|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-320 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 609.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDAGRG------KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKN 74
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGlfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 75 IHNLSDDESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLyGGKKARLEKADELLEAVGLHKSFANRYPHEFSG 154
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGL-ASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 155 GQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEIT 234
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 235 DSSRLYQEPLHPYTQALLSAIPIPDPdvEDKRKRIILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLKEADDGHFV 314
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDP--ERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQV 318
|
....*.
gi 564753507 315 ACHLYD 320
Cdd:COG4608 319 ACHLAE 324
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-324 |
0e+00 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 520.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP---TEGEVTYRGKNIHNLSDDE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 83 SFQY-NRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLH--KSFANRYPHEFSGGQRQR 159
Cdd:COG0444 80 LRKIrGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEAR-ERAIELLERVGLPdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRL 239
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 240 YQEPLHPYTQALLSAIPIPDPdveDKRKRIILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLKEADDGHFVACHLY 319
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP---DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLY 315
|
....*
gi 564753507 320 DSDAR 324
Cdd:COG0444 316 EEEAP 320
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-316 |
2.70e-162 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 456.09 E-value: 2.70e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGK--------TVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHN 77
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 78 LSDDESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQR 157
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 238 RLYQEPLHPYTQALLSAIPIPDPDVEdKRKRI-ILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLkEADDGHFVAC 316
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLE-RNKTIqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL-EGSFRHAVSC 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-261 |
1.28e-148 |
|
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: 428.17 E-value: 1.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQ 85
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERR-ERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLH 245
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
250
....*....|....*.
gi 564753507 246 PYTQALLSAIPIPDPD 261
Cdd:COG1123 499 PYTRALLAAVPSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-317 |
5.40e-148 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 419.75 E-value: 5.40e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 2 QTGALLKVSRLKMHFDAGRG-----KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIH 76
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 77 NLSDDESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEIH-GLygGKKARLEKADELLEAVGLHKSFANRYPHEFSGG 155
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINtSL--SAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 156 QRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 236 SSRLYQEPLHPYTQALLSAIPIPDPDveDKRKRIILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLKEAdDGHFVA 315
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPD--DRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDY-DGRLVA 315
|
..
gi 564753507 316 CH 317
Cdd:PRK11308 316 CF 317
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-259 |
1.92e-131 |
|
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: 385.19 E-value: 1.92e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRG------KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLyQPTEGEVTYRGKNIHNLS 79
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 80 DDESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQR 159
Cdd:COG4172 354 RRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRL 239
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250 260
....*....|....*....|
gi 564753507 240 YQEPLHPYTQALLSAIPIPD 259
Cdd:COG4172 514 FDAPQHPYTRALLAAAPLLE 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-233 |
1.78e-125 |
|
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: 358.74 E-value: 1.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQ 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEI 233
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-257 |
7.47e-119 |
|
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: 342.94 E-value: 7.47e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfq 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRR-VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLyggkKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGL----PDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLH 245
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|..
gi 564753507 246 PYTQALLSAIPI 257
Cdd:COG1124 233 PYTRELLAASLA 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
1.89e-98 |
|
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: 300.83 E-value: 1.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDAGrGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP----TEGEVTYRGKNIH 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQG-GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 77 NLSDDESFQY-NRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLH--KSFANRYPHEFS 153
Cdd:COG4172 80 GLSERELRRIrGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAAR-ARALELLERVGIPdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 154 GGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEI 233
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564753507 234 TDSSRLYQEPLHPYTQALLSAIPIPDPDVEDKRKRIILKGE 274
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-315 |
8.30e-98 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 301.77 E-value: 8.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDPYASL 101
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAA-ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 182 LDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSAIPIPDPD 261
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPS 573
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564753507 262 vEDKRKRIILKGELPSPIDPpsgcvfRTRCPAATDictakkplLKEADDGHFVA 315
Cdd:PRK10261 574 -RQRPQRVLLSDDLPSNIHL------RGEEVAAVS--------LQCVGPGHYVA 612
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-317 |
1.01e-81 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 251.18 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 2 QTGALLKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP---TEGEVTYRGKNIHNL 78
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 79 SDDEsfqYNR----KIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKArLEKADELLEAVGLHKSFA--NRYPHEF 152
Cdd:PRK09473 87 PEKE---LNKlraeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEA-FEESVRMLDAVKMPEARKrmKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 153 SGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 233 ITDSSRLYQEPLHPYTQALLSAIPIPDPDVEdkrKRIILKGELPSPIDPPSGCVFRTRCPAATDICtAKKPLLKEADDGH 312
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRLDAEGE---SLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-SSAPPLEEFGPGR 318
|
....*
gi 564753507 313 FVACH 317
Cdd:PRK09473 319 LRACF 323
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-254 |
1.98e-80 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 245.52 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRG----KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNlsd 80
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 dESFQYN-RKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKkARLEKADELLEAVGLHKSFANRYPHEFSGGQRQR 159
Cdd:COG4167 80 -GDYKYRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAE-EREERIFATLRLVGLLPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRL 239
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237
|
250
....*....|....*
gi 564753507 240 YQEPLHPYTQALLSA 254
Cdd:COG4167 238 FANPQHEVTKRLIES 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-317 |
1.13e-79 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 245.81 E-value: 1.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFdaGRGKT-VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLY----QPTEGEVTYRGKNIHNLS 79
Cdd:PRK11022 2 ALLNVDKLSVHF--GDESApFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 80 DDESFQY-NRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGlYGGKKARLEKADELLEAVGLH--KSFANRYPHEFSGGQ 156
Cdd:PRK11022 80 EKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQ-GGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 157 RQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDS 236
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 237 SRLYQEPLHPYTQALLSAIPipdPDVEDKRKRIILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLKeADDGHFVAC 316
Cdd:PRK11022 239 HDIFRAPRHPYTQALLRALP---EFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALN-MLAGRQSKC 314
|
.
gi 564753507 317 H 317
Cdd:PRK11022 315 H 315
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-253 |
7.81e-78 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 247.31 E-value: 7.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 2 QTGALLKVSRLKMHFDAGRG---KTV---KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYqPTEGEVTYRGKNI 75
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRKGilkRTVdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 76 HNLSDDESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGG 155
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 156 QRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250
....*....|....*...
gi 564753507 236 SSRLYQEPLHPYTQALLS 253
Cdd:PRK15134 510 CERVFAAPQQEYTRQLLA 527
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-260 |
1.67e-76 |
|
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: 235.86 E-value: 1.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAG---RGKTVKAV-DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSD 80
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGglfGAKQRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEiHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRI 160
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 161 GIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLY 240
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
250 260
....*....|....*....|
gi 564753507 241 QEPlHPYTQALLSAIPIPDP 260
Cdd:TIGR02769 240 SFK-HPAGRNLQSAVLPEHP 258
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-268 |
5.30e-76 |
|
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: 242.12 E-value: 5.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTgaLLKVSRLKMHFDAGRgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPT---EGEVTYRGKNIHN 77
Cdd:COG1123 1 MTP--LLEVRDLSVRYPGGD---VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 78 LSDDEsfqYNRKIQMIFQDPYASLNPrLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQR 157
Cdd:COG1123 76 LSEAL---RGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGL--SRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|.
gi 564753507 238 RLYQEPlhpytqALLSAIPIPDPDVEDKRKR 268
Cdd:COG1123 229 EILAAP------QALAAVPRLGAARGRAAPA 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-261 |
5.83e-72 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 224.18 E-value: 5.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMH------FDAGRGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLS 79
Cdd:PRK10419 3 LLNVSGLSHHyahgglSGKHQHQTV--LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 80 DDESFQYNRKIQMIFQDPYASLNPRLTVREIMTEPMEiHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQR 159
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE---ITDS 236
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDK 239
|
250 260
....*....|....*....|....*
gi 564753507 237 SRLYqeplHPYTQALLSAIPIPDPD 261
Cdd:PRK10419 240 LTFS----SPAGRVLQNAVLPAFPV 260
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-317 |
1.26e-68 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 217.85 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP----TEGEVTYRGKNIHNLSD 80
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGR-VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DESFQY-NRKIQMIFQDPYASLNPRLTVREIMTEPMEiHGLYGGK-----KARLEKADELLEAVGL--HKSFANRYPHEF 152
Cdd:COG4170 81 RERRKIiGREIAMIFQEPSSCLDPSAKIGDQLIEAIP-SWTFKGKwwqrfKWRKKRAIELLHRVGIkdHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 153 SGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 233 ITDSSRLYQEPLHPYTQALLSAIPIPDPDVEDKRKRIILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLKeaDDGH 312
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRK--IKGH 317
|
....*
gi 564753507 313 FVACH 317
Cdd:COG4170 318 EFACH 322
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-267 |
5.28e-68 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 216.48 E-value: 5.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 19 GRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDpy 98
Cdd:COG1135 13 TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGL-HKsfANRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:COG1135 91 FNLLSSRTVAENVALPLEIAGV--PKAEIRKRVAELLELVGLsDK--ADAYPSQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSAIPI 257
Cdd:COG1135 167 ATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLN 246
|
250
....*....|
gi 564753507 258 PDPDVEDKRK 267
Cdd:COG1135 247 DELPEELLAR 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-247 |
3.83e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 209.57 E-value: 3.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 3 TGALLKVSRLKMHFDagrgkTVKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGKNIHNL 78
Cdd:COG3842 2 AMPALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 79 SddesfQYNRKIQMIFQDpYAsLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQ 158
Cdd:COG3842 73 P-----PEKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGV--PKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 159 RIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHD----LSMvkhiSDRIGVMYLGHMVEIT 234
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVG 218
|
250
....*....|...
gi 564753507 235 DSSRLYQEPLHPY 247
Cdd:COG3842 219 TPEEIYERPATRF 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-243 |
1.66e-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: 203.97 E-value: 1.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 18 AGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDp 97
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 YASLNPRlTVREIMTEPMEIHGLygGKKARLEKADELLEAVGL-HKsfANRYPHEFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:cd03258 91 FNLLSSR-TVFENVALPLEIAGV--PKAEIEERVLELLELVGLeDK--ADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-222 |
2.01e-63 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 200.41 E-value: 2.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGrGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY 86
Cdd:cd03255 1 IELKNLSKTYGGG-GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 -NRKIQMIFQDPYasLNPRLTVRE-IMTePMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03255 80 rRRHIGFVFQSFN--LLPDLTALEnVEL-PLLLAGV--PKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 165 ALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRI 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-234 |
4.10e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.88 E-value: 4.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGKNIHNLSD 80
Cdd:COG1136 3 PLLELRNLTKSYGTGEGE-VTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNilggLDRPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DESFQY-NRKIQMIFQDPYasLNPRLTVRE-IMTePMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQ 158
Cdd:COG1136 78 RELARLrRRHIGFVFQFFN--LLPELTALEnVAL-PLLLAGV--SRKERRERARELLERVGLGD-RLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 159 RIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEIT 234
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-261 |
1.86e-62 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 207.25 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 3 TGALLKVSRLKMHFDAGrGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYqPT------EGEVTYRGKNIH 76
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 77 NlSDDESFQYNR--KIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARLEKADeLLEAVGLHKSfANR---YPHE 151
Cdd:PRK15134 80 H-ASEQTLRGVRgnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILN-CLDRVGIRQA-AKRltdYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 152 FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260 270
....*....|....*....|....*....|
gi 564753507 232 EITDSSRLYQEPLHPYTQALLSAIPIPDPD 261
Cdd:PRK15134 237 EQNRAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-225 |
3.13e-62 |
|
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: 197.69 E-value: 3.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfqy 86
Cdd:cd03293 1 LEVRNVSKTYGGGGG-AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 nrkIQMIFQDPyaSLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03293 75 ---RGYVFQQD--ALLPWLTVLDNVALGLELQGV--PKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-256 |
6.33e-61 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 205.47 E-value: 6.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVT-------YRGK 73
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQK-IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 74 NIHNLSDDESFQYNR----KIQMIFQDPYASLNPRLTVREIMTEPMEIHGLYGGKKARLEkADELLEAVGLHKSFA--NR 147
Cdd:PRK10261 86 QVIELSEQSAAQMRHvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVE-AKRMLDQVRIPEAQTilSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 148 YPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYL 227
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
250 260
....*....|....*....|....*....
gi 564753507 228 GHMVEITDSSRLYQEPLHPYTQALLSAIP 256
Cdd:PRK10261 245 GEAVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-225 |
8.79e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 192.61 E-value: 8.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 2 QTGALLKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGKNIHN 77
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRliagLEKPTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 78 LSDDesfqynrkIQMIFQDPyaSLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQR 157
Cdd:COG1116 78 PGPD--------RGVVFQEP--ALLPWLTVLDNVALGLELRGV--PKAERRERARELLELVGL-AGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-243 |
1.50e-59 |
|
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: 190.91 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDagrgkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesfQY 86
Cdd:cd03300 1 IELENVSKFYG-----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDpYAsLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03300 71 KRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-247 |
1.27e-58 |
|
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: 189.78 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRGKTVkAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESF 84
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTV-GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRK-IQMIFQDpYAsLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIA 163
Cdd:cd03294 98 ELRRKkISMVFQS-FA-LLPHRTVLENVAFGLEVQGV--PRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 164 RALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
....
gi 564753507 244 LHPY 247
Cdd:cd03294 253 ANDY 256
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-266 |
1.97e-58 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.94 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 8 KVSRLKMHFDAGrGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYN 87
Cdd:PRK11153 3 ELKNISKVFPQG-GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 88 RKIQMIFQDpYASLNPRlTVREIMTEPMEIHGLygGKKARLEKADELLEAVGL-HKsfANRYPHEFSGGQRQRIGIARAL 166
Cdd:PRK11153 82 RQIGMIFQH-FNLLSSR-TVFDNVALPLELAGT--PKAEIKARVTELLELVGLsDK--ADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHP 246
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
250 260
....*....|....*....|.
gi 564753507 247 YTQALL-SAIPIPDPDVEDKR 266
Cdd:PRK11153 236 LTREFIqSTLHLDLPEDYLAR 256
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-232 |
4.99e-58 |
|
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: 187.49 E-value: 4.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 2 QTGALLKVSRLKMHFDagrGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDD 81
Cdd:COG1127 1 MSEPMIEVRNLTKSFG---DRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 82 ESFQYNRKIQMIFQDP--YASlnprLTVRE-IMTePMEIHGLYGGKKARlEKADELLEAVGLhKSFANRYPHEFSGGQRQ 158
Cdd:COG1127 76 ELYELRRRIGMLFQGGalFDS----LTVFEnVAF-PLREHTDLSEAEIR-ELVLEKLELVGL-PGAADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 159 RIGIARALALEPEFIVADEPISALD-VSVqAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-254 |
5.25e-58 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 188.46 E-value: 5.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGkniHNLS-DDESFQYNRkIQMIFQDPY 98
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHfGDYSYRSQR-IRMIFQDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASLNPRLTVREIMTEPMEIHGLYGGKkARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:PRK15112 98 TSLNPRQRISQILDFPLRLNTDLEPE-QREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 179 ISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSA 254
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-233 |
6.01e-58 |
|
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: 187.51 E-value: 6.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsdDESfQYNRKIQMIFQDpyA 99
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ--DPV-ELRRKIGYVIQQ--I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTVRE-IMTEPMeihgLYGGKKARL-EKADELLEAVGLH-KSFANRYPHEFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:cd03295 85 GLFPHMTVEEnIALVPK----LLKWPKEKIrERADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEI 233
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-317 |
6.37e-56 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 185.01 E-value: 6.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKS----------------TSGRV------LMRLyQP 63
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG-WVKAVDRVSMTLTEGEIRGLVGESGSGKSliakaicgvtkdnwrvTADRMrfddidLLRL-SP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 64 TEgevtyRGKNI-HNLSddesfqynrkiqMIFQDPYASLNPRLTV-REIMtepMEIHG-LYGGK-----KARLEKADELL 135
Cdd:PRK15093 81 RE-----RRKLVgHNVS------------MIFQEPQSCLDPSERVgRQLM---QNIPGwTYKGRwwqrfGWRKRRAIELL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 136 EAVGL--HKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLS 213
Cdd:PRK15093 141 HRVGIkdHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 214 MVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSAIPIPDPDVEDKRKRIILKGELPSPIDPPSGCVFRTRCPA 293
Cdd:PRK15093 221 MLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPY 300
|
330 340
....*....|....*....|....
gi 564753507 294 ATDICTaKKPLLKEADDgHFVACH 317
Cdd:PRK15093 301 AQRECI-ETPRLTGAKN-HLYACH 322
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-233 |
6.17e-55 |
|
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: 178.48 E-value: 6.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDPyaSLNP 103
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-----RNIGMVFQDY--ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:cd03259 86 HLTVAENIAFGLKLRGV--PKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564753507 184 VSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEI 233
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-255 |
8.44e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.03 E-value: 8.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnLSDDESFQ 85
Cdd:COG1126 1 MIEIENLHKSFGD-----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQdpyaSLN--PRLTVRE-IMTEPMEIHGLygGKKARLEKADELLEAVGL-HKsfANRYPHEFSGGQRQRIG 161
Cdd:COG1126 75 LRRKVGMVFQ----QFNlfPHLTVLEnVTLAPIKVKKM--SKAEAEERAMELLERVGLaDK--ADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 162 IARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQ 241
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|....
gi 564753507 242 EPLHPYTQALLSAI 255
Cdd:COG1126 226 NPQHERTRAFLSKV 239
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-231 |
3.43e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 179.52 E-value: 3.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDpyAS 100
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRRIGYVIQQ--IG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVRE-IMTEPmeihGLYGGKKARL-EKADELLEAVGL-HKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:COG1125 87 LFPHMTVAEnIATVP----RLLGWDKERIrARVDELLELVGLdPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-231 |
2.25e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.25 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFdagrgKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlsdDESFQY 86
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDPyaSLNPRLTVREImtepMEIHG-LYG-GKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIAR 164
Cdd:COG1131 72 RRRIGYVPQEP--ALYPDLTVREN----LRFFArLYGlPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 165 ALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-232 |
4.46e-53 |
|
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: 174.61 E-value: 4.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDpyAS 100
Cdd:cd03261 12 GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS--GA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:cd03261 88 LFDSLTVFENVAFPLREHTRLSEEEIR-EIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:cd03261 166 GLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-249 |
2.01e-51 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 174.27 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNR-KIQMIFQDpyASLNP 103
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQ--FALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:TIGR01186 85 HMTILQNTSLGPELLGW--PEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 184 VSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQ 249
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-242 |
2.42e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 170.62 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRgktvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESF 84
Cdd:COG3638 1 PMLELRNLSKRYPGGT----PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRKIQMIFQDPYasLNPRLTVreimtepME--IHGLYGGK-----------KARLEKADELLEAVGLhKSFANRYPHE 151
Cdd:COG3638 77 RLRRRIGMIFQQFN--LVPRLSV-------LTnvLAGRLGRTstwrsllglfpPEDRERALEALERVGL-ADKAYQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 152 FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
250
....*....|....*....
gi 564753507 232 ------EITDS--SRLYQE 242
Cdd:COG3638 227 fdgppaELTDAvlREIYGG 245
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-229 |
8.76e-51 |
|
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: 167.64 E-value: 8.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQYNRKIQMIFQDPYAS 100
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVGLVFQNPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 L-NPrlTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:cd03225 88 FfGP--TVEEEVAFGLENLGL--PEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-229 |
1.27e-50 |
|
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: 166.21 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFdagrgKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhNLSDDESFQY 86
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDPyaSLNPRLTVREIMTEPMeihglyggkkarlekadelleavglhksfanryphefSGGQRQRIGIARAL 166
Cdd:cd03229 75 RRRIGMVFQDF--ALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-245 |
3.21e-50 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 167.36 E-value: 3.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGRgktvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY 86
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDPyaSLNPRLTVRE-IMTEPMEIHGLYGG-----KKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRI 160
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLEnVLSGRLGRRSTWRSlfglfPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 161 GIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLY 240
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELT 233
|
....*
gi 564753507 241 QEPLH 245
Cdd:cd03256 234 DEVLD 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-231 |
4.49e-50 |
|
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: 166.35 E-value: 4.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlSDDESFQYNRKIQMIFQDPYASL-N 102
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPDDQLfA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 PrlTVREimtepmEI------HGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:COG1122 91 P--TVEE------DVafgpenLGL--PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
25-239 |
6.18e-50 |
|
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: 166.20 E-value: 6.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLY-----QPTEGEVTYRGKNIHNLSDDESfQYNRKIQMIFQDPya 99
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVL-ELRRRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 slNP-RLTVREIMTEPMEIHGlYGGKKARLEKADELLEAVGLHKSFANR-YPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHG-IKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRL 239
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-231 |
3.97e-49 |
|
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: 164.83 E-value: 3.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYA 99
Cdd:COG1120 12 GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNprLTVREIMtepmeIHGLY-------GGKKARLEKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:COG1120 87 PFG--LTVRELV-----ALGRYphlglfgRPSAEDREAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-242 |
2.17e-48 |
|
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: 162.72 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFdagrgKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNlsddESFQ 85
Cdd:COG4555 1 MIEVENLSKKY-----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYasLNPRLTVREIMTEPMEIHGLYGgkKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:COG4555 72 ARRQIGVLPDERG--LYDRLTVRENIRYFAELYGLFD--EELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
25-247 |
2.17e-48 |
|
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: 162.51 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpYAsLNPR 104
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFVFQH-YA-LFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVREIMTEPMEI-HGLYGGKKARL-EKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISAL 182
Cdd:cd03296 89 MTVFDNVAFGLRVkPRSERPPEAEIrAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 183 DVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPY 247
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
24-243 |
3.08e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.63 E-value: 3.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpYA 99
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGGRDVTDLPPKD-----RNIAMVFQS-YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 sLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:COG3839 86 -LYPHMTVYENIAFPLKLRKV--PKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHD----LSMvkhiSDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-228 |
5.18e-48 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 162.13 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 3 TGALLKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDE 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGG-----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 83 --------SFQYNRkiqmIFqdpyaslnPRLTVRE-IMT-------EPMEIHGLYGGKKAR-----LEKADELLEAVGLH 141
Cdd:COG0411 76 iarlgiarTFQNPR----LF--------PELTVLEnVLVaaharlgRGLLAALLRLPRARReereaRERAEELLERVGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 142 kSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDR 221
Cdd:COG0411 144 -DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
....*..
gi 564753507 222 IGVMYLG 228
Cdd:COG0411 223 IVVLDFG 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
21-232 |
1.94e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 159.45 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDpyAS 100
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGL-HKsfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:COG2884 90 LLPDRTVYENVALPLRVTGK--SRKEIRRRVREVLDLVGLsDK--AKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 180 SALDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:COG2884 166 GNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-228 |
1.96e-47 |
|
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: 159.91 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQy 86
Cdd:cd03219 1 LEVRGLTKRFGG-----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 nRKIQMIFQDPyaSLNPRLTVRE-IMT-------EPMEIHGLYGGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQ 158
Cdd:cd03219 75 -LGIGRTFQIP--RLFPELTVLEnVMVaaqartgSGLLLARARREEREARERAEELLERVGLAD-LADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 159 RIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-241 |
4.31e-47 |
|
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: 159.39 E-value: 4.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQ 85
Cdd:TIGR02315 1 MLEVENLSKVYPNG----KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDpYAsLNPRLTVREIMtepmeIHGLYGGK-----------KARLEKADELLEAVGLhKSFANRYPHEFSG 154
Cdd:TIGR02315 77 LRRRIGMIFQH-YN-LIERLTVLENV-----LHGRLGYKptwrsllgrfsEEDKERALSALERVGL-ADKAYQRADQLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 155 GQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV--- 231
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVfdg 228
|
250
....*....|....*
gi 564753507 232 ---EITDS--SRLYQ 241
Cdd:TIGR02315 229 apsELDDEvlRHIYG 243
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-229 |
5.88e-47 |
|
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: 158.08 E-value: 5.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhNLSDDESFQYNRKIQMIFQDpyASLNPR 104
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQ--FNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVRE-IMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:cd03262 91 LTVLEnITLAPIKVKGM--SKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564753507 184 VSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03262 168 PELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-178 |
6.85e-47 |
|
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: 155.50 E-value: 6.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlsDDESFQYNRKIQMIFQDPyaSLNPRLT 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT---DDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 107 VREIMTEPMEIHGLYGG-KKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:pfam00005 76 VRENLRLGLLLKGLSKReKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
26-255 |
1.93e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 157.65 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpYAsLNPRL 105
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARD-----RKIGFVFQH-YA-LFKHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTEPMEIhgLYGGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:TIGR00968 88 TVRDNIAFGLEI--RKHPKAKIKARVEELLELVQLEG-LGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 186 VQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSAI 255
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-230 |
4.23e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.74 E-value: 4.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYASLNprlTV 107
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WRRQVAYVPQEPALWGG---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 REIMTEPMEIHGlyggKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQ 187
Cdd:COG4619 91 RDNLPFPFQLRE----RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564753507 188 AQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:COG4619 167 RRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
25-243 |
4.76e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.54 E-value: 4.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGKNIH-NLSDDEsfqynRKIQMIFQDpYA 99
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTT----LLRiiagLETPDSGRIVLNGRDLFtNLPPRE-----RRVGFVFQH-YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 sLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:COG1118 86 -LFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-233 |
8.71e-46 |
|
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: 155.11 E-value: 8.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpYAsL 101
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIAMVFQN-YA-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMEIHGLYGGK-KARLEKADELLEAVGLhksfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:cd03301 84 YPHMTVYDNIAFGLKLRKVPKDEiDERVREVAELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEI 233
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-230 |
4.18e-45 |
|
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: 151.78 E-value: 4.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFdagrgKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlsdDESFQY 86
Cdd:cd03230 1 IEVRNLSKRY-----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDPyaSLNPRLTVREIMtepmeihglyggkkarlekadelleavglhksfanryphEFSGGQRQRIGIARAL 166
Cdd:cd03230 72 KRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
30-250 |
5.91e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 153.63 E-value: 5.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI---HNLSDDESFQYNRKIQMIFQDpYaSLNPRLT 106
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VREIMTE-PMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:PRK11124 99 VQQNLIEaPCRVLGL--SKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 186 VQAQVVNLLKKLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQeplhPYTQA 250
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ----PQTEA 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-232 |
6.43e-45 |
|
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: 163.08 E-value: 6.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYa 99
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDVF- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 slnprL---TVRE-ImtepmeihgLYGGKKARLEKADELLEAVGLHkSFANRYPH-----------EFSGGQRQRIGIAR 164
Cdd:COG2274 560 -----LfsgTIREnI---------TLGDPDATDEEIIEAARLAGLH-DFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 165 ALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVE 689
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-250 |
5.60e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 5.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDagrGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlsd 80
Cdd:COG1121 1 MMMMPAIELENLTVSYG---GRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 desfQYNRKI----QmifqdpYASLNPR--LTVREIMTepMeihGLYGG-------KKARLEKADELLEAVGLHkSFANR 147
Cdd:COG1121 72 ----RARRRIgyvpQ------RAEVDWDfpITVRDVVL--M---GRYGRrglfrrpSRADREAVDEALERVGLE-DLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 148 YPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRI----- 222
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVlllnr 214
|
250 260 270
....*....|....*....|....*....|.
gi 564753507 223 GVMYLGHMVEITDS---SRLYQEPLHPYTQA 250
Cdd:COG1121 215 GLVAHGPPEEVLTPenlSRAYGGPVALLAHG 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-225 |
9.26e-44 |
|
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: 148.30 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYas 100
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 lnprL---TVREimtepmeihglyggkkarlekadELLeavglhksfanryphefSGGQRQRIGIARALALEPEFIVADE 177
Cdd:cd03228 87 ----LfsgTIRE-----------------------NIL-----------------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVL 167
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-232 |
9.41e-44 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 149.81 E-value: 9.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGrGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDE-SF 84
Cdd:TIGR02211 1 LLKCENLGKRYQEG-KLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRKIQMIFQdpYASLNPRLTVREIMTEPMEIhglygGKKARLE---KADELLEAVGL-HKSfaNRYPHEFSGGQRQRI 160
Cdd:TIGR02211 80 LRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI-----GKKSVKEakeRAYEMLEKVGLeHRI--NHRPSELSGGERQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 161 GIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHIsDRIGVMYLGHMVE 232
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-280 |
4.44e-43 |
|
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: 151.49 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 42 LVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesfQYNRKIQMIFQDpYAsLNPRLTVREIMTEPMEIHGLy 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-----PHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 122 gGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEK 201
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 202 GLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSAIPIPD-PDVEDKRKRIILKGELPSPID 280
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEaTVIERKSEQVVLAGVEGRRCD 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-231 |
7.95e-43 |
|
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: 147.52 E-value: 7.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 9 VSRLKMHFDagrgkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNlsddESFQYNR 88
Cdd:cd03265 3 VENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 89 KIQMIFQDPyaSLNPRLTVREimtePMEIHG-LYGGKKARL-EKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03265 74 RIGIVFQDL--SVDDELTGWE----NLYIHArLYGVPGAERrERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-243 |
9.94e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 148.94 E-value: 9.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDagrGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSD 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFD---GKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DesfqyNRKIQMIFQDpYAsLNPRLTVREIMTepmeiHGLYGGKKARLEKADELLEA---VGLhKSFANRYPHEFSGGQR 157
Cdd:PRK09452 84 E-----NRHVNTVFQS-YA-LFPHMTVFENVA-----FGLRMQKTPAAEITPRVMEAlrmVQL-EEFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHD----LSMvkhiSDRIGVMYLGHMVEI 233
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQD 226
|
250
....*....|
gi 564753507 234 TDSSRLYQEP 243
Cdd:PRK09452 227 GTPREIYEEP 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
30-250 |
1.22e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 145.16 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI---HNLSDDESFQYNRKIQMIFQDpYaSLNPRLT 106
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VREIMTE-PMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:COG4161 99 VMENLIEaPCKVLGL--SKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 186 VQAQVVNLLKKLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLyqepLHPYTQA 250
Cdd:COG4161 176 ITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEA 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-233 |
1.48e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 152.24 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYaslnpr 104
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTF------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 L---TVRE-ImtepmeihgLYGGKKARLEKADELLEAVGLHKsFANRYPH-----------EFSGGQRQRIGIARALALE 169
Cdd:COG1132 425 LfsgTIREnI---------RYGRPDATDEEVEEAAKAAQAHE-FIEALPDgydtvvgergvNLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 170 PEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVEI 233
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-238 |
2.40e-41 |
|
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: 144.11 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 3 TGALLKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDE 82
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAG-ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 83 SFQY-NRKIQMIFQdpyaS--LNPRLTVRE-IMTePMEihgLYGGKKARlEKADELLEAVGL-HKsfANRYPHEFSGGQR 157
Cdd:COG4181 84 RARLrARHVGFVFQ----SfqLLPTLTALEnVML-PLE---LAGRRDAR-ARARALLERVGLgHR--LDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSS 237
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
.
gi 564753507 238 R 238
Cdd:COG4181 232 A 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-254 |
2.50e-41 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.84 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP----TEGEVTYRGKNIHNLSddesfQYNRKIQMIFQDPYASLN 102
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCA-----LRGRKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 PRLTVREIMTEPmeihGLYGGKKARLEKADELLEAVGLH--KSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK10418 94 PLHTMHTHARET----CLALGKPADDATLTAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSA 254
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-222 |
1.45e-40 |
|
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: 141.52 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsddesfqyNRKIQMIFQDPYASLNPRL 105
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTepMeihGLYGG-------KKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:cd03235 86 SVRDVVL--M---GLYGHkglfrrlSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564753507 179 ISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRI 222
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-257 |
1.74e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 146.33 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRK-IQMIFQDpyASLNPR 104
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVREIMTEPMEIHGLYGGKkaRLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDV 184
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEE--RREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 185 SVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSAIPI 257
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-229 |
6.09e-40 |
|
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: 137.76 E-value: 6.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQYNRKIQMIFQdpyasl 101
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 nprltvreimtepmeihglyggkkarlekadelleavglhksfanrypheFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 182 LDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd00267 111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-253 |
7.45e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.94 E-value: 7.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLY--QP---TEGEVTYRGKNIHNLSDDESfQYNRKIQMIFQDPya 99
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDIYDPDVDVV-ELRRRVGMVFQKP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 slNP-RLTVREIMTEPMEIHGLYggKKARL-EKADELLEAVG--------LHKSfanryPHEFSGGQRQRIGIARALALE 169
Cdd:COG1117 102 --NPfPKSIYDNVAYGLRLHGIK--SKSELdEIVEESLRKAAlwdevkdrLKKS-----ALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 170 PEFIVADEPISALD-VSVqAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYT 248
Cdd:COG1117 173 PEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
....*
gi 564753507 249 QALLS 253
Cdd:COG1117 250 EDYIT 254
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-243 |
9.02e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.82 E-value: 9.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesfQ 85
Cdd:PRK11607 19 LLEIRNLTKSFDG-----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDpYAsLNPRLTVREIMTepmeihglYGGKKARLEKAD------ELLEAVGLHKsFANRYPHEFSGGQRQR 159
Cdd:PRK11607 89 YQRPINMMFQS-YA-LFPHMTVEQNIA--------FGLKQDKLPKAEiasrvnEMLGLVHMQE-FAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSV----QAQVVNLLKKLqkekGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
....*...
gi 564753507 236 SSRLYQEP 243
Cdd:PRK11607 234 PEEIYEHP 241
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-243 |
1.09e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 141.05 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDPYASLNpR 104
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTV-REIMTEPMEIhGLyGGKKARlEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:TIGR04521 98 ETVyKDIAFGPKNL-GL-SEEEAE-ERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 184 VSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-255 |
1.76e-39 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 140.06 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDAGRGktvkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGK-----NI 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 76 HNLSDDEsfqynRKIQM------IFQDPYASLNPRLTVREIMTEP-MEI---HglYGGKKArleKADELLEAVGLHKSFA 145
Cdd:PRK11701 76 YALSEAE-----RRRLLrtewgfVHQHPRDGLRMQVSAGGNIGERlMAVgarH--YGDIRA---TAGDWLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 146 NRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260 270
....*....|....*....|....*....|..
gi 564753507 226 YLGHMVE--ITDssRLYQEPLHPYTQALLSAI 255
Cdd:PRK11701 226 KQGRVVEsgLTD--QVLDDPQHPYTQLLVSSV 255
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-211 |
1.85e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 140.00 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDaGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESf 84
Cdd:COG4525 2 SMLTVRHVSVRYP-GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 qynrkiqMIFQDpyASLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIAR 164
Cdd:COG4525 80 -------VVFQK--DALLPWLNVLDNVAFGLRLRGV--PKAERRARAEELLALVGLAD-FARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 165 ALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHD 211
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-225 |
4.66e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.39 E-value: 4.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESF 84
Cdd:COG1129 3 PLLEMRGISKSFGG-----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QynRKIQMIFQDPyaSLNPRLTVRE---IMTEPMEiHGLYGGKKARlEKADELLEAVGLHKSfanryPH----EFSGGQR 157
Cdd:COG1129 78 A--AGIAIIHQEL--NLVPNLSVAEnifLGREPRR-GGLIDWRAMR-RRARELLARLGLDID-----PDtpvgDLSVAQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-255 |
6.64e-39 |
|
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: 138.42 E-value: 6.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKmHFDAGRgktvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKN-----IHNLS 79
Cdd:TIGR02323 2 PLLQVSGLS-KSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 80 DDESFQYNR-KIQMIFQDPYASLnpRLTVR---EIMTEPMEI---HglYGGKKArleKADELLEAVGLHKSFANRYPHEF 152
Cdd:TIGR02323 77 EAERRRLMRtEWGFVHQNPRDGL--RMRVSagaNIGERLMAIgarH--YGNIRA---TAQDWLEEVEIDPTRIDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 153 SGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250 260
....*....|....*....|...
gi 564753507 233 ITDSSRLYQEPLHPYTQALLSAI 255
Cdd:TIGR02323 230 SGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-232 |
8.99e-39 |
|
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: 136.58 E-value: 8.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfqyNRKIQMIFQDPyaSL 101
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRIGALIEAP--GF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREimtePMEIHG-LYGGKKARlekADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:cd03268 84 YPNLTARE----NLRLLArLLGIRKKR---IDEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-231 |
1.12e-38 |
|
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: 135.26 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQYNRKIQMIFQdpya 99
Cdd:cd03214 10 GGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 slnprltvreimtepmeihglyggkkarlekadeLLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:cd03214 81 ----------------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-242 |
1.38e-38 |
|
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: 143.40 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYR-GKNIHNLSD---D 81
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKpgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 82 ESFQYNRKIQMIFQDpyASLNPRLTVREIMTEPMeihGLYGGKKARLEKADELLEAVGLHKSFA----NRYPHEFSGGQR 157
Cdd:TIGR03269 359 GRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAI---GLELPDELARMKAVITLKMVGFDEEKAeeilDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
....*
gi 564753507 238 RLYQE 242
Cdd:TIGR03269 514 EIVEE 518
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-231 |
2.56e-38 |
|
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: 133.71 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQy 86
Cdd:cd03216 1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 nRKIQMIFQdpyaslnprltvreimtepmeihglyggkkarlekadelleavglhksfanrypheFSGGQRQRIGIARAL 166
Cdd:cd03216 75 -AGIAMVYQ--------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-242 |
4.57e-38 |
|
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: 142.59 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIFQDPYasLnPRL 105
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA---SWRRQIAWVPQNPY--L-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTepmeihgLYGGK--KARLEKAdelLEAVGLHkSFANRYPH-------E----FSGGQRQRIGIARALALEPEF 172
Cdd:COG4988 426 TIRENLR-------LGRPDasDEELEAA---LEAAGLD-EFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-225 |
8.30e-38 |
|
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: 134.34 E-value: 8.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETfGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRG-------KNIhNLSDDEsfqynRKIQMIFQDpyASLN 102
Cdd:cd03297 17 IDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI-NLPPQQ-----RKIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 PRLTVREIMTepmeihglYGGKKAR----LEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:cd03297 88 PHLNVRENLA--------FGLKRKRnredRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 179 ISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-243 |
1.55e-37 |
|
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: 134.00 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfqyNRKIQMIFQDpYAsLNPRLT 106
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQN-YA-LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VREIMTEPMEIhgLYGGKKARLEKADELLEAVGL-HksFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:cd03299 88 VYKNIAYGLKK--RKVDKKEIERKVLEIAEMLGIdH--LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 186 VQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-230 |
2.10e-37 |
|
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: 133.30 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 23 TVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDpyASLN 102
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 PRLTVREIMTEPMEIHGlYGGKKARlEKADELLEAVGL-HKSfaNRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:cd03292 91 PDRNVYENVAFALEVTG-VPPREIR-KRVPAALELVGLsHKH--RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564753507 182 LDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03292 167 LDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-253 |
5.50e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.56 E-value: 5.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 8 KVSRLKMHFDAGRGKTVKavdGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIH---------NL 78
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLK---GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 79 SDDESFQYNR-KIQMIFQdpYASLNPRLTVRE-IMTEPMEIHGLygGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQ 156
Cdd:PRK10619 82 ADKNQLRLLRtRLTMVFQ--HFNLWSHMTVLEnVMEAPIQVLGL--SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 157 RQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDS 236
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*..
gi 564753507 237 SRLYQEPLHPYTQALLS 253
Cdd:PRK10619 237 EQLFGNPQSPRLQQFLK 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-219 |
3.23e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 130.71 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGKTvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQ 85
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQT-DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 Y-NRKIQMIFQdpYASLNPRLTVREIMTEPMeihgLYGGKKAR--LEKADELLEAVGLHKSfANRYPHEFSGGQRQRIGI 162
Cdd:PRK11629 84 LrNQKLGFIYQ--FHHLLPDFTALENVAMPL----LIGKKKPAeiNSRALEMLAAVGLEHR-ANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 163 ARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHIS 219
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-243 |
4.02e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.69 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlsDDESFQyNRKIQMIFQDpYAs 100
Cdd:PRK11432 17 GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQ-QRDICMVFQS-YA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGV--PKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-232 |
5.68e-36 |
|
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: 129.97 E-value: 5.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDP--YASl 101
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LRSQIGLVSQEPvlFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 nprlTVRE-ImtepmeihgLYGGKKARLEKADELLEAVGLHK---SFANRY-----PH--EFSGGQRQRIGIARALALEP 170
Cdd:cd03249 92 ----TIAEnI---------RYGKPDATDEEVEEAAKKANIHDfimSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 171 EFIVADEPISALDVSVQAQVVNLLKKLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-232 |
2.71e-35 |
|
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: 128.11 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIFQDPYas 100
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK---SLRSMIGVVLQDTF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRlTVREIMTepmeihglYGGKKARLEKADELLEAVGLHkSFANRYP-----------HEFSGGQRQRIGIARALALE 169
Cdd:cd03254 88 LFSG-TIMENIR--------LGRPNATDEEVIEAAKEAGAH-DFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 170 PEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIE 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-233 |
3.12e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNihnLSDDESFQYNRKIQMIFQdpyaslNPR- 104
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVRRQVGMVFQ------NPDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 ----LTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK13635 93 qfvgATVQDDVAFGLENIGV--PREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEI 233
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-253 |
1.14e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 127.27 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ-----PTEGEVTYRGKNIHNlSDDESFQYNRKIQMIFQdpYASL 101
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQ--YPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANR---YPHEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 179 ISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLS 253
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVT 249
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
229-318 |
1.42e-34 |
|
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: 121.70 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 229 HMVEITDSSRLYQEPLHPYTQALLSAIPIP-DPDvedkRKRIILKGELPSPIDPPSGCVFRTRCPAATDICTAKKPLLKE 307
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRD----RKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVE 76
|
90
....*....|.
gi 564753507 308 ADDGHFVACHL 318
Cdd:TIGR01727 77 IAEGHRVACHL 87
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-252 |
1.48e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 126.36 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQ----MIFQD 96
Cdd:PRK09493 12 GPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-----RLIRqeagMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 97 PYasLNPRLTVRE-IMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVA 175
Cdd:PRK09493 86 FY--LFPHLTALEnVMFGPLRVRGA--SKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALL 252
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
21-260 |
2.74e-34 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 128.96 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP--TEGEVTYRGKNIHNLSddesfQYNRKIQMIFQDpY 98
Cdd:TIGR03258 17 ANTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAP-----PHKRGLALLFQN-Y 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 AsLNPRLTVREIMTepmeihglYGGKKARLEKAD------ELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:TIGR03258 89 A-LFPHLKVEDNVA--------FGLRAQKMPKADiaervaDALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKE-KGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQAL 251
Cdd:TIGR03258 159 LLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEF 238
|
....*....
gi 564753507 252 LSAIPIPDP 260
Cdd:TIGR03258 239 LGAANILPA 247
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-240 |
3.04e-34 |
|
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: 125.42 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGkniHNLSDDESFQYNRKIQMIFQDPYa 99
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASLRRQIGLVSQDVF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 slnprL---TVRE-IMtepmeihglYGGKKARLEKADELLEAVGLHkSFANRYPHEF-----------SGGQRQRIGIAR 164
Cdd:cd03251 87 -----LfndTVAEnIA---------YGRPGATREEVEEAARAANAH-EFIMELPEGYdtvigergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 165 ALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSRLY 240
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-253 |
6.49e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 125.25 E-value: 6.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGevTYRGKNIH-----NLSDDESF--QYNRKIQM 92
Cdd:PRK11264 14 HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG--TIRVGDITidtarSLSQQKGLirQLRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 93 IFQDpyASLNPRLTVRE-IMTEPMEIHGLygGKKARLEKADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPE 171
Cdd:PRK11264 90 VFQN--FNLFPHRTVLEnIIEGPVIVKGE--PKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 172 FIVADEPISALDVSVQAQVVNLLKKLQKEKgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQAL 251
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
..
gi 564753507 252 LS 253
Cdd:PRK11264 244 LE 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-231 |
9.55e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.99 E-value: 9.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDagrgkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhNLSDDESFQY 86
Cdd:COG4152 2 LELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 ---NRkiqmifqdpyaSLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIA 163
Cdd:COG4152 76 lpeER-----------GLYPKMKVGEQLVYLARLKGL--SKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 164 RALALEPEFIVADEPISALD-VSvqaqvVNLLKKL---QKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-225 |
1.59e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 124.33 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQ 85
Cdd:PRK11300 5 LLSVSGLMMRFGG-----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP---GHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRK-IQMIFQDpyASLNPRLTVREIMTEPMEIH---GLYGG----------KKARLEKADELLEAVGLhKSFANRYPHE 151
Cdd:PRK11300 77 IARMgVVRTFQH--VRLFREMTVIENLLVAQHQQlktGLFSGllktpafrraESEALDRAATWLERVGL-LEHANRQAGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 152 FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-243 |
1.60e-33 |
|
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: 129.89 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 2 QTGALLKVSRLKMHFDagrGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDD 81
Cdd:COG4987 329 PGGPSLELEDVSFRYP---GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 82 esfQYNRKIQMIFQDPY---ASL--NPRLtVREIMTEpmeihglyggkkARLEKAdelLEAVGLHKsFANRYPH------ 150
Cdd:COG4987 406 ---DLRRRIAVVPQRPHlfdTTLreNLRL-ARPDATD------------EELWAA---LERVGLGD-WLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 151 -E----FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHIsDRIGVM 225
Cdd:COG4987 466 gEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVL 542
|
250
....*....|....*...
gi 564753507 226 YLGHMVEITDSSRLYQEP 243
Cdd:COG4987 543 EDGRIVEQGTHEELLAQN 560
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-211 |
1.69e-33 |
|
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: 122.59 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfqYNRKIQMIFqdPYASLNPRLTV 107
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRRRLAYLG--HADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 REIMtepmEIHGLYGGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQ 187
Cdd:COG4133 93 RENL----RFWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 564753507 188 AQVVNLLKKlQKEKGLTFLFIAHD 211
Cdd:COG4133 168 ALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
29-227 |
3.09e-33 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 123.37 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI-------HNLSDDESFQYNR---KIQMIFQdpy 98
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRRQLQRirtRLGMVFQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 aSLN--PRLTVRE-IMTEPMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVA 175
Cdd:COG4598 103 -SFNlwSHMTVLEnVIEAPVHVLGR--PKAEAIERAEALLAKVGLAD-KRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRigVMYL 227
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSH--VVFL 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-231 |
4.03e-33 |
|
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: 122.09 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNlsddESFQYNRKIQMIFQDpyASL 101
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEARRRLGFVSDS--TGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMEIHGLYGGK-KARLEKADELLEAvglhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:cd03266 90 YDRLTARENLEYFAGLYGLKGDElTARLEELADRLGM----EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564753507 181 ALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03266 166 GLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-228 |
1.07e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 13 KMHFDAGRGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsddesfQYNRKIQM 92
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK------ERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 93 IFQDPYASLNpRLTVREIMTEPMEIHGlyggkkARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:cd03226 76 VMQDVDYQLF-TDSVREELLLGLKELD------AGNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRigVMYLG 228
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDR--VLLLA 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-243 |
1.33e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 124.04 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpYAs 100
Cdd:PRK10851 13 GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVGFVFQH-YA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVREIMTepmeiHGLY-------GGKKARLEKADELLEAVGL-HksFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:PRK10851 85 LFRHMTVFDNIA-----FGLTvlprrerPNAAAIKAKVTQLLEMVQLaH--LADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-222 |
4.27e-32 |
|
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: 119.46 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTgaLLKVSRLKMHFD--AGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGK----N 74
Cdd:COG4778 1 MTT--LLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 75 IHNLSDDESFQYNRkiQMIfqdPYAS--LN--PRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLHKSFANRYPH 150
Cdd:COG4778 79 LAQASPREILALRR--RTI---GYVSqfLRviPRVSALDVVAEPLLERGV--DREEARARARELLARLNLPERLWDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 151 EFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRV 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-231 |
1.36e-31 |
|
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: 117.77 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFdagrgKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVtyrgknihnLSDDESFQY 86
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV---------LFDGKPLDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03269 67 AARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGL--KKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 167 ALEPEFIVADEPISALDVsVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03269 144 IHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-228 |
1.40e-31 |
|
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: 117.99 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFdagRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNlsddESFQY 86
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDpyASLNPRLTVREIMTEPMEIHGLYggKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03263 74 RQSLGYCPQF--DALFDELTVREHLRFYARLKGLP--KSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-249 |
2.07e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.48 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ-----PTEGEVTYRGKNIHNLsddESFQYNRKIQMIFQDPY 98
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKM---DVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASlnPRLTVREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRY---PHEFSGGQRQRIGIARALALEPEFIVA 175
Cdd:PRK14247 93 PI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQ 249
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTE 242
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-231 |
2.11e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 124.59 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPyas 100
Cdd:TIGR03375 475 GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD---LRRNIGYVPQDP--- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 lnpRL---TVREIMTepmeihglYGgkkARLEKADELLEAV---GLHkSFANRYPHEF-----------SGGQRQRIGIA 163
Cdd:TIGR03375 549 ---RLfygTLRDNIA--------LG---APYADDEEILRAAelaGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALA 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 164 RALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKhISDRIGVMYLGHMV 231
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIV 678
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-231 |
2.48e-31 |
|
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: 117.31 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDP---YAS 100
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRNIGYVPQDVtlfYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVreimtepmeihGLYGGKKARLEKADELLeavGLHKsFANRYPHEF-----------SGGQRQRIGIARALALE 169
Cdd:cd03245 94 LRDNITL-----------GAPLADDERILRAAELA---GVTD-FVNKHPNGLdlqigergrglSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 170 PEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKhISDRIGVMYLGHMV 231
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-253 |
3.19e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 3 TGALLKVSRLKMHFdagrGKTvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRL--YQP---TEGEVTYRGKNIHN 77
Cdd:PRK14239 2 TEPILQVSDLSVYY----NKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 78 LSDDeSFQYNRKIQMIFQDPyaslNP-RLTVREIMTEPMEIHGLYggKKARLEKADEL-LEAVGLHKSFANRYpHE---- 151
Cdd:PRK14239 77 PRTD-TVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIK--DKQVLDEAVEKsLKGASIWDEVKDRL-HDsalg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 152 FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250 260
....*....|....*....|..
gi 564753507 232 EITDSSRLYQEPLHPYTQALLS 253
Cdd:PRK14239 227 EYNDTKQMFMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-265 |
5.31e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRK-IQMIFQDPYASLNP 103
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKrIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEP----MEIhglyggKKARlEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:PRK13646 101 DTVEREIIFGPknfkMNL------DEVK-NYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPlhpyTQALLSAIPIPD 259
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK----KKLADWHIGLPE 249
|
250
....*....|.
gi 564753507 260 -----PDVEDK 265
Cdd:PRK13646 250 ivqlqYDFEQK 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
5.47e-31 |
|
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: 116.80 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynrkiQMIFQDpyASLNPRLT 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR--------MVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VREIMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSV 186
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 187 QAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM------YLGHMVEI 233
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEV 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-231 |
7.02e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 7.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlSDDESF-QYNRKIQMIFQDPYASLNPR 104
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--YDKKSLlEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVREIMTEPMEIhglyGGKKARLEK-ADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:PRK13639 95 TVEEDVAFGPLNL----GLSKEEVEKrVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 184 VSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13639 170 PMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-238 |
1.91e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGkniHNLSDDESF 84
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRKIQMIFQDPYASLnPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIAR 164
Cdd:PRK13650 78 DIRHKIGMVFQNPDNQF-VGATVEDDVAFGLENKGI--PHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 165 ALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKhISDRIGVMYLGHmVEITDSSR 238
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTSTPR 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-240 |
2.05e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.73 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDagRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNihnLSDDESFQ 85
Cdd:PRK13642 4 ILEVENLVFKYE--KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYASLnPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:PRK13642 79 LRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGI--PREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSRLY 240
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-249 |
2.24e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.91 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAgrgktvKAV-DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ------PTEGEVTYRGKNIHNL 78
Cdd:PRK14246 10 VFNISRLYLYIND------KAIlKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 79 sddESFQYNRKIQMIFQDPyaSLNPRLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLHKSFANRY---PHEFSGG 155
Cdd:PRK14246 84 ---DAIKLRKEVGMVFQQP--NPFPHLSIYDNIAYPLKSHGIKEKREIK-KIVEECLRKVGLWKEVYDRLnspASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 156 QRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
250
....*....|....
gi 564753507 236 SSRLYQEPLHPYTQ 249
Cdd:PRK14246 236 SNEIFTSPKNELTE 249
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-243 |
2.53e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNR-KIQMIFQDPYASLNP 103
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRkKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEihglYGGKKAR-LEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISAL 182
Cdd:PRK13634 101 ETVEKDICFGPMN----FGVSEEDaKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 183 DVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-211 |
2.91e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.98 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGRGkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESF 84
Cdd:PRK10535 3 ALLELKDIRRSYPSGEE-QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRK-IQMIFQDPYasLNPRLTVreimTEPMEIHGLYGG--KKARLEKADELLEAVGLHKSfANRYPHEFSGGQRQRIG 161
Cdd:PRK10535 82 QLRREhFGFIFQRYH--LLSHLTA----AQNVEVPAVYAGleRKQRLLRAQELLQRLGLEDR-VEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564753507 162 IARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQkEKGLTFLFIAHD 211
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHD 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-243 |
3.20e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 117.64 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAGrgktVKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGKNIHNLSD 80
Cdd:PRK11650 2 AGLKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DEsfqynRKIQMIFQDpYAsLNPRLTVREIMTEPMEIHGLygGK---KARLEKADELLEAvglhKSFANRYPHEFSGGQR 157
Cdd:PRK11650 74 AD-----RDIAMVFQN-YA-LYPHMSVRENMAYGLKIRGM--PKaeiEERVAEAARILEL----EPLLDRKPRELSGGQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
....*.
gi 564753507 238 RLYQEP 243
Cdd:PRK11650 221 EVYEKP 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-231 |
3.25e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 17 DAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRG---KNIHNLSDdesfqYNRKIQMI 93
Cdd:PRK13633 16 SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWD-----IRNKAGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 94 FQDPYASLnprltVREIMTE------------PMEIHglyggkkarlEKADELLEAVGLHKsFANRYPHEFSGGQRQRIG 161
Cdd:PRK13633 91 FQNPDNQI-----VATIVEEdvafgpenlgipPEEIR----------ERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 162 IARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMV 231
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-232 |
3.34e-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: 114.63 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 16 FDAGRgktvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsDDESFQynRKIQMIFQ 95
Cdd:cd03253 10 YDPGR----PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLR--RAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 DpyaslnprlTVreIMTEPMEIHGLYGGKKARLEKADELLEAVGLH---KSFANRYPHE-------FSGGQRQRIGIARA 165
Cdd:cd03253 83 D---------TV--LFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHdkiMRFPDGYDTIvgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
3.35e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.72 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQtgalLKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSD 80
Cdd:PRK13651 1 MQ----IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DESFQ-----------YNRKIQMI----------FQDPYASLNPRLTVREIMTEPMEihglYGGKKAR-LEKADELLEAV 138
Cdd:PRK13651 77 TKEKEkvleklviqktRFKKIKKIkeirrrvgvvFQFAEYQLFEQTIEKDIIFGPVS----MGVSKEEaKKRAAKYIELV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 139 GLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMV 215
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNV 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-231 |
8.83e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.59 E-value: 8.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYRGK--NIHNLSDdesfQYNRKIQMIFQDP 97
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKST----LMKilygLYQPDSGEILIDGKpvRIRSPRD----AIALGIGMVHQHF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 yaSLNPRLTVRE-IM--TEPMEiHGLYGGKKARlEKADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPEFIV 174
Cdd:COG3845 90 --MLVPNLTVAEnIVlgLEPTK-GGRLDRKAAR-ARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 175 ADEPISALdvsVQAQVVNL---LKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG3845 165 LDEPTAVL---TPQEADELfeiLRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-237 |
9.93e-30 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 113.62 E-value: 9.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLM--RLYQPTEGEVTYRGKNIHNLSDDE--------SFQYNRKIqmifqdp 97
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDEraragiflAFQYPVEI------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 yaslnPRLTVREIMTEPM-EIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHE-FSGGQRQRIGIARALALEPEFIVA 175
Cdd:COG0396 90 -----PGVSVSNFLRTALnARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 176 DEPISALDV-SVQAqVVNLLKKLqKEKGLTFLFIAHDLSMVKHIS-DRIGVMYLGHMVEITDSS 237
Cdd:COG0396 165 DETDSGLDIdALRI-VAEGVNKL-RSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-242 |
1.77e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIH----NLSDdesfqYNRKIQMIFQDPYAS 100
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSD-----IRKKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVREIMTEPMEIhGLYGGK-KARLEKAdelLEAVGL-HKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:PRK13637 96 LFEETIEKDIAFGPINL-GLSEEEiENRVKRA---MNIVGLdYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 179 ISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
24-242 |
1.99e-29 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 118.26 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDP---YAS 100
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE---LRARMALVPQDPvlfAAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 L--NPRLTVREIMTEPMEIhglyggkKARLEKADELLEAV--GLHKSFANRyPHEFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:TIGR02204 430 VmeNIRYGRPDATDEEVEA-------AARAAHAHEFISALpeGYDTYLGER-GVTLSGGQRQRIAIARAILKDAPILLLD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:TIGR02204 502 EATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-232 |
2.21e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.16 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQ-YNRKIQMIFQDPYASLNP 103
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKkLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEIHglYGGKKARlEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:PRK13641 101 NTVLKDVEFGPKNFG--FSEDEAK-EKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564753507 184 VSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-225 |
3.15e-29 |
|
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: 115.21 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlsddESFQ------YNRKIQMIFQDpyASLNP 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF-----DSRKgiflppEKRRIGYVFQE--ARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMtepmeihgLYGGKKARLEKA----DELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:TIGR02142 89 HLSVRGNL--------RYGMKRARPSERrisfERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-254 |
3.41e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.16 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKST-----SGrvlmrLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpyASLNPR 104
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTllnliAG-----FLPPDSGRILWNGQDLTALPPAE-----RPVSMLFQE--NNLFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVRE-ImtepmeihGLygGKKARL-------EKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:COG3840 86 LTVAQnI--------GL--GLRPGLkltaeqrAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQALLSA 254
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-231 |
5.43e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 15 HFDAGRGKTvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIF 94
Cdd:PRK11231 7 NLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 QDPyasLNPR-LTVREIMTEPMEIH-GLYGgkkaRLEKADELLEAVGLHKS----FANRYPHEFSGGQRQRIGIARALAL 168
Cdd:PRK11231 83 QHH---LTPEgITVRELVAYGRSPWlSLWG----RLSAEDNARVNQAMEQTrinhLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 169 EPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-231 |
7.34e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 110.99 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLkmhfDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQY 86
Cdd:cd03224 1 LEVENL----NAGYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP---PHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRK-IQMIFQDPyaSLNPRLTVRE--IMtepmeihGLYGGKKARLEKA-DELLEAVGLHKSFANRYPHEFSGGQRQRIGI 162
Cdd:cd03224 73 ARAgIGYVPEGR--RIFPELTVEEnlLL-------GAYARRRAKRKARlERVYELFPRLKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 163 ARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-242 |
1.13e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.13 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQ 85
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 -YNRKIQMIFQDPYASLNPRLTVREIMTEPMEihglYGGKKARLEK-ADELLEAVGLHKSFANRYPHEFSGGQRQRIGIA 163
Cdd:PRK13643 81 pVRKKVGVVFQFPESQLFEETVLKDVAFGPQN----FGIPKEKAEKiAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 164 RALALEPEFIVADEPISALDVSVQAQVVNLLKKLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-232 |
1.44e-28 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 110.65 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGkniHNLSDDESFQYNRKIQMIFQ---- 95
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQVGVVLQenvl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 ------DPYASLNPRLTVREIMtepmeihglyggKKARLEKADELLEAVGL-HKSFANRYPHEFSGGQRQRIGIARALAL 168
Cdd:cd03252 88 fnrsirDNIALADPGMSMERVI------------EAAKLAGAHDFISELPEgYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 169 EPEFIVADEPISALDVSVQAQVVNLLKKLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-222 |
2.27e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 110.54 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfqynrkIQMIFQDpyAS 100
Cdd:PRK11247 24 ERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED--------TRLMFQD--AR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVreimtepMEIHGLyGGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK11247 92 LLPWKKV-------IDNVGL-GLKGQWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
6-222 |
2.72e-28 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 109.40 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGR--GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYR--GKNIhNLSDD 81
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQqgGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRheGAWV-DLAQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 82 ESFQ--YNRKIQMIFQDPYASLNPRLTVREIMTEPMEIHGLyGGKKARlEKADELLEAVGLHKSFANRYPHEFSGGQRQR 159
Cdd:TIGR02324 80 SPREvlEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGV-PREAAR-ARARELLARLNIPERLWHLPPATFSGGEQQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:TIGR02324 158 VNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRV 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
27-211 |
3.76e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.72 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQP---TEGEVTYRGKNIHNLSddesfQYNRKIQMIFQDPYasLNP 103
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-----AEQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVRE--IMTEPMEIhglygGKKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:COG4136 90 HLSVGEnlAFALPPTI-----GRAQRRARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190
....*....|....*....|....*....|
gi 564753507 182 LDVSVQAQVVNLLKKLQKEKGLTFLFIAHD 211
Cdd:COG4136 164 LDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-233 |
5.08e-28 |
|
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: 108.77 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 10 SRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGknihnlsddesfqynrK 89
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 90 IQMIFqDPYASLNPRLTVRE--IMtepmeIHGLYGGKKARL-EKADELLEAVGLHKSFANRYPHeFSGGQRQRIGIARAL 166
Cdd:cd03220 85 VSSLL-GLGGGFNPELTGREniYL-----NGRLLGLSRKEIdEKIDEIIEFSELGDFIDLPVKT-YSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEI 233
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-233 |
6.03e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlSDDESFQYNRKIQMIFQDP-------- 97
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQNPdnqfigat 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 -----YASLNPRLTVREIMTEpmeihglyggkkarleKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:PRK13632 101 veddiAFGLENKKVPPKKMKD----------------IIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKhISDRIGVMYLGHMVEI 233
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-225 |
8.40e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 108.63 E-value: 8.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTsgrVLM---RLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDP 97
Cdd:COG4604 13 GKVV--LDDVSLTIPKGGITALIGPNGAGKST---LLSmisRLLPPDSGEVLVDGLDVATTPSRE---LAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 yaSLNPRLTVREIMTepmeiHGLYGGKKARLEKAD-----ELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:COG4604 85 --HINSRLTVRELVA-----FGRFPYSKGRLTAEDreiidEAIAYLDLE-DLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-243 |
8.70e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.27 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpYAsLNPRLTVRE 109
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQS-YA-LYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 110 IMTEPMEihgLYGGKKA----RLEKADELLEAVGLhksfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:PRK11000 95 NMSFGLK---LAGAKKEeinqRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 186 VQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-231 |
9.49e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 108.71 E-value: 9.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTsgrvLMRLY----QPTEGEVTYRGKNIHNLSDDESfqyNRKIQMIFQd 96
Cdd:PRK13548 14 GRTL--LDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelSPDSGEVRLNGRPLADWSPAEL---ARRRAVLPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 97 pYASLNPRLTVREIMTepMEIHGLYGGKKARLEKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALA------LEP 170
Cdd:PRK13548 84 -HSSLSFPFTVEEVVA--MGRAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 171 EFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
1.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.94 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 4 GALLKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEV------------TYR 71
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 72 GKNIHNLSDDESFQYNRK-IQMIFQDPYASLNPRLTVREIMTEPMEIhglyGGKKARL-EKADELLEAVGLHKSFANRYP 149
Cdd:PRK13631 99 LITNPYSKKIKNFKELRRrVSMVFQFPEYQLFKDTIEKDIMFGPVAL----GVKKSEAkKLAKFYLNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 150 HEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKlQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
..
gi 564753507 230 MV 231
Cdd:PRK13631 254 IL 255
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-225 |
2.60e-27 |
|
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: 109.81 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGkniHNLSDDESFQ----YNRKIQMIFQDpyASLNPRL 105
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG---EVLQDSARGIflppHRRRIGYVFQE--ARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMtepmeihgLYGGKKA----RLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:COG4148 93 SVRGNL--------LYGRKRApraeRRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564753507 182 LDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLL 207
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-232 |
2.85e-27 |
|
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: 112.12 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLS-DDESFQYNRKIQ--MIFQD 96
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlASLRRQVALVSQdvVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 97 PYASlNPRLTVREimtepmeihglyGGKKARLEKAdelLEAVGLhKSFANRYPHEF-----------SGGQRQRIGIARA 165
Cdd:TIGR02203 421 TIAN-NIAYGRTE------------QADRAEIERA---LAAAYA-QDFVDKLPLGLdtpigengvllSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-242 |
3.17e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.91 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRK-IQMIFQDPYASLNP 103
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKkVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEihglYGGKKARLEK-ADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISAL 182
Cdd:PRK13649 101 ETVLKDVAFGPQN----FGVSQEEAEAlAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 183 DVSVQAQVVNLLKKLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:PRK13649 177 DPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-249 |
4.51e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.04 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDagrgkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ-----PTEGEVTYRGKNIH----N 77
Cdd:PRK14258 8 IKVNNLSFYYD-----TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYerrvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 78 LSddesfQYNRKIQMIFQDPyaSLNPrLTVREIMTEPMEIHGLYggKKARLE-------KADELLEAVG--LHKSfanry 148
Cdd:PRK14258 83 LN-----RLRRQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWR--PKLEIDdivesalKDADLWDEIKhkIHKS----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 149 PHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMY-- 226
Cdd:PRK14258 148 ALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgn 227
|
250 260
....*....|....*....|....*.
gi 564753507 227 ---LGHMVEITDSSRLYQEPLHPYTQ 249
Cdd:PRK14258 228 enrIGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-231 |
6.17e-27 |
|
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: 105.35 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGRgktvkAVDGISFDIKEGeTFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDdesfQY 86
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDPyaSLNPRLTVREIMTEPMEIHGLYGGK-KARlekADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03264 71 RRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEvKAR---VDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-232 |
6.34e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.21 E-value: 6.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDdESFQYNrkIQMIFQDPYaslnprL 105
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR-ASLRRN--IAVVFQDAG------L 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREImtepmeihglygGKKARLEKAD----ELLEAVGLHKS--FANRYPHEF-----------SGGQRQRIGIARALAL 168
Cdd:PRK13657 421 FNRSI------------EDNIRVGRPDatdeEMRAAAERAQAhdFIERKPDGYdtvvgergrqlSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 169 EPEFIVADEPISALDVSVQAQVVNLLKKLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-231 |
8.19e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 105.34 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDPYASLNPr 104
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 lTVREIMTEPMEIHGLYGGKKARleKADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDV 184
Cdd:PRK10908 95 -TVYDNVAIPLIIAGASGDDIRR--RVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 185 SVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK10908 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-243 |
1.34e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.58 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKnihNLSDDESFQYNRKIQMIFQDPyasLNPRLTVR 108
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYDHHYLHRQVALVGQEP---VLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 EIMTepmeihglYGGKKARLEKADELLEAVGLHkSFANRYPHEF-----------SGGQRQRIGIARALALEPEFIVADE 177
Cdd:TIGR00958 573 ENIA--------YGLTDTPDEEIMAAAKAANAH-DFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 178 PISALDVSVQAqvvnLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:TIGR00958 644 ATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
27-237 |
1.39e-26 |
|
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: 104.15 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRL--YQPTEGEVTYRGKNIHNLSDDESFQynRKIQMIFQdpyaslnpr 104
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERAR--LGIFLAFQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 ltvreimtEPMEIHGLyggkkarleKADELLeavglhksfanRYPHE-FSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:cd03217 85 --------YPPEIPGV---------KNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 184 VSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHI-SDRIGVMYLGHMVEITDSS 237
Cdd:cd03217 137 IDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-212 |
1.72e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.55 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDagrGKtvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESfq 85
Cdd:PRK11248 1 MLQISHLYADYG---GK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 ynrkiqMIFQDpyASLNPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:PRK11248 74 ------VVFQN--EGLLPWRNVQDNVAFGLQLAGV--EKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDL 212
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-244 |
2.30e-26 |
|
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: 104.55 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQynRKIQMIFQDpyASL 101
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR--LGIGYLPQE--ASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:cd03218 87 FRKLTVEENILAVLEIRGL--SKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 182 LD-VSVQaQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPL 244
Cdd:cd03218 164 VDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-232 |
4.05e-26 |
|
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: 102.39 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESfqynRKIQMIFQDPYaslnpr 104
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS----SLISVLNQRPY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 ltvreimtepmeihgLYggkkarlekADELLEAVGLhksfanryphEFSGGQRQRIGIARALALEPEFIVADEPISALDV 184
Cdd:cd03247 86 ---------------LF---------DTTLRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 185 SVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHIsDRIGVMYLGHMVE 232
Cdd:cd03247 132 ITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-232 |
4.23e-26 |
|
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: 108.89 E-value: 4.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsDDESFQynRKIQMIFQdpyaslNPRLTV 107
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL-DVQAVR--RQLGVVLQ------NGRLMS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 REIMTEpmeihgLYGGKKARLEKADELLEAVGLHKSFAnRYP---H--------EFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:TIGR03797 541 GSIFEN------IAGGAPLTLDEAWEAARMAGLAEDIR-AMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFD 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQkekgLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:TIGR03797 614 EATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQ 664
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-231 |
5.45e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 103.57 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 15 HFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGknihNLSDDESFQYNRKIQMIF 94
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 -QDPYASLNprLTVREIMTEPMEIHGL-YGGKKARLEKADELLEAVGLHKSFANRypheFSGGQRQRIGIARALALEPEF 172
Cdd:cd03267 101 gQKTQLWWD--LPVIDSFYLLAAIYDLpPARFKKRLDELSELLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-225 |
8.14e-26 |
|
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: 102.93 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlSDDESFQYNRKIQMIFQDPyaSLNPRlTVR 108
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEP--VLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 EIMTepmeihglYGGKKARLEKADELLEAVGLHkSFANRYPHEF-----------SGGQRQRIGIARALALEPEFIVADE 177
Cdd:cd03248 106 DNIA--------YGLQSCSFECVKEAAQKAHAH-SFISELASGYdtevgekgsqlSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVL 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-269 |
9.88e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 9.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlsdDESFQYNR-KIQMIFQDP----YA 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----AENEKWVRsKVGLVFQDPddqvFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SlnprlTVREIMTEPMEIHGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:PRK13647 95 S-----TVWDDVAFGPVNMGL--DKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPL--------------- 244
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIveqaglrlplvaqif 245
|
250 260
....*....|....*....|....*
gi 564753507 245 HPYTQALLSAIPIpdpDVEDKRKRI 269
Cdd:PRK13647 246 EDLPELGQSKLPL---TVKEAVQII 267
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-228 |
1.70e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlsDDESFQYNRK-IQMIFQDPYASLNPR 104
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI----TDDNFEKLRKhIGIVFQNPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 lTVREIMTEPMEIHGLYGGKKARleKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDV 184
Cdd:PRK13648 100 -IVKYDVAFGLENHAVPYDEMHR--RVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564753507 185 SVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLG 228
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-235 |
1.92e-25 |
|
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: 101.48 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 31 SFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesfQYNRKIQMIFQDpyASLNPRLTVREI 110
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 111 MTepmeiHGLYGGKK---ARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQ 187
Cdd:TIGR01277 91 IG-----LGLHPGLKlnaEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 188 AQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-212 |
2.66e-25 |
|
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: 106.29 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 3 TGALLKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDE 82
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 83 sfqYNRKIQMIFQDP--YASlnprlTVREIMtepmeihgLYGGKKARLEKADELLEAVGLHkSFANRYPH---------- 150
Cdd:TIGR02868 407 ---VRRRVSVCAQDAhlFDT-----TVRENL--------RLARPDATDEELWAALERVGLA-DWLRALPDgldtvlgegg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 151 -EFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLkkLQKEKGLTFLFIAHDL 212
Cdd:TIGR02868 470 aRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-267 |
4.57e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.10 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEG-----EVTYRGKNIHNLSDdeSFQYNRKIQMIFQ 95
Cdd:PRK14271 33 GKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 DPyaslNP-RLTVREIMTEPMEIHGLYGGKKARlEKADELLEAVGLHKSFANRY---PHEFSGGQRQRIGIARALALEPE 171
Cdd:PRK14271 109 RP----NPfPMSIMDNVLAGVRAHKLVPRKEFR-GVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 172 FIVADEPISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLHPYTQAL 251
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARY 261
|
250
....*....|....*.
gi 564753507 252 LSAIpipDPDVEDKRK 267
Cdd:PRK14271 262 VAGL---SGDVKDAKR 274
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-232 |
4.63e-25 |
|
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: 101.06 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGrgktvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlSDDESFQY 86
Cdd:TIGR03410 1 LEVSNLNVYYGQS-----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI---TKLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRK-I------QMIFqdpyaslnPRLTVRE-IMTepmeihGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQ 158
Cdd:TIGR03410 73 ARAgIayvpqgREIF--------PRLTVEEnLLT------GLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 159 RIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE 232
Cdd:TIGR03410 139 QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-245 |
6.11e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 8 KVSRLKMHF---DAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGknihnlsddesf 84
Cdd:COG1134 20 PSRSLKELLlrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 qynrKIQMIFqDPYASLNPRLTVRE----IMTepmeIHGLygGKKARLEKADELLEAVGLHKSF---ANRYphefSGGQR 157
Cdd:COG1134 88 ----RVSALL-ELGAGFHPELTGREniylNGR----LLGL--SRKEIDEKFDEIVEFAELGDFIdqpVKTY----SSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 158 QRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
250
....*....|.
gi 564753507 238 ---RLYQEPLH 245
Cdd:COG1134 232 eviAAYEALLA 242
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-243 |
6.61e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.40 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQYNRKIQMIFQD-PYASlnpRLTVR 108
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS---SKAFARKVAYLPQQlPAAE---GMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 EIMT---EPMeiHGLYG--GKKARlEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:PRK10575 104 ELVAigrYPW--HGALGrfGAADR-EKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 184 VSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-237 |
7.02e-25 |
|
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: 104.88 E-value: 7.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAgrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVL--MRLYQPTEGEVTYR------------- 71
Cdd:TIGR03269 1 IEVKNLTKKFDG-----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 72 ---GKN--------------IHNLSDDESFQYNRKIQMIFQDPYAsLNPRLTVREIMTEPMEIHGlYGGKKArLEKADEL 134
Cdd:TIGR03269 76 skvGEPcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIG-YEGKEA-VGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 135 LEAVGLhksfANRYPH---EFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHD 211
Cdd:TIGR03269 153 IEMVQL----SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*.
gi 564753507 212 LSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPD 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
9.99e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 9.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhNLSDDESFQ 85
Cdd:PRK13636 5 ILKVEELNYNYSDG----THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYASLNPRLTVREIMTEPMEIhGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARA 165
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFGAVNL-KL--PEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-211 |
1.11e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.85 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSD 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 81 DESFQYN-RKIQMIFQDpyASLNPRLTVREIMTEPMEIHGlYGGKKARlEKADELLEAVGLHKSFaNRYPHEFSGGQRQR 159
Cdd:PRK10584 80 EARAKLRaKHVGFVFQS--FMLIPTLNALENVELPALLRG-ESSRQSR-NGAKALLEQLGLGKRL-DHLPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHD 211
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-253 |
1.12e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.63 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ--PT---EGEVTYRGKNIHNlSDDESFQYNRKIQMIFQDPYAS 100
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 lnPRLTVREIMTEPmEIHGLYGGKKARLEKA-------DEL---LEAVGLhksfanryphEFSGGQRQRIGIARALALEP 170
Cdd:PRK14243 104 --PKSIYDNIAYGA-RINGYKGDMDELVERSlrqaalwDEVkdkLKQSGL----------SLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 171 EFIVADEPISALDVSVQAQVVNLLKKLQKEkgLTFLFIAHDLSMVKHISDRI----------GVMYlGHMVEITDSSRLY 240
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTaffnveltegGGRY-GYLVEFDRTEKIF 247
|
250
....*....|...
gi 564753507 241 QEPLHPYTQALLS 253
Cdd:PRK14243 248 NSPQQQATRDYVS 260
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
27-232 |
1.56e-24 |
|
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: 104.44 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhNLSD------------DESFQYNRKIQmif 94
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL-AIADpawlrrqmgvvlQENVLFSRSIR--- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 qDPYASLNPRLTVREImtepmeIHGlyggkkARLEKADElleavglhksFANRYPHEF-----------SGGQRQRIGIA 163
Cdd:TIGR01846 549 -DNIALCNPGAPFEHV------IHA------AKLAGAHD----------FISELPQGYntevgekganlSGGQRQRIAIA 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 164 RALALEPEFIVADEPISALDVSVQAQVVNLLKKLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREIC--RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-231 |
1.86e-24 |
|
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: 99.29 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLkmhfDAGRGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesf 84
Cdd:COG0410 2 PMLEVENL----HAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 qynRKIQM----------IFqdpyaslnPRLTVRE--IMtepmeihGLYGGKKARLEKADelLEAVglhksFAnRYP--H 150
Cdd:COG0410 74 ---RIARLgigyvpegrrIF--------PSLTVEEnlLL-------GAYARRDRAEVRAD--LERV-----YE-LFPrlK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 151 EF--------SGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:COG0410 128 ERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRA 206
|
....*....
gi 564753507 223 GVMYLGHMV 231
Cdd:COG0410 207 YVLERGRIV 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-224 |
1.95e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.47 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYqPT---EGEVTYRGKNIH--NLSDDEsfqynRK-IQMIFQDp 97
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQasNIRDTE-----RAgIAIIHQE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 yASLNPRLTVREIMTEPMEIHglYGGK---KARLEKADELLEAVGLHKSFANRYpHEFSGGQRQRIGIARALALEPEFIV 174
Cdd:PRK13549 91 -LALVKELSVLENIFLGNEIT--PGGImdyDAMYLRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564753507 175 ADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICV 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-203 |
2.57e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.95 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFdagRGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesf 84
Cdd:COG1137 2 MTLEAENLVKSY---GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRKiQM----------IFQdpyaslnpRLTVRE-IMTePMEIHGLygGKKARLEKADELLEAVGLHKsFANRYPHEFS 153
Cdd:COG1137 72 MHKRA-RLgigylpqeasIFR--------KLTVEDnILA-VLELRKL--SKKEREERLEELLEEFGITH-LRKSKAYSLS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564753507 154 GGQRQRIGIARALALEPEFIVADEPISALD-VSVqAQVVNLLKKLqKEKGL 203
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHL-KERGI 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-238 |
2.97e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESfqyNRKIQMIFQDpyASLNP 103
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRVASVPQD--TSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEIH-GLYGGKKARLEKA-DELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:PRK09536 91 EFDVRQVVEMGRTPHrSRFDTWTETDRAAvERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 182 LDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmvEITDSSR 238
Cdd:PRK09536 170 LDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADG---RVRAAGP 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-260 |
3.57e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKST-----SGRVLMRLYQPTEGEVTYRG--KNIHNLSDdesfqYNRKIQMIFQDP 97
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTmiqltNGLIISETGQTIVGDYAIPAnlKKIKEVKR-----LRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 YASLNPRLTVREIMTEPMEihgLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:PRK13645 100 EYQLFQETIEKDIAFGPVN---LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQeplhpyTQALLSAIPI 257
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS------NQELLTKIEI 250
|
...
gi 564753507 258 PDP 260
Cdd:PRK13645 251 DPP 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-225 |
4.94e-24 |
|
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: 102.52 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 19 GRGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYnrkIQmifqdpY 98
Cdd:COG4618 342 GSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH---IG------Y 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASLNPRL---TVRE-ImtepmeihglyggkkARLEKAD--ELLEA---VGLHK---SFANRY-------PHEFSGGQRQR 159
Cdd:COG4618 411 LPQDVELfdgTIAEnI---------------ARFGDADpeKVVAAaklAGVHEmilRLPDGYdtrigegGARLSGGQRQR 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVL 539
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
27-243 |
5.49e-24 |
|
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: 102.71 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQynrKIQMIFQDpyASLNpRLT 106
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN---SVAMVDQD--IFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VREIMT--------EPME-------IHGLYGGKKARLEKadELLEavglhkSFANrypheFSGGQRQRIGIARALALEPE 171
Cdd:TIGR03796 569 VRDNLTlwdptipdADLVrackdaaIHDVITSRPGGYDA--ELAE------GGAN-----LSGGQRQRLEIARALVRNPS 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 172 FIVADEPISALDVSVQAQVVNLLKKlqkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:TIGR03796 636 ILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-253 |
6.53e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 12 LKMHFDagrgktvkavdgisFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQ 91
Cdd:PRK10771 14 LPMRFD--------------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-----RPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 92 MIFQDpyASLNPRLTVREimtepmEIH-GLYGGKK---ARLEKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALA 167
Cdd:PRK10771 75 MLFQE--NNLFSHLTVAQ------NIGlGLNPGLKlnaAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 168 LEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVeitdssrlYQEPlhpy 247
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA--------WDGP---- 213
|
....*.
gi 564753507 248 TQALLS 253
Cdd:PRK10771 214 TDELLS 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-231 |
7.84e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQYNRKI-QMIFQDPYASLNPR 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS---KLQGIRKLvGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 lTVRE--------IMTEPMEIHglyggkkarlEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVAD 176
Cdd:PRK13644 94 -TVEEdlafgpenLCLPPIEIR----------KRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQkEKGLTFLFIAHDLSMVkHISDRIGVMYLGHMV 231
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIV 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-220 |
9.41e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 98.30 E-value: 9.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDpyASLNPRLTV 107
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 REIMTEPMEIHglyggkkARLekADEL--------LEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:PRK11831 102 FDNVAYPLREH-------TQL--PAPLlhstvmmkLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISD 220
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
231-298 |
1.20e-23 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 92.08 E-value: 1.20e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 231 VEITDSSRLYQEPLHPYTQALLSAIPIPDPDvedKRKRIILKGELPSPIDPPSGCVFRTRCPAATDIC 298
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPP---KRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-213 |
1.59e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.75 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 9 VSRLK-MHFDAGRGKTVKAvDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYN 87
Cdd:PRK10253 5 VARLRgEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 88 RKIQMIFQDpyASLNPRLTVREIMTEpmeihGLYGGKK--ARLEKADE-----LLEAVGLhKSFANRYPHEFSGGQRQRI 160
Cdd:PRK10253 81 RRIGLLAQN--ATTPGDITVQELVAR-----GRYPHQPlfTRWRKEDEeavtkAMQATGI-THLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 161 GIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLS 213
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLN 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
27-225 |
1.96e-23 |
|
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: 94.98 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIFQDpyaslnprlt 106
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN---ELGDHVGYLPQD---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 vreimtepmeihglyggkkarlekaDELLEAvglhkSFANRYpheFSGGQRQRIGIARALALEPEFIVADEPISALDVSV 186
Cdd:cd03246 85 -------------------------DELFSG-----SIAENI---LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 564753507 187 QAQVVNLLKKLqKEKGLTFLFIAHDLSMVKhISDRIGVM 225
Cdd:cd03246 132 ERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVL 168
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-225 |
2.58e-23 |
|
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: 100.44 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIFQDPY---ASL 101
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQIAWVPQHPFlfaGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 --NPRLTVREIMTEPMEihglyggKKARLEKADELLEAV--GLHKSFANRyPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:TIGR02857 413 aeNIRLARPDASDAEIR-------EALERAGLDEFVAALpqGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 178 PISALDVSVQAQVVNLLKKLQkeKGLTFLFIAHDLSmVKHISDRIGVM 225
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-232 |
3.26e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 100.58 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYnrkIQMIFQDPYA----- 99
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQEPYIfsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 ------SLNPRLTVREIM--TEPMEIhglyggkKARLEKAdelleAVGLHKSFANRyPHEFSGGQRQRIGIARALALEPE 171
Cdd:TIGR01193 565 lenlllGAKENVSQDEIWaaCEIAEI-------KDDIENM-----PLGYQTELSEE-GSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 172 FIVADEPISALDVSVQAQVVNLLKKLQKEkglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-232 |
3.46e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.09 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGkniHNLSDDESFQYNRKIQMI------F 94
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLRNQVALVsqnvhlF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 QDPYASlNPRLTVREIMTepmeihglyggkKARLEKADELLEAVGlhksFANRYPHEF-----------SGGQRQRIGIA 163
Cdd:PRK11176 430 NDTIAN-NIAYARTEQYS------------REQIEEAARMAYAMD----FINKMDNGLdtvigengvllSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 164 RALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-222 |
4.65e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNlsddESFQYNRKIQMIF----Qdp 97
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK----RRKEFARRIGVVFgqrsQ-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 yasLNPRLTVREImtepMEIHG-LYGGKKARLEKA-DELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVA 175
Cdd:COG4586 107 ---LWWDLPAIDS----FRLLKaIYRIPDAEYKKRlDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRV 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-232 |
7.75e-23 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 94.48 E-value: 7.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeSFQYNRKIQMIFQDPYaslnprL 105
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPV------L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 ---TVREIMtEPMEIHGlyggkKARLEKAdelLEAVGL---HKSFANRYPHE-------FSGGQRQRIGIARALALEPEF 172
Cdd:cd03244 90 fsgTIRSNL-DPFGEYS-----DEELWQA---LERVGLkefVESLPGGLDTVveeggenLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKklQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-231 |
9.33e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 23 TVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI--HNLSDDESFqynrkIQMIFQDPYAS 100
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKF-----VGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRLTVREIMTEPMEIhGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK13652 91 IFSPTVEQDIAFGPINL-GL--DEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-222 |
1.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRKIQMIFQDPYASLnPRL 105
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQF-VGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTEPMEIHGLYGGKKARLekADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKI--VRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 564753507 186 VQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVL 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-231 |
2.35e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.55 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 18 AGRGKT---VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsdDESFQYNRKIQMIF 94
Cdd:PRK09700 9 AGIGKSfgpVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL--DHKLAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 QDpyASLNPRLTVREimtepmeihGLYGGK--------------KARLEKADELLEAVGLHKSFaNRYPHEFSGGQRQRI 160
Cdd:PRK09700 87 QE--LSVIDELTVLE---------NLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 161 GIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-230 |
2.69e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.11 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESfqYNRKIQMIFQDPYAS-LNP 103
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVPEDRKREgLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPmeihglyggkkarlekadELLeavglhksfanryphefSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:cd03215 92 DLSVAENIALS------------------SLL-----------------SGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 184 VSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03215 137 VGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-230 |
2.86e-22 |
|
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: 97.42 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLsDDESFqyNRKIQMIFQDpyASLNPRlT 106
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRETF--GKHIGYLPQD--VELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VRE-I--MTEPMEIHGLYggKKARLEKADELLEavglhkSFANRYPHE-------FSGGQRQRIGIARALALEPEFIVAD 176
Cdd:TIGR01842 408 VAEnIarFGENADPEKII--EAAKLAGVHELIL------RLPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564753507 177 EPISALDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHIsDRIGVMYLGHM 230
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-235 |
3.67e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDAGrgktVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesfq 85
Cdd:COG3845 257 VLEVENLSVRDDRG----VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS------ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQM----IFQDPYAS-LNPRLTVRE--IMT----EPMEIHGLYGGKKARlEKADELLEAvglhksFANRYPHE--- 151
Cdd:COG3845 327 PRERRRLgvayIPEDRLGRgLVPDMSVAEnlILGryrrPPFSRGGFLDRKAIR-AFAEELIEE------FDVRTPGPdtp 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 152 ---FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:COG3845 400 arsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
....*..
gi 564753507 229 HMVEITD 235
Cdd:COG3845 479 RIVGEVP 485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-217 |
4.07e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 97.41 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGrgKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYrgKNIHNLSDDESFQY 86
Cdd:PTZ00265 383 IQFKNVRFHYDTR--KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 87 NRKIQMIFQDP-----------------------------------YASLNPRLTVR-------EIMTEPMEIHGLYGGK 124
Cdd:PTZ00265 459 RSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRakcagdlNDMSNTTDSNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 125 KARLEKADEllEAVGLHKS-----FANRYPHEF-----------SGGQRQRIGIARALALEPEFIVADEPISALDVSVQA 188
Cdd:PTZ00265 539 KNYQTIKDS--EVVDVSKKvlihdFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|....*....
gi 564753507 189 QVVNLLKKLQKEKGLTFLFIAHDLSMVKH 217
Cdd:PTZ00265 617 LVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-231 |
8.54e-22 |
|
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: 91.79 E-value: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 34 IKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqynRKIQMIFQDpyASLNPRLTVREIMte 113
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQE--NNLFAHLTVEQNV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 114 pmeihGLYGGKKARL-----EKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQA 188
Cdd:cd03298 92 -----GLGLSPGLKLtaedrQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564753507 189 QVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-236 |
1.31e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 16 FDaGRGKT---VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFqyNRKIQM 92
Cdd:PRK11288 7 FD-GIGKTfpgVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL--AAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 93 IFQDpyASLNPRLTVREimtepmeihGLYGG----------KKARLEKADELLEAVGLHKSfanryPH----EFSGGQRQ 158
Cdd:PRK11288 84 IYQE--LHLVPEMTVAE---------NLYLGqlphkggivnRRLLNYEAREQLEHLGVDID-----PDtplkYLSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 159 RIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDS 236
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATFDD 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-242 |
1.33e-21 |
|
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: 95.28 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ--PTEGEVTYRGKNI--HNLSDDESfqynRKIQMIFQDpyA 99
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkaSNIRDTER----AGIVIIHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTVRE--IMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:TIGR02633 88 TLVPELSVAEniFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 178 PISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-212 |
1.66e-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: 91.68 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTY-----RGK-NIHNLSddesfqynRKIQMIF 94
Cdd:COG1119 15 GKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerRGGeDVWELR--------KRIGLVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 QDPYASLNPRLTVREIMtepmeIHGLYGG-------KKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALA 167
Cdd:COG1119 85 PALQLRFPRDETVLDVV-----LSGFFDSiglyrepTDEQRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564753507 168 LEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDL 212
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-231 |
2.91e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlsDDESFQYNRKIQMIFQdpYA 99
Cdd:PRK13536 52 GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTVREIMTepmeIHGLYGGKKARLEKA--DELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:PRK13536 124 NLDLEFTVRENLL----VFGRYFGMSTREIEAviPSLLEFARL-ESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-231 |
4.26e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 7 LKVSRLKMHFDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMRL----YQPTEGEVTYRGKNIHNLSDde 82
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAiagsLPPDSGSILIDGKDVTKLPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 83 sFQYNRKIQMIFQDPYASLNPRLTVREIMTepM-----EIHGL-YGGKKARLEKADELLEAVGLhkSFANRYPHE---FS 153
Cdd:COG1101 76 -YKRAKYIGRVFQDPMMGTAPSMTIEENLA--LayrrgKRRGLrRGLTKKRRELFRELLATLGL--GLENRLDTKvglLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 154 GGQRQrigiarALAL------EPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYL 227
Cdd:COG1101 151 GGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
....
gi 564753507 228 GHMV 231
Cdd:COG1101 225 GRII 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-222 |
5.88e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 13 KMHFDAGrgkTVKAVDGISFDIKEGEtFGLV-GESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQ 91
Cdd:PRK10247 12 NVGYLAG---DAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 92 MIFQDPyaSLNPRlTVREIMTEPMEIHGlyggKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPE 171
Cdd:PRK10247 85 YCAQTP--TLFGD-TVYDNLIFPWQIRN----QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564753507 172 FIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-215 |
7.60e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKN-----IHNLSDDESFqynrkiqmifqdpyas 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayvPQRSEVPDSL---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 lnPrLTVREIMTepMeihGLYG--GKKARLEKADEL-----LEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEFI 173
Cdd:NF040873 71 --P-LTVRDLVA--M---GRWArrGLWRRLTRDDRAavddaLERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564753507 174 VADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMV 215
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-231 |
1.22e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 88.87 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKST-----SGRVlmRLYQPTEGEVTYRGKNIHNLSDDESFQYNRkiqmifQ 95
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaiSGRV--EGGGTTSGQILFNGQPRKPDQFQKCVAYVR------Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 DPYasLNPRLTVREIMTEPMEIHGLYGGKKARLEK--ADELLEAVGlHKSFANRYPHEFSGGQRQRIGIARALALEPEFI 173
Cdd:cd03234 89 DDI--LLPGLTVRETLTYTAILRLPRKSSDAIRKKrvEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 174 VADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-231 |
4.11e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 40 FGLvgeSGCGKSTSGRVLMRLYQPTEGEVTYrgkNIHNLSDDESFQY----NRKIQMIFQDpyASLNPRLTVReimtepm 115
Cdd:PRK11144 30 FGR---SGAGKTSLINAISGLTRPQKGRIVL---NGRVLFDAEKGIClppeKRRIGYVFQD--ARLFPHYKVR------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 116 eihG--LYGGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNL 193
Cdd:PRK11144 95 ---GnlRYGMAKSMVAQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 564753507 194 LKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-232 |
4.28e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIFQDPY---ASL 101
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA---ALRQAISVVSQRVHlfsATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLtvreimtepmeihgLYGGKKARLEKADELLEAVGLHKSFANRYP---------HEFSGGQRQRIGIARALALEPEF 172
Cdd:PRK11160 431 RDNL--------------LLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHIsDRIGVMYLGHMVE 232
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-231 |
7.05e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhNLSDDESFQYNRKIQMIFQDP-- 97
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 ---YASLNPRL--TVREIMTEPMEIhglyggkkARleKADELLEAVGlhksfANRYPHE----FSGGQRQRIGIARALAL 168
Cdd:PRK13638 89 qifYTDIDSDIafSLRNLGVPEAEI--------TR--RVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 169 EPEFIVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-232 |
9.00e-20 |
|
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: 90.26 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDeSFQynRKIQMIFQDP---------- 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA-SLR--AAIGIVPQDTvlfndtiayn 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 --YAslNPRLTVREIMtepmeihglyggKKARLEKADELLEA--------VGlhksfanryphE----FSGGQRQRIGIA 163
Cdd:COG5265 452 iaYG--RPDASEEEVE------------AAARAAQIHDFIESlpdgydtrVG-----------ErglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 164 RALALEPEFIVADEPISALDV----SVQAQvvnlLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSrterAIQAA----LREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-213 |
1.88e-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: 84.52 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 17 DAGRGKTVKAV-DGISFDIKEGETFGLVGESGCGKSTSGRVLM--RLYQPTEGEVTYRGKNIHnlsddeSFQYNRKIQMI 93
Cdd:cd03213 14 KSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD------KRSFRKIIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 94 FQDPYasLNPRLTVREIMTEPMEIHGLyggkkarlekadelleavglhksfanryphefSGGQRQRIGIARALALEPEFI 173
Cdd:cd03213 88 PQDDI--LHPTLTVRETLMFAAKLRGL--------------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564753507 174 VADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLS 213
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPS 172
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-222 |
2.54e-19 |
|
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: 85.29 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 32 FDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNihnlsddeSFQYNRKIQMIFQDPYASLNPRLTVRE-I 110
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS--------PGKGWRHIGYVPQRHEFAWDFPISVAHtV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 111 MTEPMEIHGLYG-GKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQ 189
Cdd:TIGR03771 73 MSGRTGHIGWLRrPCVADFAAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190
....*....|....*....|....*....|...
gi 564753507 190 VVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRI 222
Cdd:TIGR03771 152 LTELFIELAGA-GTAILMTTHDLAQAMATCDRV 183
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-233 |
8.91e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 83.23 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHN--LSDdesfqYNRKIQMIFQDPYASLN 102
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipLED-----LRSSLTIIPQDPTLFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 prlTVREimtePMEIHGLYggkkarleKADELLEAVGLHKSFANrypheFSGGQRQRIGIARALALEPEFIVADEPISAL 182
Cdd:cd03369 97 ---TIRS----NLDPFDEY--------SDEEIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 183 DVSVQAqvvnLLKKLQKE--KGLTFLFIAHDLSMVKHIsDRIGVMYLGHMVEI 233
Cdd:cd03369 157 DYATDA----LIQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-235 |
1.41e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.38 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYqPT---EGEVTYRGK--NIHNLSDDESfqynRKIQMIFQDpy 98
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcRFKDIRDSEA----LGIVIIHQE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASLNPRLTVREIMtepmeihgLYGGKKAR---------LEKADELLEAVGLHKSfanryPHEFSG----GQRQRIGIARA 165
Cdd:NF040905 87 LALIPYLSIAENI--------FLGNERAKrgvidwnetNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 166 LALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLD 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-211 |
1.51e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYR-GKNI------HNLSDDES-FQYnrkIQMIFQDPYA 99
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIgylpqePPLDDDLTvLDT---VLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTVREIMTEPMEIHGLYGGKKARLE---------KADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEP 170
Cdd:COG0488 92 LEAELEELEAKLAEPDEDLERLAELQEEFEalggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564753507 171 EFIVADEPISALDvsvqAQVVNLLKK-LQKEKGlTFLFIAHD 211
Cdd:COG0488 172 DLLLLDEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSHD 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-225 |
2.09e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNrkIQMIFQDpyasLN- 102
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG--IGIIHQE----LNl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 -PRLTVREIMTEPMEIHGLYGG---KKARLEkADELLEAVGL-HKSfaNRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:PRK10762 91 iPQLTIAENIFLGREFVNRFGRidwKKMYAE-ADKLLARLNLrFSS--DKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 178 PISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK10762 168 PTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-242 |
2.16e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY-------NRKIQMIFQDp 97
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayvpeDRKGEGLVLD- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 98 yaslnprLTVREIMT----EPMEIHGLYGGKKARlEKADELLEAVGLhksfanRYPH------EFSGGQRQRIGIARALA 167
Cdd:COG1129 345 -------LSIRENITlaslDRLSRGGLLDRRRER-ALAEEYIKRLRI------KTPSpeqpvgNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564753507 168 LEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEE 484
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-194 |
2.61e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY----NrkiqmifqdpyaSLNPR 104
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghrN------------AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVREIMTEPMEIHGlyggkkARLEKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALAL-EPEFIVaDEPISALD 183
Cdd:PRK13539 88 LTVAENLEFWAAFLG------GEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSnRPIWIL-DEPTAALD 159
|
170
....*....|.
gi 564753507 184 VSVQAQVVNLL 194
Cdd:PRK13539 160 AAAVALFAELI 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-210 |
1.38e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTsgrvLMR----LYQPTEGEVTYrgknihnlsddesfqyNRKIQMIF--QDPYAs 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKST----LLRaiagLWPYGSGRIAR----------------PAGARVLFlpQRPYL- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 lnPRLTVREIMTEPMEIHGLyggKKARLEKAdelLEAVGLHKsFANRY------PHEFSGGQRQRIGIARALALEPEFIV 174
Cdd:COG4178 438 --PLGTLREALLYPATAEAF---SDAELREA---LEAVGLGH-LAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*..
gi 564753507 175 ADEPISALDVSVQAQvvnLLKKLQKE-KGLTFLFIAH 210
Cdd:COG4178 509 LDEATSALDEENEAA---LYQLLREElPGTTVISVGH 542
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-212 |
1.64e-17 |
|
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: 79.32 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVkAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDdesfQYNRKIQMIFQDPya 99
Cdd:TIGR01189 10 RGERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD----EPHENILYLGHLP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTVREIMTEPMEIHGlyggkkARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHG------GAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|...
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDL 212
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-225 |
1.75e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFDAgrgKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlsDDESF 84
Cdd:PRK13537 6 APIDFRNVEKRYGD---KLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRKIQMIFQdpYASLNPRLTVReimtEPMEIHGLYGGKKARL--EKADELLEAVGLhKSFANRYPHEFSGGQRQRIGI 162
Cdd:PRK13537 77 HARQRVGVVPQ--FDNLDPDFTVR----ENLLVFGRYFGLSAAAarALVPPLLEFAKL-ENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 163 ARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
2.20e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 80.46 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHFDagrgkTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLM--RLYQPTEGEVTYRGKNIHNL 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVN-----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 79 SDDEsfQYNRKIQMIFQDPY------------ASLNPRLTVREIMT-EPMEIhglyggkkarLEKADELLEAVGLHKSFA 145
Cdd:CHL00131 77 EPEE--RAHLGIFLAFQYPIeipgvsnadflrLAYNSKRKFQGLPElDPLEF----------LEIINEKLKLVGMDPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 146 NRYPHE-FSGGQRQRIGIARALALEPEFIVADEPISALDVS---VQAQVVNLLKKLQKekglTFLFIAHDLSMVKHIS-D 220
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpD 220
|
250 260
....*....|....*....|..
gi 564753507 221 RIGVMYLGHMVEiTDSSRLYQE 242
Cdd:CHL00131 221 YVHVMQNGKIIK-TGDAELAKE 241
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-243 |
6.85e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.30 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPY-- 98
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRLAVVSQTPFlf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 --------ASLNPRLTVREIMtepmeihglyggKKARLEKA-DELLeavglhksfanRYPHEF-----------SGGQRQ 158
Cdd:PRK10789 402 sdtvanniALGRPDATQQEIE------------HVARLASVhDDIL-----------RLPQGYdtevgergvmlSGGQKQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 159 RIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKklQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSR 238
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQ 535
|
....*
gi 564753507 239 LYQEP 243
Cdd:PRK10789 536 LAQQS 540
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-231 |
1.07e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 22 KTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfQYNRKIQMIFQDpyASL 101
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQE--ASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMEI-HGLygGKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK10895 90 FRRLSVYDNLMAVLQIrDDL--SAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 181 ALDvsvQAQVVNLLKKLQ--KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK10895 167 GVD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-231 |
1.85e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNrkIQMIFQDPYasLNP 103
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG--IYLVPQEPL--LFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMtepmeihgLYG--GKKARLEKADELLEAVGLHKSfanryPHEFSG----GQRQRIGIARALALEPEFIVADE 177
Cdd:PRK15439 100 NLSVKENI--------LFGlpKRQASMQKMKQLLAALGCQLD-----LDSSAGslevADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 178 PISALdvsVQAQVVNLLKKLQK--EKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK15439 167 PTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-230 |
1.85e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.13 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTgaLLKVSRLKMHFDAGrgktvKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLY---QPTEGEVTYRGKNIH- 76
Cdd:PRK09984 1 MQT--IIRVEKLAKTFNQH-----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 77 --NLSDDesFQYNR-KIQMIFQDpyASLNPRLTVRE------IMTEPMEIHGLYGGKKARLEKADELLEAVGLhKSFANR 147
Cdd:PRK09984 74 egRLARD--IRKSRaNTGYIFQQ--FNLVNRLSVLEnvligaLGSTPFWRTCFSWFTREQKQRALQALTRVGM-VHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 148 YPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYL 227
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
...
gi 564753507 228 GHM 230
Cdd:PRK09984 229 GHV 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-210 |
2.85e-16 |
|
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: 75.27 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQptegevtYRGKNIHNLSDDESFqynrkiqMIFQDPYAslnPRLT 106
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP-------WGSGRIGMPEGEDLL-------FLPQRPYL---PLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VREIMTepmeihglyggkkarlekadelleavglhksfanrYP--HEFSGGQRQRIGIARALALEPEFIVADEPISALDV 184
Cdd:cd03223 80 LREQLI-----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*.
gi 564753507 185 SVQAQVVNLLkklqKEKGLTFLFIAH 210
Cdd:cd03223 125 ESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-194 |
4.79e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHnlSDDESFQYNrkiqMIFQDPYASLNPRLTV 107
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRDEYHQD----LLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 REIMTEPMEIHGLYGGkkarlEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARaLALEPEFI-VADEPISALDVSV 186
Cdd:PRK13538 92 LENLRFYQRLHGPGDD-----EALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDKQG 164
|
....*...
gi 564753507 187 QAQVVNLL 194
Cdd:PRK13538 165 VARLEALL 172
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-225 |
5.13e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 75.58 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 16 FDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTsgrVLMRL---YQPTEGEVTYRGKnihnLSddesfqynrkiqm 92
Cdd:cd03250 10 WDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS----IA------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 93 ifqdpYASLNPRL---TVRE--IMTEPMEihglyggkKARLEKAdelLEAVGLHKSFANrYPH-------E----FSGGQ 156
Cdd:cd03250 70 -----YVSQEPWIqngTIREniLFGKPFD--------EERYEKV---IKACALEPDLEI-LPDgdlteigEkginLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 157 RQRIGIARALALEPEFIVADEPISALDVSVQAQVVN--LLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVL 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-224 |
7.06e-16 |
|
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: 75.91 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 33 DIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVtyrgknihnLSDDESFQYnrKIQMIFQDpYASlnprlTVREIMT 112
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---------EIELDTVSY--KPQYIKAD-YEG-----TVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 113 EPMEIHGLYGGKKArlekadELLEAVGLHKSFANRYPhEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVN 192
Cdd:cd03237 84 SITKDFYTHPYFKT------EIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|..
gi 564753507 193 LLKKLQKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-249 |
1.78e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.24 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 16 FDAGRGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGK-NIHNLSddesfqynrkiqmif 94
Cdd:PRK13545 29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAIS--------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 qdpyASLNPRLTvreiMTEPMEIHGLYGG--KKARLEKADELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:PRK13545 94 ----SGLNGQLT----GIENIELKGLMMGltKEKIKEIIPEIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 173 IVADEpisALDVSVQAQVVNLLKKLQ--KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVE---ITDSSRLYQEPLHPY 247
Cdd:PRK13545 165 LVIDE---ALSVGDQTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEygdIKEVVDHYDEFLKKY 241
|
..
gi 564753507 248 TQ 249
Cdd:PRK13545 242 NQ 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-224 |
2.45e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.75 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 33 DIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVtyrgknihnlSDDESFQYnrKIQmifqdpYASLNPRLTVREImt 112
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKISY--KPQ------YISPDYDGTVEEF-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 113 epmeihgLYGGKKARLEKA---DELLEAVGLHKSFaNRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQ 189
Cdd:COG1245 422 -------LRSANTDDFGSSyykTEIIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190
....*....|....*....|....*....|....*
gi 564753507 190 VVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-230 |
2.61e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNrkIQMIFQDPYAS-LNPRL 105
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANG--IVYISEDRKRDgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTEPMEIHGLYGGkkARLEKADELLEAVGLHKSFANRYPH------EFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:PRK10762 346 SVKENMSLTALRYFSRAG--GSLKHADEQQAVSDFIRLFNIKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
30-222 |
3.80e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKnihnlsddesfqynRKIQMIFQDPYASLNPRLTVRE 109
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------------LRIGYVPQKLYLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 110 IMT-EPmeihglyGGKKARLEKADELLEAVGLHKsfanrYP-HEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQ 187
Cdd:PRK09544 89 FLRlRP-------GTKKEDILPALKRVQAGHLID-----APmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190
....*....|....*....|....*....|....*
gi 564753507 188 AQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-230 |
4.70e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSD----DESFQY---NRKIQMIFQDpyASLn 102
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpeDRQSSGLYLD--APL- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 pRLTVREIMTEPMEIHGLYGGKKARLEKadeLLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISAL 182
Cdd:PRK15439 359 -AWNVCALTHNRRGFWIKPARENAVLER---YRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 183 DVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-210 |
4.85e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 8 KVSRLKMHFDAG-RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLY--QPTEGEVtyrgknihNLSDDEsf 84
Cdd:COG2401 26 RVAIVLEAFGVElRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV--------DVPDNQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 qynrkiqmifqdpyasLNPRLTVREIMtepmeihGLYGGKKArlekADELLEAVGLHKSFA-NRYPHEFSGGQRQRIGIA 163
Cdd:COG2401 96 ----------------FGREASLIDAI-------GRKGDFKD----AVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564753507 164 RALALEPEFIVADEPISALDVSVqAQVVNL-LKKLQKEKGLTFLFIAH 210
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-224 |
5.10e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 34 IKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVT------YRGKNIHNLSDDESFQYNRKIQMIFQDPYasLNPrltv 107
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisYKPQYIKPDYDGTVEDLLRSITDDLGSSY--YKS---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 rEIMtEPMEIHGLYggkkarlekadelleavglhksfaNRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQ 187
Cdd:PRK13409 436 -EII-KPLQLERLL------------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 564753507 188 AQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-226 |
1.12e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 34 IKEGETFGLVGESGCGKSTSGRVLMRLYQP----TEGEVT-------YRGKNIHNLsddesFQ--YNRKIQMIFQDPYAS 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSwdevlkrFRGTELQNY-----FKklYNGEIKVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRL---TVREIMTEPMEiHGlyggkkarleKADELLEAVGLHKSFaNRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:PRK13409 171 LIPKVfkgKVRELLKKVDE-RG----------KLDEVVERLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564753507 178 PISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-226 |
1.36e-14 |
|
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: 72.40 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 35 KEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVT-----------YRGKNIHNLSDDesfQYNRKIQMIFQDPYASLNP 103
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTK---LLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RL---TVREIMTepmeihglyggKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:cd03236 101 KAvkgKVGELLK-----------KKDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564753507 181 ALDVSVQAQVVNLLKKLQKEKGlTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-220 |
1.48e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY---NRKIQMIFqdpyasln 102
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpqSEEVDWSF-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 prltvrEIMTEPMEIHGLYG-------GKKARLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVA 175
Cdd:PRK15056 94 ------PVLVEDVVMMGRYGhmgwlrrAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISD 220
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-242 |
2.41e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 5 ALLKVSRLKMHFdagrGKtVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlSDDESF 84
Cdd:PRK11614 4 VMLSFDKVSAHY----GK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 85 QYNRKIQMIFQDpyaslNPRLTVREIMTEPMEIHGLYGGKK---ARLEKADELLEAvgLHKSFANRyPHEFSGGQRQRIG 161
Cdd:PRK11614 76 KIMREAVAIVPE-----GRRVFSRMTVEENLAMGGFFAERDqfqERIKWVYELFPR--LHERRIQR-AGTMSGGEQQMLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 162 IARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV-EITDSSRLY 240
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVlEDTGDALLA 226
|
..
gi 564753507 241 QE 242
Cdd:PRK11614 227 NE 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-243 |
3.26e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTsgrvLMRL---YQPTEGEVTYRGKNIHNLSDDesfQYNRKIQMIFQdpyaslNPRL- 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTS----LLNAllgFLPYQGSLKINGIELRELDPE---SWRKHLSWVGQ------NPQLp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 --TVREIMtepmeihgLYGGKKARLEKADELLEAVGLHkSFANRYPH-----------EFSGGQRQRIGIARALALEPEF 172
Cdd:PRK11174 436 hgTLRDNV--------LLGNPDASDEQLQQALENAWVS-EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHIsDRIGVMYLGHMVEITDSSRLYQEP 243
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-222 |
4.22e-14 |
|
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: 70.21 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDdesfQYNRKIQMIFQDPyaSLNPRLTVR 108
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD----SIARGLLYLGHAP--GIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 EIMTEPMEIHGlyggkkarLEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQA 188
Cdd:cd03231 92 ENLRFWHADHS--------DEQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....
gi 564753507 189 QVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-183 |
7.49e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI--HNLSD-------DESFqynrkiqmifqd 96
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATrrrvgymSQAF------------ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 97 pyaSLNPRLTVReimtEPMEIHG-LYGGKKARLEKA-DELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIV 174
Cdd:NF033858 349 ---SLYGELTVR----QNLELHArLFHLPAAEIAARvAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
....*....
gi 564753507 175 ADEPISALD 183
Cdd:NF033858 421 LDEPTSGVD 429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-226 |
1.21e-13 |
|
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: 71.74 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 35 KEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVT-----------YRGKNIHNLsddesFQ--YNRKIQMIFQDPYASL 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQDY-----FKklANGEIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRL---TVREImtepmeihglyggkkarLEKADE------LLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:COG1245 172 IPKVfkgTVREL-----------------LEKVDErgkldeLAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564753507 173 IVADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-241 |
1.24e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.43 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLM--RLYQPTEGEVTYRGKNIHNLSDDE--------SFQYNRKI-----QMI 93
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDragegifmAFQYPVEIpgvsnQFF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 94 FQdpyASLNPRLTVREimTEPMEihglyggkkaRLEKADELLEAVGLHKSFANRYPHE----FSGGQRQRIGIARALALE 169
Cdd:PRK09580 99 LQ---TALNAVRSYRG--QEPLD----------RFDFQDLMEEKIALLKMPEDLLTRSvnvgFSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 170 PEFIVADEPISALDVSVQAQVVNLLKKLQKEKgLTFLFIAHDLSMVKHIS-DRIGVMYLGHMVEITDSSRLYQ 241
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDFTLVKQ 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
1.37e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 6 LLKVSRLKMHFDagrGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTyRGKNIHnlsddesFQ 85
Cdd:COG0488 315 VLELEGLSKSYG---DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVK-------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YnrkiqmiF-QDpYASLNPRLTVREIMTEpmeihglyGGKKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIAR 164
Cdd:COG0488 382 Y-------FdQH-QEELDPDKTVLDELRD--------GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 165 ALALEPEFIVADEPISALDV-SVQAqvvnLLKKLQKEKGlTFLFIAHDLSMVKHISDRI 222
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRI 499
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
28-222 |
2.30e-13 |
|
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: 66.32 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 28 DGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTyRGKNIhnlsddesfqynrKIQmifqdpyaslnprltv 107
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTV-------------KIG---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 108 reimtepmeihglyggkkarlekadelleavglhksfanrYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQ 187
Cdd:cd03221 67 ----------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190
....*....|....*....|....*....|....*
gi 564753507 188 AQVVNLLKKLQKekglTFLFIAHDLSMVKHISDRI 222
Cdd:cd03221 107 EALEEALKEYPG----TVILVSHDRYFLDQVATKI 137
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-231 |
2.68e-13 |
|
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: 67.67 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 1 MQTGALLKVSRLKMHfdaGRGKTvKAVDGISFDIKEGETFGLVGESGCGKSTsgrvLMRL-------YQPTEGEVTYRGK 73
Cdd:cd03233 1 ASTLSWRNISFTTGK---GRSKI-PILKDFSGVVKPGEMVLVLGRPGSGCST----LLKAlanrtegNVSVEGDIHYNGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 74 NihnlSDDESFQYNRKIQMIFQDPyaSLNPRLTVREimtepmeihglyggkkarlekadeLLEAVGLHKsfANRYPHEFS 153
Cdd:cd03233 73 P----YKEFAEKYPGEIIYVSEED--VHFPTLTVRE------------------------TLDFALRCK--GNEFVRGIS 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 154 GGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLS-MVKHISDRIGVMYLGHMV 231
Cdd:cd03233 121 GGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-225 |
3.67e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNRkiqmiFQDPYAS 100
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNR-----YSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 101 LNPRL---TVREIMTepmeihglyGGKKARLEKADELLEAVGLHKSFaNRYPH-----------EFSGGQRQRIGIARAL 166
Cdd:cd03290 86 QKPWLlnaTVEENIT---------FGSPFNKQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVN--LLKKLQKEKgLTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAM 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-217 |
4.17e-13 |
|
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: 70.16 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLM--------RLYQPTEGEVTYrgknihnlsddesfqynrkiqmIFQDPY 98
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----------------------VPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASLNprlTVREIMTEPMEIHGLyggKKARLEKAD--ELLEAVGLHK--------SFANRYPHEFSGGQRQRIGIARALAL 168
Cdd:TIGR00954 526 MTLG---TLRDQIIYPDSSEDM---KRRGLSDKDleQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564753507 169 EPEFIVADEPISALDVSVQAQVVNLLkklqKEKGLTFLFIAHDLSMVKH 217
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-228 |
9.55e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI-HNLSDDESfqynrkiQMIFQDPYA 99
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQ-------NMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTVREIMTEPMEIHGLYGGKKARLekADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:TIGR01257 2022 AIDDLLTGREHLYLYARLRGVPAEEIEKV--ANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564753507 180 SALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-230 |
1.26e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.89 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSD--DESFQYNRKIQMIFQdpyaslnp 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDavRQSLGMCPQHNILFH-------- 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVREIMTEPMEIHGlYGGKKARLEkADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKG-RSWEEAQLE-MEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564753507 184 VSVQAQVVNLLkkLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:TIGR01257 1094 PYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-237 |
1.27e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY-------NRKIQMI 93
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayiteSRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 94 FqdpyaslnPRLTVREIMTEPMEIH-GLYGG------KKARLEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARAL 166
Cdd:PRK09700 353 F--------PNFSIAQNMAISRSLKdGGYKGamglfhEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 167 ALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSS 237
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-231 |
1.69e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQYNrkIQMIFQDpyasLNP 103
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENG--ISMVHQE----LNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTvREIMTE------PMEIHGLYGGKKARLEKA--DELLEAVGLHKSFANrypheFSGGQRQRIGIARALALEPEFIVA 175
Cdd:PRK10982 85 VLQ-RSVMDNmwlgryPTKGMFVDQDKMYRDTKAifDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-233 |
7.30e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHN--LSDdesfqyNRKIQMIFqdPYASLNPRLT 106
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMD------LRKVLGII--PQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VReIMTEPMEIHglyggkkarlEKAD--ELLEAVGLhKSFANRYP-----------HEFSGGQRQRIGIARALALEPEFI 173
Cdd:PLN03130 1329 VR-FNLDPFNEH----------NDADlwESLERAHL-KDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 174 VADEPISALDVSVQAqvvnLLKKLQKE--KGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEI 233
Cdd:PLN03130 1397 VLDEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-224 |
8.19e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLY-----------QPTEGEVT----YRGKNIHNL---------------S 79
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkNEHTNDMTneqdYQGDEEQNVgmknvnefsltkeggS 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 80 DDESFQYNRKIQMIFQD----PYASLNPRLTVREIMTEPMEIH-GLY-----GGKKARLEKA---------DELLEAV-G 139
Cdd:PTZ00265 1267 GEDSTVFKNSGKILLDGvdicDYNLKDLRNLFSIVSQEPMLFNmSIYenikfGKEDATREDVkrackfaaiDEFIESLpN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 140 LHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiS 219
Cdd:PTZ00265 1347 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
....*
gi 564753507 220 DRIGV 224
Cdd:PTZ00265 1426 DKIVV 1430
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-232 |
1.44e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.12 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDdesfQYNRK-IQMIFQDPY---ASLNPRL 105
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH----SVLRQgVAMVQQDPVvlaDTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVreimtepmeihglygGKKARLEKADELLEAVGLhKSFANRYP-----------HEFSGGQRQRIGIARALALEPEFIV 174
Cdd:PRK10790 436 TL---------------GRDISEEQVWQALETVQL-AELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 175 ADEPISALDVSVQAQVVNLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-210 |
1.53e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMrLYQPT----EGEVTYRGKNIhnlsddESFQYNRKIQMIFQDpyaSLN-P 103
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI------DAKEMRAISAYVQQD---DLFiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 104 RLTVRE-IMTEPMEIHGLYGGKKARLEKADELLEAVGLHKSFANRYPHE-----FSGGQRQRIGIARALALEPEFIVADE 177
Cdd:TIGR00955 113 TLTVREhLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|...
gi 564753507 178 PISALDVSVQAQVVNLLKKLqKEKGLTFLFIAH 210
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-230 |
2.77e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPT-EGEVTYRGKNIHNLSDDESFQY-------NRKIQMIFQ 95
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgiamvpeDRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 DPYASLNPRLTVREIMTEPMEIHglyggKKARLEKADELLEAVGLhKSFANRYP-HEFSGGQRQRIGIARALALEPEFIV 174
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRID-----AAAELQIIGSAIQRLKV-KTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 175 ADEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-216 |
5.34e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlsDDESFQYNRkiQMIFQDPYASLNPRLTVRE 109
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK--QLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 110 -------IMTEPMEIHGLyggkkARLEKADELLE-AVGLhksfanrypheFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:PRK13540 94 nclydihFSPGAVGITEL-----CRLFSLEHLIDyPCGL-----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 564753507 182 LDvsvQAQVVNLLKKLQ--KEKGLTFLFIAH-DLSMVK 216
Cdd:PRK13540 158 LD---ELSLLTIITKIQehRAKGGAVLLTSHqDLPLNK 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-272 |
7.30e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 31 SFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddesFQynrKIQMIFQDPYASLNPRL----- 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS----FE---QLQKLVSDEWQRNNTDMlspge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 -----TVREIMTEpmEIHglyggKKARLEkadELLEAVGLHKSFANRYPHeFSGGQRQRIGIARALALEPEFIVADEPIS 180
Cdd:PRK10938 96 ddtgrTTAEIIQD--EVK-----DPARCE---QLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 181 ALDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQEPLhpYTQAL----LSAIP 256
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAL--VAQLAhseqLEGVQ 241
|
250 260
....*....|....*....|...
gi 564753507 257 IPDPDVEDKRK-------RIILK 272
Cdd:PRK10938 242 LPEPDEPSARHalpanepRIVLN 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-232 |
7.43e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI--HNLSDdesfqYNRKIQMIFQDPYASLNprlT 106
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakFGLTD-----LRRVLSIIPQSPVLFSG---T 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 VReIMTEPMEIHGLYGGKKArLEKADelLEAVGLHKSFA-----NRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:PLN03232 1326 VR-FNIDPFSEHNDADLWEA-LERAH--IKDVIDRNPFGldaevSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 182 LDVSVQAqvvnLLKKLQKE--KGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVE 232
Cdd:PLN03232 1402 VDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-238 |
1.34e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 26 AVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYasLNPRL 105
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED---YRKLFSAVFTDFH--LFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREimtepmeihglygGKKARLEKADELLEAVGL-HK------SFANRyphEFSGGQRQRIGIARALALEPEFIVADEP 178
Cdd:PRK10522 413 LGPE-------------GKPANPALVEKWLERLKMaHKleledgRISNL---KLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 179 ISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEITDSSR 238
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELTGEER 535
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-225 |
2.39e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 23 TVKAVDG------ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY-------NRK 89
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpeDRK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 90 IQMIFqdPYASlnprltVREIMTEPMEIHGLYGG----KKARLEKADELLeavglhKSFANRYPH------EFSGGQRQR 159
Cdd:PRK11288 339 AEGII--PVHS------VADNINISARRHHLRAGclinNRWEAENADRFI------RSLNIKTPSreqlimNLSGGNQQK 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 160 IGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-235 |
2.47e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.21 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGknihnlsddesfqynrKIQMIFQDpyA 99
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTvreiMTEPMEIHGLYGGKKARLEKA--DELLEAVGLHKsFANRYPHEFSGGQRQRIGIARALALEPEFIVADE 177
Cdd:PRK13546 95 GLSGQLT----GIENIEFKMLCMGFKRKEIKAmtPKIIEFSELGE-FIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 178 pisALDVSVQAQVVNLLKKLQ--KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMVEITD 235
Cdd:PRK13546 170 ---ALSVGDQTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-231 |
3.04e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.85 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTsgrVLMRL--YQPTEGEVTYRGKNihnLSDDESFQYNRKIQMIFQDPYASLNpr 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRP---LSDWSAAELARHRAYLSQQQSPPFA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 105 LTVREIMTepmeihgLYGGKKARLEKAD----ELLEAVGLhKSFANRYPHEFSGGQRQRIGIARAL-----ALEPE--FI 173
Cdd:COG4138 84 MPVFQYLA-------LHQPAGASSEAVEqllaQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 174 VADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-239 |
4.41e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIhnlsDDESFQ-YNRKIQMIFQDPYasLNPRltvr 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV----TADNREaYRQLFSAVFSDFH--LFDR---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 eimtepmeihgLYGGKKARL-EKADELLEAVGL-HK------SFANRyphEFSGGQRQRigiaraLALepefIVA---DE 177
Cdd:COG4615 421 -----------LLGLDGEADpARARELLERLELdHKvsvedgRFSTT---DLSQGQRKR------LAL----LVAlleDR 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 178 PISALD----------------VsvqaqvvnLLKKLqKEKGLTFLFIAHDlsmvkHISDRIGVMYLGHMVEITDSSRL 239
Cdd:COG4615 477 PILVFDewaadqdpefrrvfytE--------LLPEL-KARGKTVIAISHDdr-yfDLADRVLKMDYGKLVELTGPAAL 544
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-231 |
6.31e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 15 HFD-AGRGKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLM-RLYQPTE-------GEVTYRGKNIHNLsddESFQ 85
Cdd:PRK13547 6 HLHvARRHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAI---DAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 86 YNRKIQMIFQDPYASLNprLTVREIMTEPMEIHGLYGGKKARLEK--ADELLEAVGLhKSFANRYPHEFSGGQRQRIGIA 163
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA--FSAREIVLLGRYPHARRAGALTHRDGeiAWQALALAGA-TALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 164 RALA---------LEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-226 |
1.12e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.81 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 33 DIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGknihnlsddesfqynrkIQMIFQDPYASLnprltvreimt 112
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----------------ITPVYKPQYIDL----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 113 epmeihglyggkkarlekadelleavglhksfanryphefSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVN 192
Cdd:cd03222 73 ----------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
170 180 190
....*....|....*....|....*....|....
gi 564753507 193 LLKKLQKEKGLTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:cd03222 113 AIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-242 |
1.25e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNI-----HNLsddesfqyNRKIQMIFQDPY------ 98
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIakiglHDL--------RFKITIIPQDPVlfsgsl 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 -ASLNP--RLTVREIMTEpMEIHGLYGGKKARLEKADELLEAVGlhksfanrypHEFSGGQRQRIGIARALALEPEFIVA 175
Cdd:TIGR00957 1377 rMNLDPfsQYSDEEVWWA-LELAHLKTFVSALPDKLDHECAEGG----------ENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 176 DEPISALDVSVQaqvvNLLKKLQKEK--GLTFLFIAHDLSMVKHISdRIGVMYLGHMVEITDSSRLYQE 242
Cdd:TIGR00957 1446 DEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-213 |
1.71e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKST-----SGRVLMRLYQpteGEVTYRGKNIhnlsddeSFQYNRKIQMIFQDPYasL 101
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTllnalAGRIQGNNFT---GTILANNRKP-------TKQILKRTGFVTQDDI--L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVRE------IMTEPMEIhglygGKKARLEKADELLEAVGLHKS----FANRYPHEFSGGQRQRIGIARALALEPE 171
Cdd:PLN03211 152 YPHLTVREtlvfcsLLRLPKSL-----TKQEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564753507 172 FIVADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLS 213
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPS 267
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-244 |
1.75e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 27 VDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKN--------IHNLSDDESFQYNRKIQmifqDPY 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVayvpqqawIQNDSLRENILFGKALN----EKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 AslnpRLTVREIMTEP-MEIhgLYGGKKARL-EKADELleavglhksfanryphefSGGQRQRIGIARALALEPEFIVAD 176
Cdd:TIGR00957 730 Y----QQVLEACALLPdLEI--LPSGDRTEIgEKGVNL------------------SGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 177 EPISALDVSVQAQVV-NLLKKLQKEKGLTFLFIAHDLSMVKHIsDRIGVMYLGHMVEITDssrlYQEPL 244
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS----YQELL 849
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-233 |
2.24e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 29 GISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDEsfqYNRKIQMIFQDPYaslnprL--- 105
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFSMIPQDPV------Lfdg 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTEPMEihglyggkkARLEKADELLEAVGLHKSFANRYP----------HEFSGGQRQRIGIARALALEPE-FIV 174
Cdd:PTZ00243 1399 TVRQNVDPFLE---------ASSAEVWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLKKGSgFIL 1469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564753507 175 ADEPIS----ALDVSVQAQVVNLLkklqkeKGLTFLFIAHDLSMVKHIsDRIGVMYLGHMVEI 233
Cdd:PTZ00243 1470 MDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEM 1525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-222 |
2.41e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 32 FDIKEGETFGLVGESGCGKSTSGRVLmrlyqptEGEVtyrgknihnLSDDESFQYNR--KIQMIFQDPyaslnPRL---T 106
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEV---------LLDDGRIIYEQdlIVARLQQDP-----PRNvegT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 107 V----------------------REIMTEPMEIHglyggkKARLEKADELLEAVGLHKsFANRY----------PH---- 150
Cdd:PRK11147 83 VydfvaegieeqaeylkryhdisHLVETDPSEKN------LNELAKLQEQLDHHNLWQ-LENRInevlaqlgldPDaals 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564753507 151 EFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKekglTFLFIAHDLSMVKHISDRI 222
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-211 |
2.88e-09 |
|
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: 58.02 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTV----KAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTyrgknihnlsddesFQYNRKIQMIFQD 96
Cdd:TIGR03719 11 SKVVppkkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------------PQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 97 PYasLNPRLTVREIMTEPM-----------EIHGLYG----------GKKARLEkadELLEAVGLHK--------SFANR 147
Cdd:TIGR03719 77 PQ--LDPTKTVRENVEEGVaeikdaldrfnEISAKYAepdadfdklaAEQAELQ---EIIDAADAWDldsqleiaMDALR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564753507 148 YP------HEFSGGQRQRIGIARALALEPEFIVADEPISALDvsvqAQVVNLLKK-LQKEKGlTFLFIAHD 211
Cdd:TIGR03719 152 CPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPG-TVVAVTHD 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-178 |
4.68e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkAVDGISFDIKEGETFGLVGESGCGKST-----SG-RVLmrlyQptEGEVTYRGKNIHNLSDDESFQynRKIQMIF 94
Cdd:NF033858 12 GKTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSllsliAGaRKI----Q--QGRVEVLGGDMADARHRRAVC--PRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 QDPYASLNPRLTVREimtePMEIHG-LYG-GKKARLEKADELLEAVGLHkSFANRYPHEFSGGQRQRIGIARALALEPEF 172
Cdd:NF033858 83 QGLGKNLYPTLSVFE----NLDFFGrLFGqDAAERRRRIDELLRATGLA-PFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
....*.
gi 564753507 173 IVADEP 178
Cdd:NF033858 158 LILDEP 163
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
24-231 |
5.83e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKStSGRVLMRLYQPTEGEVTYRGKN--IHNLSDDESFQYNRKIQMIFQDPYASl 101
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**-RGALPAHV*GPDAGRRPWRF*TwcANRRALRRTIG*HRPVR*GRRESFSG- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 nprltvREIMTepMEIHGLYGGKKARLEKADELLEAVGLHKSfANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISA 181
Cdd:NF000106 104 ------RENLY--MIGR*LDLSRKDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564753507 182 LDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMV 231
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-222 |
1.22e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTsgrVLMRL--YQPTEGEVTYRGKNIHNLSDDE--------SFQYNRKIQM-IFQdpY 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAElarhraylSQQQTPPFAMpVFQ--Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 99 ASLnprltvreimtepmeiHGLYGGKKARLEKA-DELLEAVGLhKSFANRYPHEFSGGQRQRIGIA-------RALALEP 170
Cdd:PRK03695 90 LTL----------------HQPDKTRTEAVASAlNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564753507 171 EFIVADEPISALDVSVQAQVVNLLKKLQkEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRV 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-242 |
1.61e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSDDESFQY-------NRKIQMIFQDPYASLN 102
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgfalvteERRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 103 PRLT-VREIMTEpmeiHGLYGGKKArleKADE--LLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPI 179
Cdd:PRK10982 347 SLISnIRNYKNK----VGLLDNSRM---KSDTqwVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564753507 180 SALDVSVQAQVVNLLKKL-QKEKGLtfLFIAHDLSMVKHISDRIGVMYLGHMVEITDSSRLYQE 242
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQN 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-197 |
3.85e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.63 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVKAVDGISFDIKEGETFGLVGESGCGKST-----SGRVLMRLyqpTEGEVTYRGKNIhnlsdDESFQynRKIQMIFQ 95
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGV---ITGEILINGRPL-----DKNFQ--RSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 DPyaSLNPRLTVREimtePMEIHGLYGGkkarlekadelleavglhksfanrypheFSGGQRQRIGIARALALEPEFIVA 175
Cdd:cd03232 87 QD--VHSPNLTVRE----ALRFSALLRG----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180
....*....|....*....|..
gi 564753507 176 DEPISALDVSVQAQVVNLLKKL 197
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-228 |
9.57e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQ-PTEGEVTYRGKNIHNLSDDESFQYNrkIQMIFQDPYA-SL 101
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQG--IAMVPEDRKRdGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMTEPMeIHGLYGGKkaRLEKADELLEAVGLHKSFANRYPHEF------SGGQRQRIGIARALALEPEFIVA 175
Cdd:PRK13549 353 VPVMGVGKNITLAA-LDRFTGGS--RIDDAAELKTILESIQRLKVKTASPElaiarlSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564753507 176 DEPISALDVSVQAQVVNLLKKLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-197 |
3.30e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 25 KAVDGIsfdIKEGETFGLVGESGCGKST-----SGRVLMRLYqpTEGEVTYRGKNIhnlsdDESFQynRKIQMIFQDPYA 99
Cdd:TIGR00956 780 NNVDGW---VKPGTLTALMGASGAGKTTllnvlAERVTTGVI--TGGDRLVNGRPL-----DSSFQ--RSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SlnPRLTVRE------IMTEPMEIhglygGKKARLEKADELLEAVGLhKSFANRYPHEFSGG----QRQRIGIARALALE 169
Cdd:TIGR00956 848 L--PTSTVREslrfsaYLRQPKSV-----SKSEKMEYVEEVIKLLEM-ESYADAVVGVPGEGlnveQRKRLTIGVELVAK 919
|
170 180
....*....|....*....|....*....
gi 564753507 170 PEFIV-ADEPISALDVSVQAQVVNLLKKL 197
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-222 |
7.53e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 20 RGKTVkAVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGknihNLS-----------DDESFQYnr 88
Cdd:PRK10636 11 RGVRV-LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQlawvnqetpalPQPALEY-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 89 kiqMIFQD-PYASLNPRLTVREIMTEPMEIHGLYGGKKAR-----LEKADELLEAVGLHKSFANRYPHEFSGGQRQRIGI 162
Cdd:PRK10636 84 ---VIDGDrEYRQLEAQLHDANERNDGHAIATIHGKLDAIdawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 163 ARALALEPEFIVADEPISALDVSVqaqVVNLLKKLQKEKGlTFLFIAHDLSMVKHISDRI 222
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-248 |
8.31e-07 |
|
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: 49.52 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 4 GALLKVSRLKMHFDAGRGKTVKAVDGIsfdIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNLSddeS 83
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 84 FQYNRKIQMIFQDPYA-------SLNPRLTVRE-IMTEPMEIHGLYGGKKARLEKADELLEAVGlhksfanrypHEFSGG 155
Cdd:cd03288 91 HTLRSRLSIILQDPILfsgsirfNLDPECKCTDdRLWEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 156 QRQRIGIARALALEPEFIVADEPISALDVSVQaqvvNLLKK--LQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMVEI 233
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVEC 235
|
250
....*....|....*
gi 564753507 234 TDSSRLYQEPLHPYT 248
Cdd:cd03288 236 DTPENLLAQEDGVFA 250
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-222 |
1.04e-06 |
|
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: 47.75 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 37 GETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYrgknihnLSDDESFQYNRkiqmifqdpyaslnprltvreimtepme 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVL---------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 117 ihglyggkkarlekadelleaVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQV-----V 191
Cdd:smart00382 47 ---------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190
....*....|....*....|....*....|....*.
gi 564753507 192 NLLKKLQKEKGLTFLFIAHDLSM-----VKHISDRI 222
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRR 141
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-229 |
1.19e-06 |
|
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: 50.29 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKnihnLSDDESFQY----NRKIQMIFQDPYASLNPRL 105
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----ISFSPQTSWimpgTIKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTEpmEIHGLYGgkkarlEKADELLEAVGLhksfanryphEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:TIGR01271 521 VIKACQLE--EDIALFP------EKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564753507 186 VQAQVV-NLLKKLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGH 229
Cdd:TIGR01271 583 TEKEIFeSCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGV 624
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-232 |
2.44e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGK-STSGRVLMRLYQPTEGEVTYRGknihnlsddeSFQYNRKIQMIFQdpyaslnprLTVR 108
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG----------TVAYVPQVSWIFN---------ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 EIMtepmeihgLYGG--KKARLEKAdelLEAVGLHKSFANRYPHEF----------SGGQRQRIGIARALALEPEFIVAD 176
Cdd:PLN03130 697 DNI--------LFGSpfDPERYERA---IDVTALQHDLDLLPGGDLteigergvniSGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 177 EPISALDVSVQAQVVNllKKLQKE-KGLTFLFIAHDLSMVKHIsDRIGVMYLGHMVE 232
Cdd:PLN03130 766 DPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-211 |
7.05e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 21 GKTVkaVDGISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVtYRGKnihnlsddesfqynrKIQMIFQDPY-A 99
Cdd:PRK11147 331 GKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGT---------------KLEVAYFDQHrA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 100 SLNPRLTV--------REIMTEPMEIHG-------LYGGKKARLE-KAdelleavglhksfanrypheFSGGQRQRIGIA 163
Cdd:PRK11147 393 ELDPEKTVmdnlaegkQEVMVNGRPRHVlgylqdfLFHPKRAMTPvKA--------------------LSGGERNRLLLA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564753507 164 RaLALEP-EFIVADEPISALDVsvqaQVVNLLKKLQKEKGLTFLFIAHD 211
Cdd:PRK11147 453 R-LFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
153-242 |
7.77e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 153 SGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKlQKEKGLTFLFIAHDLSMVKHIsDRIGVMYLGHM-- 230
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIke 819
|
90
....*....|....*.
gi 564753507 231 ----VEITDSSRLYQE 242
Cdd:PLN03232 820 egtfAELSKSGSLFKK 835
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
152-210 |
3.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 3.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564753507 152 FSGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKekglTFLFIAH 210
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
119-222 |
7.27e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.70 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 119 GLYGGKKARLEKA------------DEL--LEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPE--FIVADEPISAL 182
Cdd:cd03238 41 GLYASGKARLISFlpkfsrnklifiDQLqfLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 564753507 183 DVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:cd03238 121 HQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-183 |
1.10e-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: 44.13 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQpTEGEVTYRGKNIHNLsddeSFQYNRKI-----QMIF---------Q 95
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSV----TLQTWRKAfgvipQKVFifsgtfrknL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 96 DPYAslnpRLTVREIMTEPMEIhglygGKKARLE----KADELLEAVGlhksfanrypHEFSGGQRQRIGIARALALEPE 171
Cdd:TIGR01271 1313 DPYE----QWSDEEIWKVAEEV-----GLKSVIEqfpdKLDFVLVDGG----------YVLSNGHKQLMCLARSILSKAK 1373
|
170
....*....|..
gi 564753507 172 FIVADEPISALD 183
Cdd:TIGR01271 1374 ILLLDEPSAHLD 1385
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
119-183 |
1.33e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564753507 119 GLYGGKKARLEK-ADELLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFIVADEPISALD 183
Cdd:PRK10938 368 GIYQAVSDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
102-222 |
1.98e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 102 NPRLTVREIMtepmEIHG----LYG--GKKARLEkadeLLEAVGLHKSFANRYPHEFSGGQRQRIGIARAL--ALEPEFI 173
Cdd:cd03270 90 NPRSTVGTVT----EIYDylrlLFArvGIRERLG----FLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLY 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564753507 174 VADEPISALDVSVQAQVVNLLKKLqKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:cd03270 162 VLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-190 |
2.28e-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: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKnihnLSDDESFQY----NRKIQMIFQDPYASLNPRL 105
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----ISFSSQFSWimpgTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 106 TVREIMTEPmEIHGLyggkkarLEKADELLEAVGLhksfanryphEFSGGQRQRIGIARALALEPEFIVADEPISALDVS 185
Cdd:cd03291 132 VVKACQLEE-DITKF-------PEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
....*
gi 564753507 186 VQAQV 190
Cdd:cd03291 194 TEKEI 198
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-183 |
4.65e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.38 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 23 TVKAVDG-------ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQpTEGEVTYRGKNIHNLSDDE---SFQYNRKIQM 92
Cdd:cd03289 9 TAKYTEGgnavlenISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrkAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 93 IFQDPY-ASLNPrltvreimtepmeihglYGgkKARLEKADELLEAVGLhKSFANRYPHE-----------FSGGQRQRI 160
Cdd:cd03289 88 IFSGTFrKNLDP-----------------YG--KWSDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLM 147
|
170 180
....*....|....*....|...
gi 564753507 161 GIARALALEPEFIVADEPISALD 183
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLD 170
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-281 |
5.21e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 24 VKAVDGIsfdIKEGETFGLVGESGCGKSTSGRVLM-RLYQ---PTEGEVTYRGkniHNLSDDESFQ-----YNRKIQMIF 94
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsNTDGfhiGVEGVITYDG---ITPEEIKKHYrgdvvYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 95 qdpyaslnPRLTVREIM-------TEPMEIHGLygGKKARLEK-ADELLEAVGLHKSFANRYPHEF----SGGQRQRIGI 162
Cdd:TIGR00956 151 --------PHLTVGETLdfaarckTPQNRPDGV--SREEYAKHiADVYMATYGLSHTRNTKVGNDFvrgvSGGERKRVSI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 163 ARALALEPEFIVADEPISALDVSVQAQVVNLLKKLQKEKGLTFLFIAHDLSM-VKHISDRIGVMYLGHMVeitdssrlYQ 241
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQI--------YF 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 564753507 242 EPLH---PYTQALLSAIP----IPD--PDVEDKRKRIILKG-ELPSPIDP 281
Cdd:TIGR00956 293 GPADkakQYFEKMGFKCPdrqtTADflTSLTSPAERQIKPGyEKKVPRTP 342
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-226 |
5.76e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 5.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564753507 153 SGGQRQRIGIARALALEPE----FIVADEPISALDVSVQAQVVNLLKKLQKeKGLTFLFIAHDLSMVKhISDRIGVMY 226
Cdd:cd03227 79 SGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-183 |
1.42e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 30 ISFDIKEGETFGLVGESGCGKSTSGRVLMRLYQPTEGEVTYRGKniHNLSDDesfqynRKIQMIFQDPYASLNPRLTVRE 109
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGD------RSRFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564753507 110 imtepmEIHGLYG--GKKARlEKADELLEAVGLhKSFANRYPHEFSGGQRQRIGIARaLALEPEFI-VADEPISALD 183
Cdd:PRK13543 102 ------NLHFLCGlhGRRAK-QMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
109-222 |
1.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564753507 109 EIMTEPMEIHGLYGGKKARLEkadeLLEAVGLHKSFANRYPHEFSGGQRQRIGIARALALEPEFI--VADEPISALDVSV 186
Cdd:PRK00635 438 QLPSKSLSIEEVLQGLKSRLS----ILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQD 513
|
90 100 110
....*....|....*....|....*....|....*.
gi 564753507 187 QAQVVNLLKKLqKEKGLTFLFIAHDLSMVKhISDRI 222
Cdd:PRK00635 514 THKLINVIKKL-RDQGNTVLLVEHDEQMIS-LADRI 547
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
153-191 |
1.87e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 1.87e-03
10 20 30
....*....|....*....|....*....|....*....
gi 564753507 153 SGGQRQRIGIARALALEPEFIVADEPISALDVSVQAQVV 191
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVV 822
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
44-78 |
6.85e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.16 E-value: 6.85e-03
10 20 30
....*....|....*....|....*....|....*
gi 564753507 44 GESGCGKSTSGRVLMRLYQPTEGEVTYRGKNIHNL 78
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI 67
|
|
| |
