRGTAQN---YPGALSGGQR 159
Cdd:TIGR00958 554 -HRQVALVGQEP---VLFSGSVRENIAYGL------TDTPDEEiMAAAKAANAhdfimEFPNGYDTEvgeKGSQLSGGQK 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 160 QRVGIARALIVAPDLLIADEAVSALDVSVQAgivnLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETG 236
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-263 |
4.59e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrlTGRQLGPVRRRMQAVFQDPTSSL-NP 106
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQIfSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGE---GLGVHRIGTRADRAER---VAAMLDRVglprgtaqnyPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:PRK13652 95 TVEQDIAFGPinlGLDEETVAHRVSSALHmlgLEELRDRV----------PHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPrHPYTRALLD--AVP 258
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP-DLLARVHLDlpSLP 243
|
....*
gi 2075269590 259 RLVPT 263
Cdd:PRK13652 244 KLIRS 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-241 |
6.26e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdRLTG----RQLGPVrrrMqaVFQDPts 102
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSprdaIALGIG---M--VHQHF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTMTV------GAavgEGLGVHRIGTRADRAeRVAAMLDRVGL---PRGTAQNypgaLSGGQRQRVGIARALIVAPD 173
Cdd:COG3845 90 MLVPNLTVaenivlGL---EPTKGGRLDRKAARA-RIRELSERYGLdvdPDAKVED----LSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 174 LLIADEAVSALdvSVQAgIVNLLLDLRE--EMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG3845 162 ILILDEPTAVL--TPQE-ADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
47-245 |
7.09e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 47 GESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQlgpvrRRMQAVFQdpTSSLNPTMTVGAAVGEGLGVHRIGtR 126
Cdd:PRK11432 39 GPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDICMVFQ--SYALFPHMSLGENVGYGLKMLGVP-K 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 127 ADRAERVAAMLDRVGLPrGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLA 206
Cdd:PRK11432 111 EERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNIT 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 2075269590 207 MLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK11432 190 SLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-242 |
8.78e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHfAGRRIDRLTGRQ--LGPVRRRMQAVFQDPT 101
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTSKQkeIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 SSLNPTMTVGAAvgeGLGVHRIGTRADRAERVAA-MLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:PRK13643 95 SQLFEETVLKDV---AFGPQNFGIPKEKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 181 VSALDVSVQAGIVNLLLDLrEEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-245 |
9.84e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrQLGPVRRRMQAVFQDptSSLNPTM 108
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-----ELEPADRDIAMVFQN--YALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGtRADRAERVAA---------MLDRvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK11650 92 SVRENMAYGLKIRGMP-KAEIEERVAEaarilelepLLDR----------KPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 180 AVSALDVSVQagiVNLLLDLRE---EMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK11650 161 PLSNLDAKLR---VQMRLEIQRlhrRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-243 |
1.45e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.84 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 7 VNDLGVEFRLKSPpwrppLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVH--FAGRRIDRLTGR 84
Cdd:PRK13651 5 VKNIVKIFNKKLP-----TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 -------------------QLGPVRRRMQAVFQDPTSSL-NPTMTVGAAVGE-GLGVhrigTRADRAERVAAMLDRVGLP 143
Cdd:PRK13651 80 kekvleklviqktrfkkikKIKEIRRRVGVVFQFAEYQLfEQTIEKDIIFGPvSMGV----SKEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 144 RGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDvsvQAGIVNLLLDLRE--EMGLAMLFIAHDLDVVRHFC 221
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD---PQGVKEILEIFDNlnKQGKTIILVTHDLDNVLEWT 232
|
250 260
....*....|....*....|..
gi 2075269590 222 DRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-245 |
2.24e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 90.68 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgrqlgPVRRRMQA----VFQDPtsS 103
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL------PMHKRARLgigyLPQEA--S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 LNPTMTVG---AAVGEGLGVhrigTRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:cd03218 86 IFRKLTVEeniLAVLEIRGL----SKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 181 VSALD-VSVQAgIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:cd03218 161 FAGVDpIAVQD-IQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-232 |
2.86e-21 |
|
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: 90.22 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 20 PWRPP-LVLhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQ 98
Cdd:cd03248 22 PTRPDtLVL---QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL---HSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 99 DPTSSlnpTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRG--TAQNYPGA-LSGGQRQRVGIARALIVAPDLL 175
Cdd:cd03248 96 EPVLF---ARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGydTEVGEKGSqLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLLDLREEMGLamLFIAHDLDVVRHfCDRVMVLYLGRV 232
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERRTV--LVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-236 |
2.92e-21 |
|
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: 90.28 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRLKSPPWRPPLVL------------HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVH 72
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 73 fagrridrltgrqlgpVRRRMQAVFqDPTSSLNPTMTV------GAAVgegLGVhrigTRADRAERVAAMLDRVGLprGT 146
Cdd:cd03220 81 ----------------VRGRVSSLL-GLGGGFNPELTGreniylNGRL---LGL----SRKEIDEKIDEIIEFSEL--GD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 147 AQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLReEMGLAMLFIAHDLDVVRHFCDRVM 225
Cdd:cd03220 135 FIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRAL 213
|
250
....*....|.
gi 2075269590 226 VLYLGRVMETG 236
Cdd:cd03220 214 VLEKGKIRFDG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-232 |
5.30e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQ---LG----PVRRRMQAVFQDPTSS 103
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlaRGlvylPEDRQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 LNPTmtvgaavgeGLGVHRIGTRADRAeRVAAMLDR----VGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK15439 360 WNVC---------ALTHNRRGFWIKPA-RENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
30-242 |
5.40e-21 |
|
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: 90.14 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLgravLRLL-----PISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPTSSL 104
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTL----LSLItgdlpPTYGNDVRLFGERRGGEDVWEL---RKRIGLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVGAAVGEGL----GVHRIGTRADRaERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:COG1119 92 PRDETVLDVVLSGFfdsiGLYREPTDEQR-ERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDL-DVVRHFcDRVMVLYLGRVMETGRTADVF 242
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeEIPPGI-THVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
29-236 |
6.99e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 89.31 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRidrlTGRQLGPVRRRMQAVFQDPTsslnpTM 108
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKKFLRRIGVVFGQKT-----QL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGTRAD------RAERVAAMLDRVGLPRGTAQNypgaLSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPparfkkRLDELSELLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-227 |
7.23e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 2 TALLDVNDLGveFRLKSPPwrpplVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRL 81
Cdd:PRK10247 5 SPLLQLQNVG--YLAGDAK-----ILN---NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 82 TgrqlgPVRRRMQAVFQDPTSSLnptmtVGAAVGEGLGV-HRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQ 160
Cdd:PRK10247 75 K-----PEIYRQQVSYCAQTPTL-----FGDTVYDNLIFpWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 161 RVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVL 227
Cdd:PRK10247 145 RISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
30-244 |
1.02e-20 |
|
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: 92.41 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPvrrRMQAVFQDptSSLNPTmT 109
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK---HIGYLPQD--VELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGeglgvhRIGTRADrAERV--AAMLDRV-----GLPRG--TAQNYPGA-LSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:TIGR01842 408 VAENIA------RFGENAD-PEKIieAAKLAGVhelilRLPDGydTVIGPGGAtLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVrHFCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-240 |
1.66e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 34 SFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrRIDRLTGRQLGPVRRRMQAVFQDptSSLNPTMTVGAA 113
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-----TLNGQDHTTTPPSRRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 114 VGegLGVHRiGTRADRAER--VAAMLDRVGLprgtaQNY----PGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:PRK10771 92 IG--LGLNP-GLKLNAAQRekLHAIARQMGI-----EDLlarlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTAD 240
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-236 |
2.02e-20 |
|
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: 87.63 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVaPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrltGRQLGPVRRRMQAVFQDPTSSlnPT 107
Cdd:cd03264 14 RALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIGYLPQEFGVY--PN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGTRaDRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:cd03264 87 FTVREFLDYIAWLKGIPSK-EVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2075269590 188 VQAGIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:cd03264 165 ERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-265 |
3.20e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 15 RLKSPPWRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrrIDRLTGRQLGPVRRRMQ 94
Cdd:PRK13644 3 RLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 95 AVFQDPTsslnpTMTVGAAVGEGLGVH---------RIGTRADRAervaamLDRVGLPRGTAQNyPGALSGGQRQRVGIA 165
Cdd:PRK13644 81 IVFQNPE-----TQFVGRTVEEDLAFGpenlclppiEIRKRVDRA------LAEIGLEKYRHRS-PKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 166 RALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVrHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
250 260
....*....|....*....|
gi 2075269590 246 RhpyTRALLDAVPRLVPTGE 265
Cdd:PRK13644 227 S---LQTLGLTPPSLIELAE 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
30-241 |
3.41e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.39 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgrqlgPVRRRMQA----------VFQD 99
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL------PMHKRARLgigylpqeasIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 100 ptsslnptMTVG---AAVGEGLGVhrigTRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLI 176
Cdd:COG1137 93 --------LTVEdniLAVLELRKL----SKKEREERLEELLEEFGITH-LRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 177 ADEAVSALD-VSVqAGIVNLLLDLReEMGLAMLFIAHD----LDVvrhfCDRVMVLYLGRVMETGRTADV 241
Cdd:COG1137 160 LDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVLITDHNvretLGI----CDRAYIISEGKVLAEGTPEEI 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-218 |
3.56e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHfagrridRLTGRQLGPVRRRmqavfqdptSSLNPTM 108
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-------RAGGARVAYVPQR---------SEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 --TVGAAVGEGL----GVHRIGTRADRAeRVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:NF040873 71 plTVRDLVAMGRwarrGLWRRLTRDDRA-AVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVR 218
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
23-245 |
4.99e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 90.77 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 23 PPLVlhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQL---------------G 87
Cdd:TIGR03796 492 PPLI----ENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLansvamvdqdiflfeG 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 88 PVRrrmqavfqDPTSSLNPTMTVGAAVgeglgvhrigtradRAERVAAMLDRV-GLPRGTAQNYP--GA-LSGGQRQRVG 163
Cdd:TIGR03796 568 TVR--------DNLTLWDPTIPDADLV--------------RACKDAAIHDVItSRPGGYDAELAegGAnLSGGQRQRLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 164 IARALIVAPDLLIADEAVSALDVSVQAGIVNlllDLREEmGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFA 243
Cdd:TIGR03796 626 IARALVRNPSILILDEATSALDPETEKIIDD---NLRRR-GCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWA 700
|
..
gi 2075269590 244 AP 245
Cdd:TIGR03796 701 VG 702
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-234 |
5.69e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVR-RRMQAVFQdpTSSLNPTMTV 110
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQ--SFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 GAAVgEGLGVHRIGTRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:PRK10584 106 LENV-ELPALLRGESSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2075269590 191 GIVNLLLDLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVME 234
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-272 |
8.48e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.13 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREIL-------------GVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAV 96
Cdd:PRK11831 10 MRGVSFTRGNRCIFdnisltvprgkitAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 97 FQdpTSSLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLI 176
Cdd:PRK11831 90 FQ--SGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 177 ADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGrTADVFAAPRHPYTRALLDA 256
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG-SAQALQANPDPRVRQFLDG 245
|
250 260
....*....|....*....|.
gi 2075269590 257 -----VPRLVPTGEPRRLLAG 272
Cdd:PRK11831 246 iadgpVPFRYPAGDYHADLLG 266
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-234 |
1.20e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 89.65 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 16 LKSPPWRPPlVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqLGPVRRRMQA 95
Cdd:PLN03232 1242 LRYRPGLPP-VLH---GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 96 VFQDPT-------SSLNP-TMTVGAAVGEGLgvHRIGTRaDRAERVAAMLDrvglprgtAQNYPGA--LSGGQRQRVGIA 165
Cdd:PLN03232 1315 IPQSPVlfsgtvrFNIDPfSEHNDADLWEAL--ERAHIK-DVIDRNPFGLD--------AEVSEGGenFSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 166 RALIVAPDLLIADEAVSALDVSVQAGIVNlllDLREEM-GLAMLFIAHDLDVVRHfCDRVMVLYLGRVME 234
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQR---TIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-242 |
1.36e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGVEFRLKSPPwrpplVLHAVRGVSFTVAPREILGVVGESGSGKTSL----------GRAVLRLLPISSGEVHF 73
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEN-----ELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthfngliksKYGTIQVGDIYIGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 74 AGRRIDRLTGRQLG---PVRRRMQAVFQDPTSSLNPTmTVGAAVGEG---LGVHRIgtraDRAERVAAMLDRVGLPRGTA 147
Cdd:PRK13631 96 NHELITNPYSKKIKnfkELRRRVSMVFQFPEYQLFKD-TIEKDIMFGpvaLGVKKS----EAKKLAKFYLNKMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 148 QNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*
gi 2075269590 228 YLGRVMETGRTADVF 242
Cdd:PRK13631 250 DKGKILKTGTPYEIF 264
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-227 |
1.43e-19 |
|
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: 88.88 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQdptsslNPTM 108
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQ------HPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAaVGEGLgvhRIGTRADRAERVAAMLDRVG-------LPRGTAQ---NYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:TIGR02857 408 FAGT-IAENI---RLARPDASDAEIREALERAGldefvaaLPQGLDTpigEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLdVVRHFCDRVMVL 227
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-242 |
1.55e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRLksppwrpplvlhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPiSSGEVHFAGRRIDRLTGR 84
Cdd:COG4138 1 LQLNDVAVAGRL--------------GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 QLgpvrRRMQAVF--QDPTSSLnptMTVGAAVGegLGVHRIGTRADRAERVAAMLDRVG----LPRGTAQnypgaLSGGQ 158
Cdd:COG4138 66 EL----ARHRAYLsqQQSPPFA---MPVFQYLA--LHQPAGASSEAVEQLLAQLAEALGledkLSRPLTQ-----LSGGE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 159 RQRVGIARALI-VAPD------LLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGR 231
Cdd:COG4138 132 WQRVRLAAVLLqVWPTinpegqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGK 210
|
250
....*....|.
gi 2075269590 232 VMETGRTADVF 242
Cdd:COG4138 211 LVASGETAEVM 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-232 |
1.91e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.91 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgrqlgPVRRRMQ---AVFQDPTSSL 104
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL------PEYKRAKyigRVFQDPMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTV----------GAAVGEGLGVhrigTRADRA---ERVAA--------MLDRVGLprgtaqnypgaLSGGQRQRVG 163
Cdd:COG1101 94 APSMTIeenlalayrrGKRRGLRRGL----TKKRRElfrELLATlglglenrLDTKVGL-----------LSGGQRQALS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 164 IARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-244 |
2.09e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvrrrMQAVFQDPTSSLNPTM 108
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEG----LGVHRIGTRADRaERVAAMLDRVGLPRGTAQNYpGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:PRK15056 96 LVEDVVMMGryghMGWLRRAKKRDR-QIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 185 DVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVmVLYLGRVMETGRTADVFAA 244
Cdd:PRK15056 174 DVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTA 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
29-232 |
3.48e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREIL-------------GVVGESGSGKTSLGRAVLRLLPISSGEVhfagrridrLTGRQ-LGPVRRRMQ 94
Cdd:PRK11247 14 LLNAVSKRYGERTVLnqldlhipagqfvAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 95 AVFQDptSSLNPTMTVGAAVGEGLGvhriGTRADRAERVaamLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDL 174
Cdd:PRK11247 85 LMFQD--ARLLPWKKVIDNVGLGLK----GQWRDAALQA---LAAVGLAD-RANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 175 LIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-238 |
4.16e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.14 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 34 SFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqlgPVRRRMQAVFQDptSSLNPTMTVGAA 113
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 114 VGegLGVH-RIGTRADRAERVAAMLDRVGLPRGTAQnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGI 192
Cdd:TIGR01277 91 IG--LGLHpGLKLNAEQQEKVVDAAQQVGIADYLDR-LPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2075269590 193 VNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRT 238
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-232 |
4.93e-19 |
|
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: 83.79 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrRIDRLTGRQLGPV--RRRMQAVFQDPT---S 102
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-----LLDGTDIRQLDPAdlRRNIGYVPQDVTlfyG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTMTVGAAVGEGLGVHRIGTRA---DRAERVAAMLDRVGLPRGTAqnypgaLSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:cd03245 93 TLRDNITLGAPLADDERILRAAELAgvtDFVNKHPNGLDLQIGERGRG------LSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRhFCDRVMVLYLGRV 232
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-232 |
5.07e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.37 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 15 RLKSPPWRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAV--LRLLPISSGEVHFAGRRIDRLTgrqlgpVRRR 92
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS------FRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 93 MQAVFQDptSSLNPTMTVgaavgeglgvhrigtraDRAERVAAMLdrvglpRGtaqnypgaLSGGQRQRVGIARALIVAP 172
Cdd:cd03213 84 IGYVPQD--DILHPTLTV-----------------RETLMFAAKL------RG--------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 173 DLLIADEAVSALDVSVQAGIVNLLLDLReEMGLAMLFIAHDL-DVVRHFCDRVMVLYLGRV 232
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-236 |
5.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.17 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLgraVLRLLPI---SSGEVHFAGRRIDRLTGRQlgpVRRRMQAVFQDPTSSL 104
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLNGIylpQRGRVKVMGREVNAENEKW---VRSKVGLVFQDPDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NpTMTVGAAVGegLGVHRIGTRADRAE-RVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:PRK13647 93 F-SSTVWDDVA--FGPVNMGLDKDEVErRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 184 LDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-233 |
5.54e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLgvefRLKSPPWRPPLVLhaVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDR 80
Cdd:PRK10535 1 MTALLELKDI----RRSYPSGEEQVEV--LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRRR-MQAVFQdpTSSLNPTMTVGAAVgEGLGVHRIGTRADRAERVAAMLDRVGLprGTAQNY-PGALSGGQ 158
Cdd:PRK10535 75 LDADALAQLRREhFGFIFQ--RYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGL--EDRVEYqPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHfCDRVMVLYLGRVM 233
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-224 |
6.98e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGR-RIDRLTgrqlgpvrrrmqavfQDPTssLNPTMT 109
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlRIGYLP---------------QEPP--LDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEGLG-VHRIGTRADRAE------------------------------RVAAMLDRVGLPRGTAQNYPGALSGGQ 158
Cdd:COG0488 78 VLDTVLDGDAeLRALEAELEELEaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDVsvqAGIV---NLLLDLReemGlAMLFIAHDldvvRHFCDRV 224
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDL---ESIEwleEFLKNYP---G-TVLVVSHD----RYFLDRV 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
46-246 |
8.97e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 8.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 46 VGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrQLGPVRRRMQAVFQdpTSSLNPTMTVGAAVGEGLGVHRIGt 125
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGMVFQ--SYALYPHLSVAENMSFGLKLAGAK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 126 RADRAERV---------AAMLDRvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS--VQAGIVn 194
Cdd:PRK11000 107 KEEINQRVnqvaevlqlAHLLDR----------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrVQMRIE- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 195 lLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAPR 246
Cdd:PRK11000 176 -ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-251 |
1.02e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.93 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISS-----GEVHFAGRRI-DRLTgrQLGPVRRRMQAVFqdPTSS 103
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRV--NLNRLRRQVSMVH--PKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 LNPtMTVGAAVGegLGVHRIGTR--------ADRAERVAAMLDRVglpRGTAQNYPGALSGGQRQRVGIARALIVAPDLL 175
Cdd:PRK14258 99 LFP-MSVYDNVA--YGVKIVGWRpkleiddiVESALKDADLWDEI---KHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLY-----LGRVMETGRTADVFAAPRHPYT 250
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSRT 252
|
.
gi 2075269590 251 R 251
Cdd:PRK14258 253 R 253
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-234 |
3.39e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.56 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKSPPWRP--PLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpv 89
Cdd:PLN03130 1238 IKFEDVVLRYRPelPPVLH---GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL--- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 90 RRRMQAVFQ-------------DPTSSLNptmtvGAAVGEGLgvhrigTRA---DRAERVAAMLDRVGLPRGtaQNYpga 153
Cdd:PLN03130 1312 RKVLGIIPQapvlfsgtvrfnlDPFNEHN-----DADLWESL------ERAhlkDVIRRNSLGLDAEVSEAG--ENF--- 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 154 lSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNlllDLREEM-GLAMLFIAHDLDVVRHfCDRVMVLYLGRV 232
Cdd:PLN03130 1376 -SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQK---TIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
..
gi 2075269590 233 ME 234
Cdd:PLN03130 1451 VE 1452
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-243 |
4.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT-GRQLGPVRRRMQAVFQDPTS 102
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SL-NPTMTVGAAVGE---GLGVHRIGTRADRaervaaMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:PRK13646 97 QLfEDTVEREIIFGPknfKMNLDEVKNYAHR------LLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-227 |
4.83e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHF-AGRRIDRLTGR---QLGPVRRrmQAVFQDPTSSLN 105
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRpylPLGTLRE--ALLYPATAEAFS 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PtmtvgaavgeglgvhrigtradraERVAAMLDRVGLPR-----GTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:COG4178 457 D------------------------AELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2075269590 181 VSALDVSVQAgivNLLLDLREEM-GLAMLFIAHDlDVVRHFCDRVMVL 227
Cdd:COG4178 513 TSALDEENEA---ALYQLLREELpGTTVISVGHR-STLAAFHDRVLEL 556
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-243 |
5.27e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 4 LLDVNDLGveFRLKSPPwrpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrLTG 83
Cdd:PRK13638 1 MLATSDLW--FRYQDEP--------VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 84 RQLGPVRRRMQAVFQDPTSSLNPTmTVGAAVG---EGLGV--HRIGTRADRAervAAMLDRVGLPRGTAQnypgALSGGQ 158
Cdd:PRK13638 70 RGLLALRQQVATVFQDPEQQIFYT-DIDSDIAfslRNLGVpeAEITRRVDEA---LTLVDAQHFRHQPIQ----CLSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRT 238
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
....*
gi 2075269590 239 ADVFA 243
Cdd:PRK13638 221 GEVFA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-241 |
5.51e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 26 VLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGR---QLGpvrrrMQAVFQDpTS 102
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLG-----IGIIYQE-LS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTmtvgaAVGEGLGVHRIGTR----------ADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAP 172
Cdd:PRK09700 91 VIDEL-----TVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 173 DLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-235 |
1.06e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.34 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISS--GEVHFAGRRIDRLTGRQLGpvRRRMQAVFQDPTssLNP 106
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTE--RAGIVIIHQELT--LVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLGVHRIGTRADRAE---RVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:TIGR02633 92 ELSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 184 LDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMET 235
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-258 |
1.69e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgrQLGPVRRRMQAVFQDPtsslnptM 108
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTP-------F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHRIGTRADRAERVAAML----DRVGLPRG--TAQNYPGA-LSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLAsvhdDILRLPQGydTEVGERGVmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 182 SALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAAP-------RHPYTRALL 254
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQSgwyrdmyRYQQLEAAL 556
|
....
gi 2075269590 255 DAVP 258
Cdd:PRK10789 557 DDAP 560
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-236 |
2.94e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.06 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLL---PISSGEVHFAGRRIDRlTGRQLGPVRR-RMQA--VFQDPTS 102
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQR-EGRLARDIRKsRANTgyIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTMTVGAAVGeGLG-------VHRIGTRADRAERVAAmLDRVGLPRGTAQNYpGALSGGQRQRVGIARALIVAPDLL 175
Cdd:PRK09984 98 VNRLSVLENVLIG-ALGstpfwrtCFSWFTREQKQRALQA-LTRVGMVHFAHQRV-STLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETG 236
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-243 |
3.02e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.37 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqLGPVRRRMQAVFQDpTSSLNPTM 108
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQVALVSQN-VHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGlgvhRIGTRAD--RAERVAAMLDRV-GLPRG--TAQNYPGA-LSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:PRK11176 434 ANNIAYART----EQYSREQieEAARMAYAMDFInKMDNGldTVIGENGVlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK11176 510 ALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-242 |
3.49e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGpvrRRMQAVFQDPTSslnPT-M 108
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRLALLPQHHLT---PEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVH-----RIGTRaDRAeRVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:PRK11231 92 TVRELVAYGRSPWlslwgRLSAE-DNA-RVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 184 LDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-244 |
4.24e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRlksppwRPPLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGR 84
Cdd:PRK10790 341 IDIDNVSFAYR------DDNLVLQ---NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 QLgpvRRRMQAVFQDP---TSSLNPTMTVGAAVGEGlGVHRIGTRADRAERVAAMLDRVGLPRGTAQNypgALSGGQRQR 161
Cdd:PRK10790 412 VL---RQGVAMVQQDPvvlADTFLANVTLGRDISEE-QVWQALETVQLAELARSLPDGLYTPLGEQGN---NLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 162 VGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLamLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADV 241
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
...
gi 2075269590 242 FAA 244
Cdd:PRK10790 562 LAA 564
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-242 |
5.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.40 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT-GRQLGPVRRRMQAVFQDPTS 102
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTmTVGAAVGegLGVHRIGTRADRAERVA-AMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:PRK13649 97 QLFEE-TVLKDVA--FGPQNFGVSQEEAEALArEKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 182 SALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVF 242
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-246 |
6.61e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 5 LDVNDLGVEFRLKSppwrpplvlhavrgVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPiSSGEVHFAGRRIDRLTGR 84
Cdd:PRK03695 1 MQLNDVAVSTRLGP--------------LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 85 QLGpvRRRMQAVFQDPTSSLNPtmtvgaaVGEGLGVH-----RIGTRADRAERVAAML---DRvgLPRGTAQnypgaLSG 156
Cdd:PRK03695 66 ELA--RHRAYLSQQQTPPFAMP-------VFQYLTLHqpdktRTEAVASALNEVAEALgldDK--LGRSVNQ-----LSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 157 GQRQRVGIARA-LIVAPD------LLIADEAVSALDVSvQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYL 229
Cdd:PRK03695 130 GEWQRVRLAAVvLQVWPDinpagqLLLLDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
250
....*....|....*..
gi 2075269590 230 GRVMETGRTADVFAAPR 246
Cdd:PRK03695 209 GKLLASGRRDEVLTPEN 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-283 |
7.23e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.87 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 45 VVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQlgpVRRRMQAVFQDPTSSLNptMTVGAAVGEGLGVHR-- 122
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQNATTPGD--ITVQELVARGRYPHQpl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 123 -IGTRADRAERVAAMLDRVGLPRGTAQNYpGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLRE 201
Cdd:PRK10253 113 fTRWRKEDEEAVTKAMQATGITHLADQSV-DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 202 EMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGrtadvfaAPRHPYTRALLDAVPRLvptgepRRLLAGDP--PSPLA 279
Cdd:PRK10253 192 EKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERIYGL------RCMIIDDPvaGTPLV 258
|
....
gi 2075269590 280 PPSG 283
Cdd:PRK10253 259 VPLG 262
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
31-208 |
8.06e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLtgrqlgpvRRRMQAVFQDPTSSLNPTMTv 110
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--------DVAEACHYLGHRNAMKPALT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 gaaVGEGLGVHRiGTRADRAERVAAMLDRVGLPRgtAQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:PRK13539 90 ---VAENLEFWA-AFLGGEELDIAAALEAVGLAP--LAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170
....*....|....*....
gi 2075269590 190 AGIVNLLLDLREEMGLAML 208
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIA 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
30-241 |
8.79e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGpvrRRMQAVFQDPtsSLNPTMT 109
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---KRLAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEGLGVHRIG--TRADRaERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV- 186
Cdd:COG4604 92 VRELVAFGRFPYSKGrlTAEDR-EIIDEAIAYLDL-EDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMk 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 187 -SVQagIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:COG4604 170 hSVQ--MMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-252 |
1.14e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPI-----SSGEVHFAGRRidrLTGRQLGP--VRRRMQAVFQDPT 101
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKN---LYAPDVDPveVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 ---SSLNPTMTVGAAVGeglgvhriGTRAD------RAERVAAMLDRVglpRGTAQNYPGALSGGQRQRVGIARALIVAP 172
Cdd:PRK14243 102 pfpKSIYDNIAYGARIN--------GYKGDmdelveRSLRQAALWDEV---KDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 173 DLLIADEAVSALDVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHFCDRVMVL---------YLGRVMETGRTADVFA 243
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFN 248
|
....*....
gi 2075269590 244 APRHPYTRA 252
Cdd:PRK14243 249 SPQQQATRD 257
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-231 |
1.25e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISS--GEVHFAGRRIdrltgrQLGPVRRRMQA----VFQDPTs 102
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEEL------QASNIRDTERAgiaiIHQELA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 sLNPTMTVGAAVGEGLGVHRIGtRADRAE---RVAAMLDRVGLPRGTAQNYpGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK13549 93 -LVKELSVLENIFLGNEITPGG-IMDYDAmylRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGR 231
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-236 |
1.36e-16 |
|
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: 77.31 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSL-----GRavLRLLPISSGEVHFAGRRIDRLTgrqlgpVRRRMQAVFQDPTssLNP 106
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLldaisGR--VEGGGTTSGQILFNGQPRKPDQ------FQKCVAYVRQDDI--LLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVG-----AAVgegLGVHRIGTRADRAERVAAM-LDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:cd03234 95 GLTVRetltyTAI---LRLPRKSSDAIRKKRVEDVlLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEMGLAMLFIaHD--LDVVRHFcDRVMVLYLGRVMETG 236
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTI-HQprSDLFRLF-DRILLLSSGEIVYSG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-245 |
7.46e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREIL-------------GVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGpvRRRMQA 95
Cdd:PRK10575 13 ALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA--RKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 96 VFQDPTSSlnpTMTVGAAVGEG-------LGvhRIGtRADRaERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIAraL 168
Cdd:PRK10575 91 PQQLPAAE---GMTVRELVAIGrypwhgaLG--RFG-AADR-EKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIA--M 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 169 IVAPD--LLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK10575 161 LVAQDsrCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-227 |
1.07e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFRLKSppwrpplVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGevhfagrRIDR 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRR-------VLS---DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 81 LTGRQLGPVRrrmQAVFQDPTSSLnptmTVGAAVGEGLGVHRigtrADraerVAAMLDRVglPRGTAQNYP-GALSGGQR 159
Cdd:PRK09544 64 NGKLRIGYVP---QKLYLDTTLPL----TVNRFLRLRPGTKK----ED----ILPALKRV--QAGHLIDAPmQKLSGGET 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 160 QRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-246 |
1.31e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLgravLRLL-----PiSSGEVHFAGRRidrltgrqlgPVRRRMQ------AV 96
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLtgilvP-TSGEVRVLGYV----------PFKRRKEfarrigVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 97 F------------QDpTSSLNptmtvgAAVgeglgvHRIgTRADRAERVAAMLDRVGL------P-RgtaqnypgALSGG 157
Cdd:COG4586 101 FgqrsqlwwdlpaID-SFRLL------KAI------YRI-PDAEYKKRLDELVELLDLgelldtPvR--------QLSLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 158 QRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGR 237
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
250
....*....|..
gi 2075269590 238 TADV---FAAPR 246
Cdd:COG4586 239 LEELkerFGPYK 250
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-232 |
2.80e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT---GRQLGPV-----RRRMQAVfqdpt 101
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdGLANGIVyisedRKRDGLV----- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 sslnptmtVGAAVGEGLGV------HRIGTRADRAERVAAMLDRVGL-----PrgTAQNYPGALSGGQRQRVGIARALIV 170
Cdd:PRK10762 343 --------LGMSVKENMSLtalryfSRAGGSLKHADEQQAVSDFIRLfniktP--SMEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 171 APDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
28-236 |
3.49e-15 |
|
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: 72.35 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRridrltgrqlgpvrrrmqavfqdPTSSLNPT 107
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-----------------------PVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MtvgaavgeglgvhrigtradrAERVAAMLDRVGLPRGTAQNYPGA-LSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:cd03247 73 L---------------------SSLISVLNQRPYLFDTTLRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2075269590 187 SVQAGIVNLLLDLREEMGLamLFIAHDLDVVRHFcDRVMVLYLGRVMETG 236
Cdd:cd03247 132 ITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-236 |
4.26e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLhavRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDPT-- 101
Cdd:PTZ00243 1323 PLVL---RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPVlf 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 -----SSLNPTMTVGAA-VGEGLGVhrIGTRadraERVAAM---LDRVGLPRGTaqNYpgalSGGQRQRVGIARALIV-A 171
Cdd:PTZ00243 1397 dgtvrQNVDPFLEASSAeVWAALEL--VGLR----ERVASEsegIDSRVLEGGS--NY----SVGQRQLMCMARALLKkG 1464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 172 PDLLIADEAVS----ALDVSVQAGIVNLLldlreeMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETG 236
Cdd:PTZ00243 1465 SGFILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-248 |
5.94e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 15 RLKSPPWRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP---ISSGEVHFAGRRIDRltgRQLgpvRR 91
Cdd:TIGR00955 26 RLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA---KEM---RA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 92 RMQAVFQD----PTSSLNPTMTVGAAvgegLGVHRIGTRADRAERVAAMLDRVGLprGTAQN----YPG---ALSGGQRQ 160
Cdd:TIGR00955 100 ISAYVQQDdlfiPTLTVREHLMFQAH----LRMPRRVTKKEKRERVDEVLQALGL--RKCANtrigVPGrvkGLSGGERK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 161 RVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIaHD--LDVVRHFcDRVMVLYLGRVMETGRT 238
Cdd:TIGR00955 174 RLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQpsSELFELF-DKIILMAEGRVAYLGSP 251
|
250
....*....|...
gi 2075269590 239 ---ADVFAAPRHP 248
Cdd:TIGR00955 252 dqaVPFFSDLGHP 264
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-217 |
6.22e-15 |
|
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: 72.01 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRqlgPVRRRMQAVFQDptsSLNPTM 108
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE---PHENILYLGHLP---GLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TvgaaVGEGLGV-HRIGTRADRAerVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:TIGR01189 89 S----ALENLHFwAAIHGGAQRT--IEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|
gi 2075269590 188 VQAGIVNLLLDLREEMGLAMLFIAHDLDVV 217
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-234 |
3.06e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI------DRL-TGRQLGPVRRRMQAVFqdPTS 102
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprsplDAVkKGMAYITESRRDNGFF--PNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 SLNPTMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTA---QNYpGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK09700 357 SIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHsvnQNI-TELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVME 234
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-224 |
4.70e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKSPPWRPPLVLHA------------VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFaGRRID 79
Cdd:COG0488 301 VEIRFPPPERLGKKVLELeglsksygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 80 rltgrqlgpvrrrmQAVF-QDpTSSLNPTMTVGAAVGEGLgvhrigtRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQ 158
Cdd:COG0488 380 --------------IGYFdQH-QEELDPDKTVLDELRDGA-------PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGE 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDV-SVQAgIVNLLLDLReemGlAMLFIAHDldvvRHFCDRV 224
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP---G-TVLLVSHD----RYFLDRV 495
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-244 |
6.64e-14 |
|
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: 72.67 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 12 VEFRLKSPPWRPPLVLhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrRIDRLTGRQLG--PV 89
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-----IIDGLNIAKIGlhDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 90 RRRMQAVFQDP---TSSLNptmtvgaavgegLGVHRIGTRADR----AERVAAMLDRV-GLPRG-TAQNYPGA--LSGGQ 158
Cdd:TIGR00957 1359 RFKITIIPQDPvlfSGSLR------------MNLDPFSQYSDEevwwALELAHLKTFVsALPDKlDHECAEGGenLSVGQ 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDVS----VQAGIVNLLLDlreemgLAMLFIAHDLDVVRHFCdRVMVLYLGRVME 234
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAE 1499
|
250
....*....|
gi 2075269590 235 TGRTADVFAA 244
Cdd:TIGR00957 1500 FGAPSNLLQQ 1509
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-214 |
1.23e-13 |
|
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: 71.24 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGrqlGPVRRRMQAVFQDPtsslnptM 108
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ---DEVRRRVSVCAQDA-------H 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLgvhRIGTRADRAERVAAMLDRVGLPRGTAQNYPG----------ALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:TIGR02868 420 LFDTTVRENL---RLARPDATDEELWAALERVGLADWLRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDL 214
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-236 |
2.55e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrridRLTGRQLGP----VRRR---MQAVFqdpt 101
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA--------WLFGQPVDAgdiaTRRRvgyMSQAF---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 sSLNPTMTVGaavgEGLGVH----RIGtRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIA 177
Cdd:NF033858 349 -SLYGELTVR----QNLELHarlfHLP-AAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 178 DEAVSALDVSVQAGIVNLLLDLREEMGLAmLFIAhdldvvRHF------CDRVMVLYLGRVMETG 236
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSREDGVT-IFIS------THFmneaerCDRISLMHAGRVLASD 479
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-216 |
3.02e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRL----------TGRQLGpVRRRMQAVfqdp 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqdllyLGHQPG-IKTELTAL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 tsslnptmtvgaavgEGLGV-HRIGTRADRAERVAAmLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK13538 93 ---------------ENLRFyQRLHGPGDDEALWEA-LAQVGL-AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDV 216
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-237 |
3.15e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgrQLGPVRRRMQAVFQdpTSSLNPTMT 109
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGaavgEGLGVH----RIGTRADRAErVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:PRK13536 131 VR----ENLLVFgryfGMSTREIEAV-IPSLLEFARLES-KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 186 VSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGR 237
Cdd:PRK13536 205 PHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-234 |
3.76e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPissgevhfagrridrltgrqlgpvRRRMQAVFQDPTSSLNPT 107
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK------------------------GTPVAGCVDVPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGeglgvhRIGTRADRAERvaamLDRVGLprGTAQNY---PGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:COG2401 100 ASLIDAIG------RKGDFKDAVEL----LNAVGL--SDAVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 185 DVSVqAGIVNL-LLDLREEMGLAMLFIAHDLDVVRH-FCDRVMVLYLGRVME 234
Cdd:COG2401 168 DRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDlQPDLLIFVGYGGVPE 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-243 |
6.08e-13 |
|
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: 69.06 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRaVLRLL---PISSGEV----------------HFAGRRIDRlTGRQLG 87
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMdqyEPTSGRIiyhvalcekcgyverpSKVGEPCPV-CGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 88 P---------------VRRRMQAVFQDpTSSLNPTMTVGAAVGEGLgvHRIGTRADRA-ERVAAMLDRVGLP-RGT--AQ 148
Cdd:TIGR03269 91 PeevdfwnlsdklrrrIRKRIAIMLQR-TFALYGDDTVLDNVLEAL--EEIGYEGKEAvGRAVDLIEMVQLShRIThiAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 149 NypgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLY 228
Cdd:TIGR03269 168 D----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
250
....*....|....*
gi 2075269590 229 LGRVMETGRTADVFA 243
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-212 |
1.44e-12 |
|
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: 64.87 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFagrridrltgrqlgPVRRRMQAVFQDPTsslnptmt 109
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------------PEGEDLLFLPQRPY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 vgaavgeglgvhrigtradraervaamldrvgLPRGT---AQNYP--GALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:cd03223 75 --------------------------------LPLGTlreQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 2075269590 185 DVSVQAgivnLLLDLREEMGLAMLFIAH 212
Cdd:cd03223 123 DEESED----RLYQLLKELGITVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-217 |
1.47e-12 |
|
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: 65.59 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRltgrQLGPVRRRMQAVFQdptsslNPTMTVG 111
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSIARGLLYLGH------APGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGEGLGV-HRIGTRadraERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:cd03231 88 LSVLENLRFwHADHSD----EQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|....*..
gi 2075269590 191 GIVNLLLDLREEMGLAMLFIAHDLDVV 217
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-232 |
1.79e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIS-SGEVHFAGRRIDRLTGRQlgPVRRRMQAVFQD-PTSSLNPT 107
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQ--AIRAGIAMVPEDrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVG-----AAVGEGLGVHRIGTRADRaERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:TIGR02633 354 LGVGknitlSVLKSFCFKMRIDAAAEL-QIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-240 |
2.22e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT---GRQLGpvrrrMQAVFQDPTssLNPT 107
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG-----IYLVPQEPL--LFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHrigtrADRAERVAAMLDRVGL---PRGTAqnypGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:PRK15439 101 LSVKENILFGLPKR-----QASMQKMKQLLAALGCqldLDSSA----GSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 185 dvsVQAGIVNLLLDLRE--EMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTAD 240
Cdd:PRK15439 172 ---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-237 |
4.72e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.03 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 11 GVEFRLKSPPWRPPLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGR-------------- 76
Cdd:cd03250 5 DASFTWDSGEQETSFTLK---DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 77 -RIDRLTGRQLGPvrRRMQAVFQDptSSLNPTMTVGAA-----VGEglgvhrigtradraervaamldrvglpRGTAqny 150
Cdd:cd03250 82 iRENILFGKPFDE--ERYEKVIKA--CALEPDLEILPDgdlteIGE---------------------------KGIN--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 151 pgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLdlreeMGLAM-----LFIAHDLDVVRHfCDRVM 225
Cdd:cd03250 128 ---LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCI-----LGLLLnnktrILVTHQLQLLPH-ADQIV 198
|
250
....*....|..
gi 2075269590 226 vlylgrVMETGR 237
Cdd:cd03250 199 ------VLDNGR 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-245 |
6.75e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.02 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISsGEVhfagrRIDRLTGRQLGPV--RRRMQAVFQDPT---SSLNPT 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSL-----KINGIELRELDPEswRKHLSWVGQNPQlphGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGAAVGEGLGVHRIGTRADRAERVAAMLDrvGLprgtaqNYP-----GALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAWVSEFLPLLPQ--GL------DTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 183 ALDV-SVQAgivnLLLDLREEM-GLAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAAP 245
Cdd:PRK11174 515 SLDAhSEQL----VMQALNAASrRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-244 |
1.12e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRqlgpVRRRMQAVFQdpTSSLNPTMT 109
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH----ARQRVGVVPQ--FDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGaavgEGLGV--HRIGTRADRAERVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVS 187
Cdd:PRK13537 97 VR----ENLLVfgRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 188 VQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFAA 244
Cdd:PRK13537 173 ARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-236 |
1.19e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.23 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQDP---TSSL 104
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQAISVVSQRVhlfSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVGAAvgeglgvhrigTRADraERVAAMLDRVGLpRGTAQNYPG----------ALSGGQRQRVGIARALIVAPDL 174
Cdd:PRK11160 431 RDNLLLAAP-----------NASD--EALIEVLQQVGL-EKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 175 LIADEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHFcDRVMVLYLGRVMETG 236
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-243 |
1.21e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISS--GEVHFAGRRIDRltgrqlgPVRRRMQAVFQDPTssLNPTMT 109
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-------QILKRTGFVTQDDI--LYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAV--GEGLGVHRIGTRADRAERVAAMLDRVGLPRG----TAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:PLN03211 157 VRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 184 LDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-232 |
1.35e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLP-ISSGEVHFAGRRIDRLTGRQlgPVRRRMQAVFQD-PTSSLNPT 107
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDrKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTVGA----AVgegLGVHRIGTRADRAERVAAM---LDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:PRK13549 356 MGVGKnitlAA---LDRFTGGSRIDDAAELKTIlesIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-243 |
2.18e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 34 SFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLgpvRRRMQAVFQD-PTSSLNPtmtvga 112
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL---QKLVSDEWQRnNTDMLSP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 113 avGE---GLGVHRI---GTR-ADRAERVAA------MLDRvglpRGTaqnYpgaLSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:PRK10938 94 --GEddtGRTTAEIiqdEVKdPARCEQLAQqfgitaLLDR----RFK---Y---LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 180 AVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-235 |
2.85e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISS--GEVHFAGRridrltgrqlgpVRRrmqavFQDPTSS--- 103
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE------------VCR-----FKDIRDSeal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 ----------LNPTMTVGaavgEG--LGvHRIGTRA--DRAE---RVAAMLDRVGLprgtaQNYPGALSG----GQRQRV 162
Cdd:NF040905 79 giviihqelaLIPYLSIA----ENifLG-NERAKRGviDWNEtnrRARELLAKVGL-----DESPDTLVTdigvGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 163 GIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMET 235
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-235 |
3.64e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 1 MTALLDVNDLGVEFrlksppwrpPLVLhAVRGVSFTVAPREILGVVGESGSGKTSLgravLRLL-----PiSSGEVHFAG 75
Cdd:PRK11288 1 SSPYLSFDGIGKTF---------PGVK-ALDDISFDCRAGQVHALMGENGAGKSTL----LKILsgnyqP-DAGSILIDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 76 RridrltgrqlgpvrrrmQAVFQDPTSSLN-------------PTMTVGAAVGEGLGVHRIG--TRADRAERVAAMLDRV 140
Cdd:PRK11288 66 Q-----------------EMRFASTTAALAagvaiiyqelhlvPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 141 GL---PRgTAQNYpgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVV 217
Cdd:PRK11288 129 GVdidPD-TPLKY---LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEI 203
|
250
....*....|....*...
gi 2075269590 218 RHFCDRVMVLYLGRVMET 235
Cdd:PRK11288 204 FALCDAITVFKDGRYVAT 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
33-227 |
3.72e-11 |
|
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: 60.15 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHfagrridrltgrqlgpvrrrmqavfqdptssLNPTMTVGa 112
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------------------WGSTVKIG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 113 avgeglgvhrigtradraervaamldrvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV-SVQAg 191
Cdd:cd03221 67 -------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA- 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 2075269590 192 IVNLLLDLReemGlAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:cd03221 109 LEEALKEYP---G-TVILVSHDRYFLDQVATKIIEL 140
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-241 |
4.34e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.37 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrridrltgrqlgpvrrrmQAVFQDPTSSLNPT 107
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------------SAALIAISSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 108 MTvGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLprGTAQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:PRK13545 100 LT-GIENIELKGLMMGLTKEKIKEIIPEIIEFADI--GKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 187 SVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
30-243 |
4.53e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGpvRRRMQAVFQDPT-----SSL 104
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYLPQEASifrrlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTMTVgaavgegLGVHRIGTRADRAERVAAMLDRVGLPRgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:PRK10895 97 DNLMAV-------LQIRDDLSAEQREDRANELMEEFHIEH-LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2075269590 185 DVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADVFA 243
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-236 |
8.15e-11 |
|
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: 60.62 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLlP---ISSGEVHFAGRRIDRLtgrqlgPVRRRMQA----VFQDPts 102
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyeVTEGEILFKGEDITDL------PPEERARLgiflAFQYP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 103 slnPTMTvgaavgeglGVhrigtradraeRVAAMLDRVGLprgtaqnypgALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:cd03217 87 ---PEIP---------GV-----------KNADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEmGLAMLFIAHD---LDVVRhfCDRVMVLYLGRVMETG 236
Cdd:cd03217 134 GLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSG 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-224 |
9.94e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFaGRRIdrltgrQLGPVrrrmqavfqDPT-SSLNPTMTV 110
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------KLAYV---------DQSrDALDPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 GAAVGEGLGVHRIGTRaDRAERvaAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQA 190
Cdd:TIGR03719 404 WEEISGGLDIIKLGKR-EIPSR--AYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
170 180 190
....*....|....*....|....*....|....
gi 2075269590 191 GIVNLLLDLreeMGLAMLfIAHDldvvRHFCDRV 224
Cdd:TIGR03719 481 ALEEALLNF---AGCAVV-ISHD----RWFLDRI 506
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-227 |
1.10e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 125 TRAD--RAERVAAMLDRV-GLPRGTAQN---YPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLD 198
Cdd:PTZ00265 1324 TREDvkRACKFAAIDEFIeSLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
90 100
....*....|....*....|....*....
gi 2075269590 199 LREEMGLAMLFIAHDLDVVRHfCDRVMVL 227
Cdd:PTZ00265 1404 IKDKADKTIITIAHRIASIKR-SDKIVVF 1431
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-232 |
4.57e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQ-------LGPVRRRMQAVFqdPTSSLN 105
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagimLCPEDRKAEGII--PVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMTVGA---AVGEGLGVHRiGTRADRAERVAAMLdRVGLPrgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVS 182
Cdd:PRK11288 350 DNINISArrhHLRAGCLINN-RWEAENADRFIRSL-NIKTP--SREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2075269590 183 ALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-238 |
1.13e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLT-------GRQLGPVRRRMQAVFQDPT 101
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhGFALVTEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 SSLNPTMTVGAAVGEGLGV-HRIGTRADRAERVAAMldRVGLPrgTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:PRK10982 343 IGFNSLISNIRNYKNKVGLlDNSRMKSDTQWVIDSM--RVKTP--GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 181 VSALDVSVQAGIVNLLLDL-REEMGLAMlfIAHDLDVVRHFCDRVMVLYLGRV---METGRT 238
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELaKKDKGIII--ISSEMPELLGITDRILVMSNGLVagiVDTKTT 478
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
45-219 |
1.67e-09 |
|
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: 56.96 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 45 VVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTGRQLGPVRRRMQAVFQDPTSSLNPTMTVGAAVGEGLGVHRIG 124
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 125 TRADrAERVAAMLDRvgLPRGTaQNYPGA----LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSV-----QAGIVNL 195
Cdd:cd03290 112 AVTD-ACSLQPDIDL--LPFGD-QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKF 187
|
170 180
....*....|....*....|....
gi 2075269590 196 LLDLREemglAMLFIAHDLDVVRH 219
Cdd:cd03290 188 LQDDKR----TLVLVTHKLQYLPH 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-249 |
4.21e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrlTGRQLGPVRRRMQAVFQDPTSSLNp 106
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKIMREAVAIVPEGRRVFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAAVGEGLGVHRIGTRADRAERVAAMLDRVGLPRgtAQNyPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERR--IQR-AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 187 SVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVM--ETGRTADVFAAPRHPY 249
Cdd:PRK11614 171 IIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDALLANEAVRSAY 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-227 |
1.27e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 29 AVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDrltgrqlgpvrrrmqavFQDPTSS----- 103
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-----------------FNGPKSSqeagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 ------LN--PTMTVGAAVGegLG---VHRIGtRADRAERVA---AMLDRVGLPRGTAQNYpGALSGGQRQRVGIARALI 169
Cdd:PRK10762 82 giihqeLNliPQLTIAENIF--LGrefVNRFG-RIDWKKMYAeadKLLARLNLRFSSDKLV-GELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 170 VAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVL 227
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVF 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-248 |
1.32e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRhFCDRVMVLylgRVM 233
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVL---SNR 655
|
90
....*....|....*
gi 2075269590 234 ETGRTADVFAAPRHP 248
Cdd:PTZ00265 656 ERGSTVDVDIIGEDP 670
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-232 |
1.74e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLHAvrgvSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRidrltgrqlgpVRRRMQavfQDPTSs 103
Cdd:PRK11147 17 PLLDNA----ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDL-----------IVARLQ---QDPPR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 lNPTMTVGAAVGEGLG------------VHRIGTRA-----DRAERVAAMLD----------------RVGLPRGTAQNy 150
Cdd:PRK11147 78 -NVEGTVYDFVAEGIEeqaeylkryhdiSHLVETDPseknlNELAKLQEQLDhhnlwqlenrinevlaQLGLDPDAALS- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 151 pgALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLReemGlAMLFIAHDLDVVRHFCDRVMVLYLG 230
Cdd:PRK11147 156 --SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFISHDRSFIRNMATRIVDLDRG 229
|
..
gi 2075269590 231 RV 232
Cdd:PRK11147 230 KL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-241 |
3.37e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIS--------SGEVHFAGRRIDRLTGRQLGPVRRRM-QAVFQDP 100
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLpQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 TSSLNPTMTVGA---AVGEGLGVHRIGTRADRAERVAAMLDRVGLPRGTaqnypgaLSGGQRQRVGIARAL--------- 168
Cdd:PRK13547 97 AFSAREIVLLGRyphARRAGALTHRDGEIAWQALALAGATALVGRDVTT-------LSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 169 IVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-232 |
4.38e-08 |
|
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: 52.65 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIS---SGEVHFAGRRIDRLTGRQLGpvrrrmQAVFQDPTSSLNP 106
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG------EIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 107 TMTVGAavgeglgvhrigtradraervaaMLDRVGLPRGTAqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:cd03233 97 TLTVRE-----------------------TLDFALRCKGNE--FVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2075269590 187 SVQAGIVNLLLDLREEMGLAMLFIAH--DLDVVRHFcDRVMVLYLGRV 232
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLF-DKVLVLYEGRQ 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
33-250 |
5.43e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.99 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIDRLTgrqLGPVRRRMQAVFQDPT-------SSLN 105
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPIlfsgsirFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 106 PTMT-VGAAVGEGLgvhRIGTRADRAERVAAMLDRVGLPRGtaQNYpgalSGGQRQRVGIARALIVAPDLLIADEAVSAL 184
Cdd:cd03288 117 PECKcTDDRLWEAL---EIAQLKNMVKSLPGGLDAVVTEGG--ENF----SVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075269590 185 DVSVQAGIVNLLLDLREEMglAMLFIAHDLDVVRHfCDRVMVLYLGRVMETGRTADVFAAPRHPYT 250
Cdd:cd03288 188 DMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-236 |
1.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 21 WRPPLVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVL-RLLPISSGEVHFAGRridrltgrqlgpvrrrmqaVFQD 99
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVIRGT-------------------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 100 PTSSLNPTMTVGAAVGEGLGVHRigTRADRAERVAAMLDRVGLPRGTAQNYPGA----LSGGQRQRVGIARALIVAPDLL 175
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSPFDP--ERYERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLldLREEM-GLAMLFIAHDLdvvrHF---CDRVMVLYLGRVMETG 236
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDKC--IKDELrGKTRVLVTNQL----HFlsqVDRIILVHEGMIKEEG 821
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-218 |
1.18e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI--DRLTGRQlgpvrrrmQAVFQDPTSSLNPTMTV 110
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkDLCTYQK--------QLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 GAAVGEGLGVHRIGTRADRAERVAAMldrvglprGTAQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:PRK13540 92 RENCLYDIHFSPGAVGITELCRLFSL--------EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|....*....
gi 2075269590 190 AGIVNLLLDLREEMGLAMLFIAHDLDVVR 218
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-224 |
1.26e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhfagrridrltgrQLGP-VRrrMQAVFQDpTSSLNPTMTV 110
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIGEtVK--LAYVDQS-RDALDPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 111 GAAVGEGLGVHRIGTRaDRAERvaAMLDRVGLpRGTAQNYP-GALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:PRK11819 406 WEEISGGLDIIKVGNR-EIPSR--AYVGRFNF-KGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
170 180 190
....*....|....*....|....*....|....*
gi 2075269590 190 AGIVNLLLDLreeMGLAMLfIAHDldvvRHFCDRV 224
Cdd:PRK11819 482 RALEEALLEF---PGCAVV-ISHD----RWFLDRI 508
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-228 |
1.43e-07 |
|
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: 51.60 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 36 TVAPREILGVVGESGSGKTSlgraVLRLLpisSGEV------------------HFAGRRI----DRLTGRQLGPVRRrM 93
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKST----ALKIL---AGKLkpnlgkfddppdwdeildEFRGSELqnyfTKLLEGDVKVIVK-P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 94 QAVFQDPTSslnptmtVGAAVGEGLgvhrigTRADRAERVAAMLDRVGLpRGTAQNYPGALSGGQRQRVGIARALIVAPD 173
Cdd:cd03236 94 QYVDLIPKA-------VKGKVGELL------KKKDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 174 LLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLY 228
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-230 |
2.18e-07 |
|
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: 52.71 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 2 TALLDVNDLGVEFRLKSPPwrpplvlhAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRIdrl 81
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSSP--------AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--- 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 82 tgrqLGPVRRRMQAVFQDPTSSLNPTMTVGAavgEGLGVH-RI-GTRADRAERVAAM-LDRVGLPRgTAQNYPGALSGGQ 158
Cdd:TIGR01257 2004 ----LTNISDVHQNMGYCPQFDAIDDLLTGR---EHLYLYaRLrGVPAEEIEKVANWsIQSLGLSL-YADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075269590 159 RQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLG 230
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-236 |
4.61e-07 |
|
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: 51.48 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 24 PLVLHavrGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGrridrltgrQLGPVRRrmQAVFQDptSS 103
Cdd:TIGR00957 651 PPTLN---GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------SVAYVPQ--QAWIQN--DS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 LNPTMTVGAAVGEGLGVHRIgtradraERVAAMLDRVGLPRG--TAQNYPGA-LSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:TIGR00957 715 LRENILFGKALNEKYYQQVL-------EACALLPDLEILPSGdrTEIGEKGVnLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 181 VSALDVSVQAGIVNLLLDlreEMGL----AMLFIAHDLDVVRHfCDRVMVLYLGRVMETG 236
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIG---PEGVlknkTRILVTHGISYLPQ-VDVIIVMSGGKISEMG 843
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-236 |
4.94e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSL-----GRAVLRllpISSGEVHFAGRRIdrltgRQLGPVRRRMQAVF---QDPT 101
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLsatlaGREDYE---VTGGTVEFKGKDL-----LELSPEDRAGEGIFmafQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 -----SSLNPTMTVGAAVGEGLGVHRIgTRADRAERVAAMLDRVGLPRGT-AQNYPGALSGGQRQRVGIARALIVAPDLL 175
Cdd:PRK09580 89 eipgvSNQFFLQTALNAVRSYRGQEPL-DRFDFQDLMEEKIALLKMPEDLlTRSVNVGFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075269590 176 IADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHD---LDVVRHfcDRVMVLYLGRVMETG 236
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSG 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-241 |
7.51e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGR----RID-----RLTGRQLGPVRRRMQAVFQ 98
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsviAISaglsgQLTGIENIEFKMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 99 DPTSSLNPTMTVGAAVGEGLgvhrigtradraervaamldrvglpRGTAQNYpgalSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:PRK13546 118 KEIKAMTPKIIEFSELGEFI-------------------------YQPVKKY----SSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075269590 179 EAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-185 |
7.68e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 19 PPWRPPLVLHAV----------RGVSFTVAPREILGVVGESGSGKTSLgravLRLL----PIS-SGEVHFAGRRidRLTG 83
Cdd:PRK10938 255 PANEPRIVLNNGvvsyndrpilHNLSWQVNPGEHWQIVGPNGAGKSTL----LSLItgdhPQGySNDLTLFGRR--RGSG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 84 RQLGPVRRRMQAVfqdpTSSLNPTMTVGAAVG--------EGLGVHRigTRADRaERVAAM--LDRVGLPRGTAQNYPGA 153
Cdd:PRK10938 329 ETIWDIKKHIGYV----SSSLHLDYRVSTSVRnvilsgffDSIGIYQ--AVSDR-QQKLAQqwLDILGIDKRTADAPFHS 401
|
170 180 190
....*....|....*....|....*....|..
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-232 |
1.52e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSL-----GRAVLRLLpisSGEVHFAGRRIDrltgrqlgpvrrrmqavfqdptssl 104
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELamsvfGRSYGRNI---SGTVFKDGKEVD------------------------- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 npTMTVGAAVGEGL----------------------------GVHRIGTRADRAERVAA--MLDRVGLPRGTAQNYPGAL 154
Cdd:NF040905 328 --VSTVSDAIDAGLayvtedrkgyglnliddikrnitlanlgKVSRRGVIDENEEIKVAeeYRKKMNIKTPSVFQKVGNL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075269590 155 SGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRV 232
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-226 |
5.04e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 36 TVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVhFAGRRI----DRLTGRQLGPVrrrmQAVFQDPTSSLNPTMtVG 111
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKIsykpQYIKPDYDGTV----EDLLRSITDDLGSSY-YK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 AAVGEGLGVHRIgtradraervaamLDRvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAG 191
Cdd:PRK13409 435 SEIIKPLQLERL-------------LDK----------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*
gi 2075269590 192 IVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMV 226
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-212 |
5.85e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.82 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIssgevhFAGRRidrltgrqlgpVRRRMQAVFQDPTsslNPTMT 109
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV------YGGRL-----------TKPAKGKLFYVPQ---RPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGA---AVGEGLGVHRIGTRADRAERVAAMLDRVGL----PRG----TAQNYPGALSGGQRQRVGIARALIVAPDLLIAD 178
Cdd:TIGR00954 528 LGTlrdQIIYPDSSEDMKRRGLSDKDLEQILDNVQLthilEREggwsAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 2075269590 179 EAVSALDVSVQAGIVNLLldlrEEMGLAMLFIAH 212
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-224 |
6.13e-06 |
|
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: 47.62 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAP-REIL-------------GVVGESGSGKTSLGRAVLRLLPISSGEVHFA-GRRIDRLTgrqlgpvrrrmqav 96
Cdd:TIGR03719 9 RVSKVVPPkKEILkdislsffpgakiGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLP-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 97 fQDPtsSLNPTMTVGAAVGEGLG-VHRIGTR------------------ADRAERVAAMLDRVG---------------- 141
Cdd:TIGR03719 75 -QEP--QLDPTKTVRENVEEGVAeIKDALDRfneisakyaepdadfdklAAEQAELQEIIDAADawdldsqleiamdalr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 142 LPRGTAQnyPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLlldLREEMGlAMLFIAHDldvvRHFC 221
Cdd:TIGR03719 152 CPPWDAD--VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPG-TVVAVTHD----RYFL 221
|
...
gi 2075269590 222 DRV 224
Cdd:TIGR03719 222 DNV 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-226 |
6.99e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 41 EILGVVGESGSGKTSLGRAVLRLLPISSGEVHFaGRRI----DRLTGRQLGPVRRRMQAVFQD--PTSSLNptmtvgAAV 114
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKIsykpQYISPDYDGTVEEFLRSANTDdfGSSYYK------TEI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 115 GEGLGVHRIgtradraervaamLDRvglprgtaqnYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVN 194
Cdd:COG1245 440 IKPLGLEKL-------------LDK----------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|..
gi 2075269590 195 LLLDLREEMGLAMLFIAHDLDVVRHFCDRVMV 226
Cdd:COG1245 497 AIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-228 |
1.08e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 1.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMVLY 228
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-237 |
1.14e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.67 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 39 PREILGVVGESGSGKTSLGRAVLRLLPISSGevhfagrridrltgrqlgpvrrrmqavfqdptsslnptmtvgaavgegl 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG------------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 119 GVHRIGTRADRAERVAAMLDRVGLPRGtaqnypGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGI-----V 193
Cdd:smart00382 32 GVIYIDGEDILEEVLDQLLLIIVGGKK------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2075269590 194 NLLLDLREEMGLAMLFIAHDLDVVRhfcDRVMVLYLGRVMETGR 237
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLG---PALLRRRFDRRIVLLL 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-192 |
1.27e-05 |
|
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: 46.83 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 25 LVLHAVRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRridrltgrqlgpvrrrmqAVFQDPTSSL 104
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------------ISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 105 NPTmTVGAAVGEGLGV----HRIGTRADRAERVAAML---DRVGLPRGTAqnypgALSGGQRQRVGIARALIVAPDLLIA 177
Cdd:TIGR01271 499 MPG-TIKDNIIFGLSYdeyrYTSVIKACQLEEDIALFpekDKTVLGEGGI-----TLSGGQRARISLARAVYKDADLYLL 572
|
170
....*....|....*
gi 2075269590 178 DEAVSALDVSVQAGI 192
Cdd:TIGR01271 573 DSPFTHLDVVTEKEI 587
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-185 |
1.66e-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: 45.62 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAV-RGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPIsSGEVHFAGRRIDRLTGRQ----LGPVRRRMqAVFQDP-T 101
Cdd:cd03289 17 NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKwrkaFGVIPQKV-FIFSGTfR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 102 SSLNPTmtvgaavgeglgvhriGTRADraERVAAMLDRVGLpRGTAQNYPG-----------ALSGGQRQRVGIARALIV 170
Cdd:cd03289 95 KNLDPY----------------GKWSD--EEIWKVAEEVGL-KSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLS 155
|
170
....*....|....*
gi 2075269590 171 APDLLIADEAVSALD 185
Cdd:cd03289 156 KAKILLLDEPSAHLD 170
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-226 |
1.86e-05 |
|
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: 45.09 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 41 EILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRRI----DRLTGRQLGPVRRRMQAVFQDPTSS-------LNPtmt 109
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADYEGTVRDLLSSITKDFYTHpyfkteiAKP--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 vgaavgegLGVHRIgtradraervaamLDRVgLPRgtaqnypgaLSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQ 189
Cdd:cd03237 103 --------LQIEQI-------------LDRE-VPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2075269590 190 AGIVNLLLDLREEMGLAMLFIAHDLDVVRHFCDRVMV 226
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-242 |
2.09e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 42 ILGVVGESGSGKTSLGRAVLRLLPissgevHFAGRRIDrltgrqlgpVRRRMQAVFQDPTSsLNPTMTVGAAVGEGLGVH 121
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELS------HAETSSVV---------IRGSVAYVPQVSWI-FNATVRENILFGSDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 122 RIGtradRAERVAAMLDRVGLPRGTAQNYPGA----LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLl 197
Cdd:PLN03232 709 RYW----RAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC- 783
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2075269590 198 dLREEM-GLAMLFIAHDLdvvrHF---CDRVMVLYLGRVMETGRTADVF 242
Cdd:PLN03232 784 -MKDELkGKTRVLVTNQL----HFlplMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-222 |
2.41e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHfAGRRIDrltgrqlgpvrrrmQAVFQDPTSSLNPTMT 109
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLE--------------VAYFDQHRAELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 110 VGAAVGEGLGVHRIGTRaDRaeRVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVq 189
Cdd:PRK11147 400 VMDNLAEGKQEVMVNGR-PR--HVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET- 475
|
170 180 190
....*....|....*....|....*....|....*...
gi 2075269590 190 agivnllLDLREEMgLA-----MLFIAHDldvvRHFCD 222
Cdd:PRK11147 476 -------LELLEEL-LDsyqgtVLLVSHD----RQFVD 501
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-224 |
2.46e-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: 44.56 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 28 HAVRGVSFTVAPREILGVVGESGSGKTSL--------GRavLRLL-PISSGEVHFAGR----RIDRLTGrqLGPVrrrmQ 94
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaeGQ--RRYVeSLSAYARQFLGQmdkpDVDSIEG--LSPA----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 95 AVFQDpTSSLNPTMTVGaAVGE-----GLGVHRIGTRadraERVAAMLDrVGLPRGTAQNYPGALSGGQRQRVGIARALI 169
Cdd:cd03270 81 AIDQK-TTSRNPRSTVG-TVTEiydylRLLFARVGIR----ERLGFLVD-VGLGYLTLSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2075269590 170 VAPD--LLIADEAVSALDVSVQAGIVNLLLDLReEMGLAMLFIAHDLDVVRHfCDRV 224
Cdd:cd03270 154 SGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
154-228 |
2.81e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 2.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLY 228
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
39-196 |
4.01e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 39 PREILGVVGESGSGKTSLgravlrLLPISSGEVHFAGRRIDRLTGRQLGPV----RRRMQAVFQDPTSSLNPTMTVG--- 111
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTL------LKTIASNTDGFHIGVEGVITYDGITPEeikkHYRGDVVYNAETDVHFPHLTVGetl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 112 --AAVGEGLGVHRIG-TRADRAERVAAMLDRV-GLP--RGT--AQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSA 183
Cdd:TIGR00956 160 dfAARCKTPQNRPDGvSREEYAKHIADVYMATyGLShtRNTkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170
....*....|...
gi 2075269590 184 LDVSVQAGIVNLL 196
Cdd:TIGR00956 240 LDSATALEFIRAL 252
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
154-245 |
4.42e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLdLREEMGLAMLFIAHDLDVVRHfCDRVMVLYLGRVM 233
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVE 860
|
90
....*....|..
gi 2075269590 234 ETGRTADVFAAP 245
Cdd:PTZ00243 861 FSGSSADFMRTS 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-185 |
1.14e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 31 RGVSFTVAP-REIL-------------GVVGESGSGKTSLgravLRLL----PISSGEVHFA-GRRIDRLTgrqlgpvrr 91
Cdd:PRK11819 10 NRVSKVVPPkKQILkdislsffpgakiGVLGLNGAGKSTL----LRIMagvdKEFEGEARPApGIKVGYLP--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 92 rmqavfQDPtsSLNPTMTVGAAVGEGLG-VHRIGTRADR-----AERVAAM---------------------LDR----- 139
Cdd:PRK11819 77 ------QEP--QLDPEKTVRENVEEGVAeVKAALDRFNEiyaayAEPDADFdalaaeqgelqeiidaadawdLDSqleia 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2075269590 140 ---VGLPRGTAQnyPGALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:PRK11819 149 mdaLRCPPWDAK--VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-228 |
1.59e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075269590 154 LSGGQRQRVGIARALIVAPDLLIADEAVSALDVSVQAGIVNLLLDLREemGLAMLFIAHDLDVVRHFCDRVMVLY 228
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
126-179 |
1.72e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 126 RADRAERVAAMLDRVGLprgtaqnYP------GALSGGQRQRVGIARALIVAPDLLIADE 179
Cdd:NF033858 110 AAERRRRIDELLRATGL-------APfadrpaGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-192 |
2.63e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.15 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 30 VRGVSFTVAPREILGVVGESGSGKTSLGRAVLRLLPISSGEVHFAGRridrltgrqlgpvrrrmqAVFQDPTSSLNP-TM 108
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------------ISFSSQFSWIMPgTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 109 TVGAAVGEGLGVHR---IGTRADRAERVAAMLDRVGLPRGTAQNypgALSGGQRQRVGIARALIVAPDLLIADEAVSALD 185
Cdd:cd03291 115 KENIIFGVSYDEYRyksVVKACQLEEDITKFPEKDNTVLGEGGI---TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
....*..
gi 2075269590 186 VSVQAGI 192
Cdd:cd03291 192 VFTEKEI 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-185 |
2.88e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.59 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 33 VSFTVAPREILGVVGESGSGKTSLGRAVLRLLPiSSGEVHFAGRRIDRLTGRQLgpvrRRMQAVFQDPTSSLNPTMTVGA 112
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW----RKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 113 AVGEGLGVHRIGtradraeRVAamlDRVGLpRGTAQNYPG-----------ALSGGQRQRVGIARALIVAPDLLIADEAV 181
Cdd:TIGR01271 1313 DPYEQWSDEEIW-------KVA---EEVGL-KSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 2075269590 182 SALD 185
Cdd:TIGR01271 1382 AHLD 1385
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
132-225 |
4.27e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 132 RVAAMLDRVGLPRGTAQNYPGALSGGQRQRVGIARALIVAPDLLIADEAVSALDVSvqaGIVNLLLDLREEMGLAMLfIA 211
Cdd:PRK10636 128 RAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLIL-IS 203
|
90
....*....|....
gi 2075269590 212 HDLDVVRHFCDRVM 225
Cdd:PRK10636 204 HDRDFLDPIVDKII 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-199 |
6.34e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 32 GVSFTVAPREILGVVGESGSGKTSL-----GRAVLRLlpISSGEVHFAGRRIDRLTGRQLGPVRRrmqavfQD---PTSS 103
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGV--ITGGDRLVNGRPLDSSFQRSIGYVQQ------QDlhlPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 104 LNPTMTVGAAVGEGLGVhrigTRADRAERVAAMLDRVGLprgtaQNYPGALSG--------GQRQRVGIARALIVAPDLL 175
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSV----SKSEKMEYVEEVIKLLEM-----ESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLL 923
|
170 180
....*....|....*....|....*
gi 2075269590 176 I-ADEAVSALDVSVQAGIVNLLLDL 199
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-186 |
9.55e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 9.55e-04
10 20 30
....*....|....*....|....*....|..
gi 2075269590 155 SGGQRQRVGIARALIVAPDLLIADEAVSALDV 186
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
27-241 |
1.92e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 27 LHAVRGVSFTVAPREILGVVGESGSGKTSlGRAVLRLLPISSGEVHF------AGRRIDRLTGRQLGPVRRRMQAVFqdp 100
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWrf*twcANRRALRRTIG*HRPVR*GRRESF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075269590 101 TSSLNPTMtvgaaVGEGLGVHRIGTRAdraeRVAAMLDRVGLPRGtAQNYPGALSGGQRQRVGIARALIVAPDLLIADEA 180
Cdd:NF000106 102 SGRENLYM-----IGR*LDLSRKDARA----RADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075269590 181 VSALDVSVQAGIVNLLLDLREEmGLAMLFIAHDLDVVRHFCDRVMVLYLGRVMETGRTADV 241
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| |
