|
Name |
Accession |
Description |
Interval |
E-value |
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-323 |
0e+00 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 665.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQ 160
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADK 240
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 241 LYENPLHPYTRALLSATPAIHPDPTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLLDQRQVACHHAEQ 320
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAVEQ 321
|
...
gi 15599702 321 FLG 323
Cdd:PRK11308 322 DEN 324
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-323 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 584.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRGLFKGH-AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVK 79
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGGLFGRTvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 GASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQR 159
Cdd:COG4608 84 GLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPAD 239
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 240 KLYENPLHPYTRALLSATPAIHPDPTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLL-DQRQVACHHA 318
Cdd:COG4608 244 ELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVgPGHQVACHLA 323
|
....*
gi 15599702 319 EQFLG 323
Cdd:COG4608 324 EEGSG 328
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-320 |
2.55e-175 |
|
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: 488.02 E-value: 2.55e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALT-LIEEP--TSGSLKIAGQEVKG 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRG------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILgLLPPPgiTSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLR-RDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRP--EHYQRYPHMFSGG 157
Cdd:COG0444 75 LSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 158 QRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGP 237
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 238 ADKLYENPLHPYTRALLSATPAIHPDpTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLL-DQRQVACH 316
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLDPD-GRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVgPGHRVACH 313
|
....
gi 15599702 317 HAEQ 320
Cdd:COG0444 314 LYEE 317
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-263 |
3.74e-142 |
|
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: 411.22 E-value: 3.74e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGlfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGK-----GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQR 161
Cdd:COG1123 333 SRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 162 IALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
250 260
....*....|....*....|..
gi 15599702 242 YENPLHPYTRALLSATPAIHPD 263
Cdd:COG1123 493 FANPQHPYTRALLAAVPSLDPA 514
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-319 |
2.71e-138 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 394.84 E-value: 2.71e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEVSRG---LFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLI-NTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQR 159
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPAD 239
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 240 KLYENPLHPYTRALLSATPAIHPDPTKPKiRIQ---GELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLLDQRQVACH 316
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLERNK-TIQlleGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHAVSCL 326
|
...
gi 15599702 317 HAE 319
Cdd:PRK15079 327 KVD 329
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-258 |
3.19e-130 |
|
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: 381.34 E-value: 3.19e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGLFKGHA-QVRALNGVSFELEAGKTLAVVGESGCGKSTLARA-LTLIeePTSGSLKIAGQEVK 79
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGLFRRTVgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAlLRLI--PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 GASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLI-NTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQ 158
Cdd:COG4172 351 GLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 159 RQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPA 238
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
250 260
....*....|....*....|
gi 15599702 239 DKLYENPLHPYTRALLSATP 258
Cdd:COG4172 511 EQVFDAPQHPYTRALLAAAP 530
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-236 |
3.90e-116 |
|
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: 334.47 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASK 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGG------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREE-RREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRI 162
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-263 |
3.80e-111 |
|
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: 322.52 E-value: 3.80e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAskd 84
Cdd:COG1124 2 LEVRNLSVSYG------QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLIntaLSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIAL 164
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRI---HGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
250
....*....|....*....
gi 15599702 245 PLHPYTRALLSATPAIHPD 263
Cdd:COG1124 230 PKHPYTRELLAASLAFERA 248
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-256 |
2.24e-108 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 316.39 E-value: 2.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRGLFKGHaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLFRRQ-QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRdvqMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQ 160
Cdd:COG4167 80 GDYKYRCKHIR---MIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADK 240
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*.
gi 15599702 241 LYENPLHPYTRALLSA 256
Cdd:COG4167 237 VFANPQHEVTKRLIES 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-267 |
4.90e-97 |
|
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: 296.60 E-value: 4.90e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTrhyeVSrglFKGHAQ-VRALNGVSFELEAGKTLAVVGESGCGKSTLARA-LTLIEEP---TSGSLKIAG 75
Cdd:COG4172 3 SMPLLSVEDLS----VA---FGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSiLRLLPDPaahPSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 76 QEVKGASKDQRRQLR-RDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLR-PE-HYQRYPH 152
Cdd:COG4172 76 QDLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPErRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRP 232
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260 270
....*....|....*....|....*....|....*
gi 15599702 233 AEMGPADKLYENPLHPYTRALLSATPAIHPDPTKP 267
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPP 270
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-316 |
8.92e-91 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 273.91 E-value: 8.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRGLfkghaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEP---TSGSLKIAGQE 77
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGD------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 78 VKGASKDQRRQLR-RDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLrPEHYQR---YPHM 153
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRmkmYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 154 FSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPA 233
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 234 EMGPADKLYENPLHPYTRALLSATPAIHPD----PTkpkirIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLLD 309
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLLNAVPRLDAEgeslLT-----IPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGP 316
|
....*..
gi 15599702 310 QRQVACH 316
Cdd:PRK09473 317 GRLRACF 323
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-276 |
8.63e-89 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 277.89 E-value: 8.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGLF-KGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLnRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQ 160
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADK 240
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
250 260 270
....*....|....*....|....*....|....*..
gi 15599702 241 LYENPLHPYTRALLSATPAIHPDPTKP-KIRIQGELP 276
Cdd:PRK10261 551 VFENPQHPYTRKLMAAVPVADPSRQRPqRVLLSDDLP 587
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-316 |
3.32e-80 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 246.96 E-value: 3.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALT-LIEEP---TSGSLKIAGQEVKGASKDQRRQL-RRDVQMVFQN 99
Cdd:PRK11022 18 APFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMgLIDYPgrvMAEKLEFNGQDLQRISEKERRNLvGAEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 100 PYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLrPEHYQR---YPHMFSGGQRQRIALARAMMLQPKVLV 176
Cdd:PRK11022 98 PMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 177 ADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSA 256
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 257 TPAIHPDptkpKIRIQ---GELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLLDQRQVACH 316
Cdd:PRK11022 257 LPEFAQD----KARLAslpGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKCH 315
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-276 |
4.32e-80 |
|
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: 252.13 E-value: 4.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALT-LIEEP--TSGSLKIAGQE 77
Cdd:COG1123 1 MTPLLEVRDLSVRY--------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgLLPHGgrISGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 78 VKGASKDQRRqlrRDVQMVFQNPYASLNPrQKIGDQLAEPLLiNTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGG 157
Cdd:COG1123 73 LLELSEALRG---RRIGMVFQDPMTQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 158 QRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGP 237
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 15599702 238 ADKLYENPlhpytrALLSATPAIHPDPTKPKIRIQGELP 276
Cdd:COG1123 227 PEEILAAP------QALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-256 |
2.18e-79 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 242.77 E-value: 2.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRGLFKGHaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRRQ-TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRdvqMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQ 160
Cdd:PRK15112 80 GDYSYRSQRIR---MIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADK 240
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*.
gi 15599702 241 LYENPLHPYTRALLSA 256
Cdd:PRK15112 237 VLASPLHELTKRLIAG 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-262 |
1.85e-75 |
|
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: 232.39 E-value: 1.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYEVSrGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS 82
Cdd:TIGR02769 1 SLLEVRDVTHTYRTG-GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRI 162
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLY 242
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
250 260
....*....|....*....|
gi 15599702 243 ENPlHPYTRALLSATPAIHP 262
Cdd:TIGR02769 240 SFK-HPAGRNLQSAVLPEHP 258
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-256 |
1.76e-73 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 227.65 E-value: 1.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYEvSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS 82
Cdd:PRK10419 2 TLLNVSGLSHHYA-HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRI 162
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAE---MGPAD 239
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKL 240
|
250
....*....|....*..
gi 15599702 240 KLYenplHPYTRALLSA 256
Cdd:PRK10419 241 TFS----SPAGRVLQNA 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-257 |
1.91e-69 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 224.97 E-value: 1.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGLFKGH-AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARAL-TLIeePTSGSLKIAGQEVK 79
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILKRTvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALlRLI--NSQGEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 GASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLIN-TALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQ 158
Cdd:PRK15134 351 NLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 159 RQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPA 238
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
250
....*....|....*....
gi 15599702 239 DKLYENPLHPYTRALLSAT 257
Cdd:PRK15134 511 ERVFAAPQQEYTRQLLALS 529
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-264 |
3.54e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.39 E-value: 3.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 8 RDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRR 87
Cdd:COG1135 5 ENLSKTFPTKGG------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 88 QLRRDVQMVFQNpyASLNPRQKIGDQLAEPLLInTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARA 167
Cdd:COG1135 79 AARRKIGMIFQH--FNLLSSRTVAENVALPLEI-AGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 168 MMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLH 247
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
250
....*....|....*..
gi 15599702 248 PYTRALLSATPAIHPDP 264
Cdd:COG1135 235 ELTRRFLPTVLNDELPE 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-231 |
3.65e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 204.89 E-value: 3.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG1136 1 MSPLLELRNLTKSYG------TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRD-VQMVFQNPYasLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQR 159
Cdd:COG1136 75 LSERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLA-GVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGR 231
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGR 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-316 |
3.16e-64 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 205.91 E-value: 3.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 24 HAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEP----TSGSLKIAGQEVKGASKDQRRQL-RRDVQMVFQ 98
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIiGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 99 NPYASLNPRQKIGDQLAEPLLINTALSR-----EERREKVQQMMRQVGLR-PEHYQR-YPHMFSGGQRQRIALARAMMLQ 171
Cdd:COG4170 97 EPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKdHKDIMNsYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 172 PKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTR 251
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTK 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 252 ALLSATPAIHPD-PTKPKIR-IQGELPNPLNPPEGCAFHKRCPYATERCrSEVPELRLLDQRQVACH 316
Cdd:COG4170 257 ALLRSMPDFRQPlPHKSRLNtLPGSIPPLQHLPIGCRLGPRCPYAQKKC-VETPRLRKIKGHEFACH 322
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-254 |
1.22e-63 |
|
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: 201.36 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVF 97
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNP--YASLNprqkIGDQLAEPLLINTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:COG1127 89 QGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 176 VADEPTSALDvSIQAQVLN-LFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPlHPYTRALL 254
Cdd:COG1127 164 LYDEPTAGLD-PITSAVIDeLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-245 |
1.38e-62 |
|
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: 198.57 E-value: 1.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNpYA 102
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRqKIGDQLAEPLLInTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:cd03258 93 LLSSR-TVFENVALPLEI-AGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 183 ALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:cd03258 170 ALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-264 |
4.54e-62 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 205.71 E-value: 4.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 15 EVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARA-LTLIEEP----TSGSLKIAGQEVKGASKDQRRQL 89
Cdd:PRK15134 10 NLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSiLRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 90 RRD-VQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLR--PEHYQRYPHMFSGGQRQRIALAR 166
Cdd:PRK15134 90 RGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRqaAKRLTDYPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 167 AMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPL 246
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
250
....*....|....*...
gi 15599702 247 HPYTRALLSATPAIHPDP 264
Cdd:PRK15134 250 HPYTQKLLNSEPSGDPVP 267
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-245 |
3.64e-61 |
|
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: 194.47 E-value: 3.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgasKD 84
Cdd:COG1122 1 IELENLSFSYP---------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNPyaslnprqkiGDQLAEPL--------LINTALSREERREKVQQMMRQVGLrpEHY-QRYPHMFS 155
Cdd:COG1122 69 NLRELRRKVGLVFQNP----------DDQLFAPTveedvafgPENLGLPREEIRERVEEALELVGL--EHLaDRPPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 156 GGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEM 235
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTV-IIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
250
....*....|
gi 15599702 236 GPADKLYENP 245
Cdd:COG1122 216 GTPREVFSDY 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-231 |
6.99e-61 |
|
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: 193.48 E-value: 6.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:cd03255 1 IELKNLSKTYG------GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRD-VQMVFQNPYasLNPRQKIGDQLAEPLLInTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIA 163
Cdd:cd03255 75 ELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 164 LARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGR 231
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-255 |
2.61e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 190.21 E-value: 2.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkGASK 83
Cdd:COG1126 1 MIEIENLHKSF--------GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLRRDVQMVFQNpyASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIA 163
Cdd:COG1126 70 KDINKLRRKVGMVFQQ--FNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 164 LARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYE 243
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTM-VVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|..
gi 15599702 244 NPLHPYTRALLS 255
Cdd:COG1126 226 NPQHERTRAFLS 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-251 |
3.93e-59 |
|
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: 189.64 E-value: 3.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFK--GHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQM 95
Cdd:cd03261 4 RGLTKsfGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNP--YASLNprqkIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPK 173
Cdd:cd03261 82 LFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 174 VLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPlHPYTR 251
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVR 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-258 |
1.07e-58 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 198.93 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGS-------LKIA 74
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQ------KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmlLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 75 GQEVKGASKDQRRQLRR----DVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLrPEHYQ-- 148
Cdd:PRK10261 84 SRQVIELSEQSAAQMRHvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 149 -RYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:PRK10261 163 sRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
250 260 270
....*....|....*....|....*....|.
gi 15599702 228 YLGRPAEMGPADKLYENPLHPYTRALLSATP 258
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-231 |
6.81e-56 |
|
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: 180.36 E-value: 6.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgasKDQRRQLRRDVQMVFQNPya 102
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT---KLSLKELRRKVGLVFQNP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 slnPRQKIGDQLAEPL---LINTALSREERREKVQQMMRQVGLrpEHYQ-RYPHMFSGGQRQRIALARAMMLQPKVLVAD 178
Cdd:cd03225 85 ---DDQFFGPTVEEEVafgLENLGLPEEEIEERVEEALELVGL--EGLRdRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 179 EPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTI-IIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-246 |
7.90e-55 |
|
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: 178.05 E-value: 7.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkd 84
Cdd:cd03293 1 LEVRNVSKTYG------GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 qrrqlrRDVQMVFQNPyaSLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIAL 164
Cdd:cd03293 73 ------PDRGYVFQQD--ALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNL--AVvrHVADDVLVMYlGRPAEMGpadKLY 242
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVLS-ARPGRIV---AEV 216
|
....
gi 15599702 243 ENPL 246
Cdd:cd03293 217 EVDL 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
3.17e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 175.28 E-value: 3.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGG------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASkdqrrqlrRDVQMVFQNPyaSLNPRQKIGDQLAEPLLINTaLSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQ 160
Cdd:COG1116 78 PG--------PDRGVVFQEP--ALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNL--AVVrhVADDVLVM 227
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAVF--LADRVVVL 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-263 |
6.98e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 176.92 E-value: 6.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 8 RDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRR 87
Cdd:PRK11153 5 KNISKVFPQGGR------TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 88 QLRRDVQMVFQ--NPYASLNprqkIGDQLAEPL-LINTalSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIAL 164
Cdd:PRK11153 79 KARRQIGMIFQhfNLLSSRT----VFDNVALPLeLAGT--PKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSH 231
|
250
....*....|....*....
gi 15599702 245 PLHPYTRALLSATpaIHPD 263
Cdd:PRK11153 232 PKHPLTREFIQST--LHLD 248
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-249 |
1.36e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.44 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG3842 2 AMPALELENVSKRY----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 askdqrrqL---RRDVQMVFQNpYAsLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGG 157
Cdd:COG3842 72 --------LppeKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGL-EGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 158 QRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHN----LAvvrhVADDVLVMYLGRPA 233
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIE 215
|
250
....*....|....*.
gi 15599702 234 EMGPADKLYENPLHPY 249
Cdd:COG3842 216 QVGTPEEIYERPATRF 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-231 |
3.61e-51 |
|
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: 167.36 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkDQRRQLRRDVQMVF 97
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNPyaSLNPRQKIGDQLAEPLlintalsreerrekvqqmmrqvglrpehyqryphmfSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03229 83 QDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-236 |
1.40e-50 |
|
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: 166.93 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDqrrqlRRDVQMVF 97
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNPyaSLNPRQKIGDQLAEPLLINTaLSREERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-241 |
1.75e-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: 166.97 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEE-----PTSGSLKIAGQEVKGASKDqRRQLRRD 92
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVD-VLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 93 VQMVFQNPyaslNP-RQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQR-YPHMFSGGQRQRIALARAMML 170
Cdd:cd03260 83 VGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 171 QPKVLVADEPTSALDVSIQAQVLNLFMDLQQqfRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-245 |
3.61e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 3.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 19 GLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEV---KGASKDQRRQLRRDVQM 95
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNpYaSLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:COG4161 87 VFQQ-Y-NLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADkLYENP 245
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQ-VIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQP 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-231 |
5.49e-50 |
|
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: 165.40 E-value: 5.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkGASKD 84
Cdd:cd03262 1 IEIKNLHKSF--------GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNpyASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIAL 164
Cdd:cd03262 70 NINELRQKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTM-VVVTHEMGFAREVADRVIFMDDGR 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-245 |
8.89e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.96 E-value: 8.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 21 FKGHAQvrALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEV---KGASKDQRRQLRRDVQMVF 97
Cdd:PRK11124 11 FYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNpYaSLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:PRK11124 89 QQ-Y-NLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKlYENP 245
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELAETGITQ-VIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQP 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-255 |
3.01e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 164.54 E-value: 3.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 21 FKGHaqvRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA---SKDQR--RQLRRDVQM 95
Cdd:PRK11264 13 FHGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslSQQKGliRQLRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNpyASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:PRK11264 90 VFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLS 255
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTM-VIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-237 |
3.41e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 165.32 E-value: 3.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNPYAsln 105
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEH--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 prqkigdQLAE----------PLliNTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:TIGR04521 94 -------QLFEetvykdiafgPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGP 237
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-316 |
7.63e-49 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 166.13 E-value: 7.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIeepTSGSLKIAGQE------ 77
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRmrfddi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 78 --VKGASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSR-----EERREKVQQMMRQVGLRpEHY--- 147
Cdd:PRK15093 74 dlLRLSPRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIK-DHKdam 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 148 QRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 228 YLGRPAEMGPADKLYENPLHPYTRALLSATPAI-HPDPTKPKIR-IQGELPNPLNPPEGCAFHKRCPYATERCrSEVPEL 305
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDFgSAMPHKSRLNtLPGAIPLLEHLPIGCRLGPRCPYAQREC-IETPRL 311
|
330
....*....|.
gi 15599702 306 RLLDQRQVACH 316
Cdd:PRK15093 312 TGAKNHLYACH 322
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-182 |
9.32e-49 |
|
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: 160.12 E-value: 9.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPyaSLNPRQK 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 110 IGDQLAEPLLInTALSREERREKVQQMMRQVGLRPEHYQR---YPHMFSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:pfam00005 76 VRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-245 |
1.62e-48 |
|
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: 162.02 E-value: 1.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRqlrrdVQMVF 97
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-----VNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNpYAsLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03300 79 QN-YA-LFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-246 |
2.21e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.77 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskD 84
Cdd:COG1131 1 IEVRGLTKRY----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNP--YASLNPRQkigdqlaepLLINTA----LSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQ 158
Cdd:COG1131 67 DPAEVRRRIGYVPQEPalYPDLTVRE---------NLRFFArlygLPRKEARERIDELLELFGL-TDAADRKVGTLSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 159 RQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTayVFIS-HNLAVVRHVADDVLVMYLGRPAEMGP 237
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT--VLLStHYLEEAERLCDRVAIIDKGRIVADGT 214
|
....*....
gi 15599702 238 ADKLYENPL 246
Cdd:COG1131 215 PDELKARLL 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-242 |
4.44e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 161.38 E-value: 4.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYEvsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS 82
Cdd:COG3638 1 PMLELRNLSKRYP---------GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRRQLRRDVQMVFQNPYasLNPRQK------IGdQLAEPLLINTALSR--EERREKVQQMMRQVGLRPEHYQRyPHMF 154
Cdd:COG3638 72 GRALRRLRRRIGMIFQQFN--LVPRLSvltnvlAG-RLGRTSTWRSLLGLfpPEDRERALEALERVGLADKAYQR-ADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR--- 231
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRvvf 227
|
250
....*....|....*.
gi 15599702 232 ---PAEMGPA--DKLY 242
Cdd:COG3638 228 dgpPAELTDAvlREIY 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
29-231 |
5.47e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.60 E-value: 5.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNpyASLNPRQ 108
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAEPLLInTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:COG2884 95 TVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599702 189 QAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:COG2884 173 SWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-252 |
5.80e-48 |
|
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: 162.04 E-value: 5.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 20 LFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRR-DVQMVFQ 98
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 99 NpyASLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLRP-EHyqRYPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03294 110 S--FALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGLEGwEH--KYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRA 252
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-256 |
2.86e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 159.71 E-value: 2.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQ---- 76
Cdd:PRK11701 3 DQPLLSVRGLTKLY----------GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgql 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 77 -EVKGASKDQRRQL-RRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMF 154
Cdd:PRK11701 73 rDLYALSEAERRRLlRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAE 234
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
250 260
....*....|....*....|..
gi 15599702 235 MGPADKLYENPLHPYTRALLSA 256
Cdd:PRK11701 233 SGLTDQVLDDPQHPYTQLLVSS 254
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-286 |
8.89e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.08 E-value: 8.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQlrrdVQMVF 97
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERR----VGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNpYAsLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPKVLV 176
Cdd:COG1118 82 QH-YA-LFPHMTVAENIAFGLRVR-PPSKAEIRARVEELLELVQL--EGLaDRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 177 ADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSA 256
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270
....*....|....*....|....*....|.
gi 15599702 257 TPAIHPDPTKPKIRIQG-ELPNPLNPPEGCA 286
Cdd:COG1118 237 VNVLRGRVIGGQLEADGlTLPVAEPLPDGPA 267
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-231 |
1.22e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.51 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPYAslnPRQK 109
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQEPAL---WGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLLINtalSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQ 189
Cdd:COG4619 90 VRDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599702 190 AQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:COG4619 167 RRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-245 |
5.77e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 159.08 E-value: 5.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG-ASKDqrrqlrRDVQMV 96
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlPPKD------RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 97 FQNpYAsLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:COG3839 81 FQS-YA-LYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGL--EDLlDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-249 |
1.05e-44 |
|
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: 152.49 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgASKDQRRqlrRDVQMVF 97
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA--TDVPVQE---RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNpYAsLNPRQKIGDQLAEPLLINTALSR---EERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKV 174
Cdd:cd03296 81 QH-YA-LFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPY 249
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-255 |
1.06e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 153.27 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkGHAQvrALNGVSFELEAGKTLAVVGESGCGKSTLARALT----LIEEP-TSGSLKIAG 75
Cdd:COG1117 8 LEPKIEVRNLNVYY--------GDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmndLIPGArVEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 76 QEVKGASKDQRrQLRRDVQMVFQNPyaslNPRQK-IGDQLAEPLLINTALSREERREKVQQMMRQVGLRPE---HYQRYP 151
Cdd:COG1117 78 EDIYDPDVDVV-ELRRRVGMVFQKP----NPFPKsIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEvkdRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 152 HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFrtAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGE 230
|
250 260
....*....|....*....|....
gi 15599702 232 PAEMGPADKLYENPLHPYTRALLS 255
Cdd:COG1117 231 LVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-247 |
1.21e-44 |
|
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: 152.34 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQ-VRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMV 96
Cdd:cd03256 4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 97 FQNPyaSLNPRQKIGD-----QLAEPLLINTALSR--EERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMM 169
Cdd:cd03256 84 FQQF--NLIERLSVLEnvlsgRLGRRSTWRSLFGLfpKEEKQRALAALERVGLLDKAYQRADQL-SGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 170 LQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLH 247
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-231 |
1.07e-43 |
|
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: 147.39 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVF 97
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QnpyaslnprqkigdqlaepllintalsreerrekvqqmmrqvglrpehyqryphmFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTaYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-239 |
1.47e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 150.27 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaSKDQRRQLRRDVQMVFQNPyasln 105
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIRKKVGMVFQNP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIGDQLAEPL---LINTALSREERREKVQQMMRQVGLrpEHYQRY-PHMFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:TIGR04520 87 DNQFVGATVEDDVafgLENLGVPREEMRKRVDEALKLVGM--EDFRDRePHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 182 SALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGRPAEMG-PAD 239
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGtPRE 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-257 |
1.74e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.12 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 20 LFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEV----------KGASKDQRRQL 89
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 90 RRDVQMVFQnpYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMM 169
Cdd:PRK10619 91 RTRLTMVFQ--HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 170 LQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPY 249
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM-VVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
....*...
gi 15599702 250 TRALLSAT 257
Cdd:PRK10619 248 LQQFLKGS 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-254 |
2.80e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.09 E-value: 2.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 8 RDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRr 87
Cdd:PRK09493 5 KNVSKHF--------GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 88 QLRRDVQMVFQNPYasLNPRQKIGDQLA-EPLLINTAlSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALAR 166
Cdd:PRK09493 74 LIRQEAGMVFQQFY--LFPHLTALENVMfGPLRVRGA-SKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 167 AMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPL 246
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTM-VIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
....*...
gi 15599702 247 HPYTRALL 254
Cdd:PRK09493 229 SQRLQEFL 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
29-256 |
4.91e-43 |
|
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: 148.22 E-value: 4.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrRQLRRDVQMVFQNpyASLNPRQ 108
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELRRKIGYVIQQ--IGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAeplLINTAL--SREERREKVQQMMRQVGLRPEHY-QRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:cd03295 91 TVEENIA---LVPKLLkwPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSA 256
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-231 |
5.82e-43 |
|
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: 147.50 E-value: 5.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASK 83
Cdd:TIGR02211 1 LLKCENLGKRYQ------EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLR-RDVQMVFQnpYASLNPRQKIGDQLAEPLLINTaLSREERREKVQQMMRQVGL--RPEHYqryPHMFSGGQRQ 160
Cdd:TIGR02211 75 NERAKLRnKKLGFIYQ--FHHLLPDFTALENVAMPLLIGK-KSVKEAKERAYEMLEKVGLehRINHR---PSELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGR 231
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQ 218
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
22-256 |
6.81e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 148.02 E-value: 6.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 22 KGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskdQRRQLRRDVQMVFQNpY 101
Cdd:TIGR00968 8 KRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAT-----RVHARDRKIGFVFQH-Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 AsLNPRQKIGDQLAEPLLINTaLSREERREKVQQMMRQVGLrpEHYQ-RYPHMFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:TIGR00968 82 A-LFKHLTVRDNIAFGLEIRK-HPKAKIKARVEELLELVQL--EGLGdRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSA 256
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGE 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
29-231 |
1.22e-42 |
|
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: 144.83 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPYaslnprq 108
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKNIAYVPQDPF------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kigdqlaeplLINTALsreerREKVqqmmrqvglrpehyqryphmFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:cd03228 87 ----------LFSGTI-----RENI--------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599702 189 QAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLVMYLGR 231
Cdd:cd03228 132 EALILEALRALAKG-KTV-IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
29-243 |
2.81e-42 |
|
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: 154.99 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPY---ASLn 105
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQIGVVLQDVFlfsGTI- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 prqkigdqlAEplliNTALSREER-REKVQQMMRQVGL------RPEHYQRY----PHMFSGGQRQRIALARAMMLQPKV 174
Cdd:COG2274 566 ---------RE----NITLGDPDAtDEEIIEAARLAGLhdfieaLPMGYDTVvgegGSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYE 243
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKG-RTV-IIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLA 698
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-262 |
5.97e-42 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 146.00 E-value: 5.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKS-TLARALTLIE---EPTSGSLKIAGQEVKGASkdqrrqLR-RDVQMVFQN 99
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCA------LRgRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 100 PYASLNPRQKIGDQLAEPLLintALSREERREKVQQMMRQVGL--RPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:PRK10418 88 PRSAFNPLHTMHTHARETCL---ALGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSAT 257
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAH 244
|
....*
gi 15599702 258 PAIHP 262
Cdd:PRK10418 245 LALYG 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-215 |
2.38e-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: 143.73 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:COG4181 6 APIIELRGLTKTVGTGAG------ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRQLRRD-VQMVFQNpyaslnprqkigdqlaEPLLIN-TAL----------SREERREKVQQMMRQVGL--RPEHY 147
Cdd:COG4181 80 DEDARARLRARhVGFVFQS----------------FQLLPTlTALenvmlplelaGRRDARARARALLERVGLghRLDHY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 148 qryPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLA 215
Cdd:COG4181 144 ---PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-245 |
2.58e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 146.79 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 13 HYEVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRrqlrrD 92
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR-----D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 93 VQMVFQNpYAsLNPRQKIGDQLAEPLLInTALSREERREKVQQMMRQVGLrpEHYQ-RYPHMFSGGQRQRIALARAMMLQ 171
Cdd:PRK11432 80 ICMVFQS-YA-LFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDL--AGFEdRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 172 PKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-243 |
2.90e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.77 E-value: 2.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEvsrglfkgHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkg 80
Cdd:PRK13635 2 KEEIIRVEHISFRYP--------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 aSKDQRRQLRRDVQMVFQNPyaslnPRQKIGDQLAEPL---LINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGG 157
Cdd:PRK13635 72 -SEETVWDVRRQVGMVFQNP-----DNQFVGATVQDDVafgLENIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 158 QRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGRPAEMGP 237
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
....*.
gi 15599702 238 ADKLYE 243
Cdd:PRK13635 224 PEEIFK 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-244 |
3.80e-41 |
|
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: 143.46 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEvsrglfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgask 83
Cdd:COG4555 1 MIEVENLSKKYG----------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLRRDVQMVFQNP--YASLNPRQKIgdqlaepLLINTA--LSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQR 159
Cdd:COG4555 67 KEPREARRQIGVLPDERglYDRLTVRENI-------RYFAELygLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPAD 239
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV-LFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
....*
gi 15599702 240 KLYEN 244
Cdd:COG4555 218 ELREE 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-244 |
9.52e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 149.52 E-value: 9.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEVSRglfkghaqvRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:COG4988 337 IELEDVSFSYPGGR---------PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QrrqLRRDVQMVFQNPYasLnprqkIGDQLAEPLLI-NTALSREErrekVQQMMRQVGLRpEHYQRYPH----------- 152
Cdd:COG4988 408 S---WRRQIAWVPQNPY--L-----FAGTIRENLRLgRPDASDEE----LEAALEAAGLD-EFVAALPDgldtplgeggr 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLVMYLGRP 232
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTV-ILITHRLALLAQ-ADRILVLDDGRI 549
|
250
....*....|..
gi 15599702 233 AEMGPADKLYEN 244
Cdd:COG4988 550 VEQGTHEELLAK 561
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
29-245 |
2.01e-40 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 143.31 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNpyASLNPRQ 108
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRRIGYVIQQ--IGLFPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAE-PLLINTalSREERREKVQQMMRQVGLRPEHY-QRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:COG1125 92 TVAENIATvPRLLGW--DKERIRARVDELLELVGLDPEEYrDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAYVFISHNL--AVvrHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:COG1125 170 ITREQLQDELLRLQRELGKTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
3.55e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.99 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEvsrglfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG1121 3 MMPAIELENLTVSYG----------GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKD-----QRRQLRRDV-----QMVFQNPYASLNPRQKIgdqlaepllintalsREERREKVQQMMRQVGLrpEHYQRY 150
Cdd:COG1121 73 ARRRigyvpQRAEVDWDFpitvrDVVLMGRYGRRGLFRRP---------------SRADREAVDEALERVGL--EDLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 151 P-HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVM-- 227
Cdd:COG1121 136 PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTI-LVVTHDLGAVREYFDRVLLLnr 214
|
250
....*....|
gi 15599702 228 ---YLGRPAE 234
Cdd:COG1121 215 glvAHGPPEE 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
26-243 |
4.84e-40 |
|
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: 140.51 E-value: 4.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNpYAsLN 105
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIGMIFQH-YN-LI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIGDQLAEPLL-----INTALSR--EERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVAD 178
Cdd:TIGR02315 92 ERLTVLENVLHGRLgykptWRSLLGRfsEEDKERALSALERVGLADKAYQRADQL-SGGQQQRVAIARALAQQPDLILAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 179 EPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYE 243
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-231 |
5.10e-40 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 137.95 E-value: 5.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqRRQLRRDVQMVF 97
Cdd:cd03216 4 RGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP--RDARRAGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QnpyaslnprqkigdqlaepllintalsreerrekvqqmmrqvglrpehyqryphmFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03216 82 Q-------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-239 |
7.89e-40 |
|
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: 140.18 E-value: 7.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASk 83
Cdd:COG1120 1 MLEAENLSVGY--------GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 dqRRQLRRDVQMVFQNPYASLN------------PRQKIGDQLaepllintalsREERREKVQQMMRQVGLrpEHY-QRY 150
Cdd:COG1120 70 --RRELARRIAYVPQEPPAPFGltvrelvalgryPHLGLFGRP-----------SAEDREAVEEALERTGL--EHLaDRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 151 PHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLG 230
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
....*....
gi 15599702 231 RPAEMGPAD 239
Cdd:COG1120 215 RIVAQGPPE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-236 |
3.46e-39 |
|
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: 137.39 E-value: 3.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS-KDqrrqlrRDVQMV 96
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKD------RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 97 FQNpYAsLNPRQKIGDQLAEPLLINTAlSREERREKVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:cd03301 78 FQN-YA-LYPHMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQI--EHLlDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-231 |
5.16e-39 |
|
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: 135.60 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskDQRRQLRRDVQMVF 97
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNP--YASLNPRQKIgdqlaepllintalsreerrekvqqmmrqvglrpehyqryphMFSGGQRQRIALARAMMLQPKVL 175
Cdd:cd03230 80 EEPslYENLTVRENL------------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGR 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-245 |
5.20e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.19 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQR-RQLRRDVQMVFQNPYASL 104
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 NPRQKIGDQLAEPLliNTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSAL 184
Cdd:PRK13641 99 FENTVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 185 DVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTV-ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
29-237 |
3.71e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.61 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNPY---ASLn 105
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTFlfsGTI- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 prqkigdqlAEplliNTALSREER-REKVQQMMRQVGLRpEHYQRYPH-----------MFSGGQRQRIALARAMMLQPK 173
Cdd:COG1132 431 ---------RE----NIRYGRPDAtDEEVEEAAKAAQAH-EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 174 VLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGP 237
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKG-RTT-IVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-245 |
5.56e-38 |
|
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: 137.63 E-value: 5.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 45 VVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskdQRRQLRRDVQMVFQNpYAsLNPRQKIGDQLAEPLLINtAL 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMR-KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 125 SREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFR 204
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599702 205 TAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
18-256 |
6.46e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 135.31 E-value: 6.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVK----------GASKDQRR 87
Cdd:COG4598 12 RDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvPADRRQLQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 88 QLRRDVQMVFQ--NPYASLNPRQKIgdqLAEPLLINtALSREERREKVQQMMRQVGL-RPEHYqrYPHMFSGGQRQRIAL 164
Cdd:COG4598 92 RIRTRLGMVFQsfNLWSHMTVLENV---IEAPVHVL-GRPKAEAIERAEALLAKVGLaDKRDA--YPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVfISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 15599702 245 PLHPYTRALLSA 256
Cdd:COG4598 245 PKSERLRQFLSS 256
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-245 |
7.14e-38 |
|
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: 134.49 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHyevsrglFKGhaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:cd03219 1 LEVRGLTKR-------FGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRqlRRDVQMVFQNP--YASLNPRQ--KIGDQLAEPLLINTALSREER---REKVQQMMRQVGLRpEHYQRYPHMFSGG 157
Cdd:cd03219 71 EIA--RLGIGRTFQIPrlFPELTVLEnvMVAAQARTGSGLLLARARREEreaRERAEELLERVGLA-DLADRPAGELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 158 QRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTaYVFISHNLAVVRHVADDVLVMYLGRPAEMGP 237
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGIT-VLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
....*...
gi 15599702 238 ADKLYENP 245
Cdd:cd03219 227 PDEVRNNP 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-256 |
1.30e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.73 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEAGKTLAVVGESGCGKSTLaraLTLI---EEPTSGSLKIAGQEVKGASKDQRrqlrrDVQMVFQ--NPYASLNPRQ 108
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTL---LNLIagfLPPDSGRILWNGQDLTALPPAER-----PVSMLFQenNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGdqlaepLLINTALS-REERREKVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:COG3840 91 NIG------LGLRPGLKlTAEQRAQVEQALERVGL--AGLlDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSA 256
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-244 |
4.83e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.02 E-value: 4.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGaSKDQRRQLRRDVQMVFQNPYASLNPR 107
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QKIGDQLAEPllINTALSREERREKVQQMMRQVGLRPEHYQ-RYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:PRK13637 100 TIEKDIAFGP--INLGLSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
29-241 |
8.63e-37 |
|
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: 131.58 E-value: 8.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPYAslnprq 108
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQDTFL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kigdqLAEPLLINTALSREE-RREKVQQMMRQVGL------RPEHYQRYP----HMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03254 89 -----FSGTIMENIRLGRPNaTDEEVIEAAKEAGAhdfimkLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 178 DEPTSALDVS----IQAQVLNLFMDlqqqfRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03254 164 DEATSNIDTEteklIQEALEKLMKG-----RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-231 |
2.64e-36 |
|
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: 128.71 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVqmvf 97
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 qnpyaslnprqkigdqlaepllintALsreerrekVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPKVLV 176
Cdd:cd03214 76 -------------------------AY--------VPQALELLGL--AHLaDRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 177 ADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-255 |
4.56e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 136.43 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfkgHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:COG4987 334 LELEDVSFRYP--------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLrrdVQMVFQNPY---ASlnprqkigdqLAEPLLI-NTALSREErrekVQQMMRQVGLRP--------------EH 146
Cdd:COG4987 406 DLRRR---IAVVPQRPHlfdTT----------LRENLRLaRPDATDEE----LWAALERVGLGDwlaalpdgldtwlgEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 147 YQRyphmFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLV 226
Cdd:COG4987 469 GRR----LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTV-LLITHRLAGLER-MDRILV 541
|
250 260
....*....|....*....|....*....
gi 15599702 227 MYLGRPAEMGPADKLYENplHPYTRALLS 255
Cdd:COG4987 542 LEDGRIVEQGTHEELLAQ--NGRYRQLYQ 568
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-227 |
1.22e-35 |
|
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: 128.71 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEVSRglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKI--AGQEV 78
Cdd:COG4778 1 MTTLLEVENLSKTFTLHL---QGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 79 KGASKDQRR--QLRRDVQmvfqnPYAS--LN--PRQKIGDQLAEPLLiNTALSREERREKVQQMMRQVGLRPEHYQRYPH 152
Cdd:COG4778 78 DLAQASPREilALRRRTI-----GYVSqfLRviPRVSALDVVAEPLL-ERGVDREEARARARELLARLNLPERLWDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-201 |
1.95e-35 |
|
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: 127.52 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 27 VRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNpyASLNP 106
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 RQKIGDQLAEPLLInTALSREERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:cd03292 92 DRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170
....*....|....*
gi 15599702 187 SIQAQVLNLFMDLQQ 201
Cdd:cd03292 170 DTTWEIMNLLKKINK 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-250 |
2.03e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 128.81 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALT-LIE----EPTSGSLKIAGQEVKGASKDQRRqLRRDVQMVFQ--NPYa 102
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLElneeARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQypNPF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 slnPRQKIGDQLAEPLLINTAL-SREERREKVQQMMRQVGLRPEHYQR---YPHMFSGGQRQRIALARAMMLQPKVLVAD 178
Cdd:PRK14267 98 ---PHLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 179 EPTSALDVSIQAQVLNLFMDLQQQFrtAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYT 250
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-245 |
2.20e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.61 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRrqlrrDVQMVF 97
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR-----HVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNpYAsLNPRQKIGDQLAEPLLINTaLSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:PRK09452 93 QS-YA-LFPHMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
29-234 |
4.20e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.57 E-value: 4.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPyaslnPRQ 108
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIG----DQLAEPLLiNTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSAL 184
Cdd:PRK13632 96 FIGatveDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 185 DVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRhVADDVLVM------YLGRPAE 234
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFsegkliAQGKPKE 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-245 |
4.93e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 128.27 E-value: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgASKDQRRQLRRDVQMVFQNPyaslnprq 108
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNP-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kiGDQLAEPLL--------INTALSREERREKVQQMMRQVGLrpEHYQRY-PHMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:PRK13639 88 --DDQLFAPTVeedvafgpLNLGLSKEEVEKRVKEALKAVGM--EGFENKpPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 180 PTSALDVSIQAQVLNLFMDLQQQFRTayVFIS-HNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEGIT--IIIStHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-245 |
6.88e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.21 E-value: 6.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIaGQEVKGASKDQR--RQLRRDVQMVFQNPYASLN 105
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKklKPLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIGDQLAEPllINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK13634 100 EETVEKDICFGP--MNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-241 |
1.60e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEAGKTLAVVGESGCGKSTLaraLTLIE---EPTSGSLKIAGQEVKGASKDQRrqlrrDVQMVFQ--NPYASLNPRQ 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL---LNLIAgflTPASGSLTLNGQDHTTTPPSRR-----PVSMLFQenNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAEPLLINtalsrEERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:PRK10771 91 NIGLGLNPGLKLN-----AAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 189 QAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-227 |
1.71e-34 |
|
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: 124.95 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD-----QRRQLRRDV-----QM 95
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyvpQRRSIDRDFpisvrDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNPYASLNPRQKIgdqlaepllintalsREERREKVQQMMRQVGLrpEHYQRYP-HMFSGGQRQRIALARAMMLQPKV 174
Cdd:cd03235 91 VLMGLYGHKGLFRRL---------------SKADKAKVDEALERVGL--SELADRQiGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVM 227
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTI-LVVTHDLGLVLEYFDRVLLL 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-227 |
1.82e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.29 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG1129 1 AEPLLEMRGISKSF----------GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRrdVQMVFQ--NPYASLNPRQKI--GDQLAEPLLINtalsREERREKVQQMMRQVGLRPEhyqryPHM--- 153
Cdd:COG1129 71 RSPRDAQAAG--IAIIHQelNLVPNLSVAENIflGREPRRGGLID----WRAMRRRARELLARLGLDID-----PDTpvg 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 154 -FSGGQRQRIALARAMMLQPKVLVADEPTSALDvsiQAQVLNLF---MDLQQQfRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:COG1129 140 dLSVAQQQLVEIARALSRDARVLILDEPTASLT---EREVERLFriiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-227 |
1.91e-34 |
|
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: 124.68 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 21 FKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskdqRRQLRRDVQMVFQNP 100
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YaslnpRQKIGDQLAEPLLINTALSrEERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:cd03226 81 D-----YQLFTDSVREELLLGLKEL-DAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-254 |
2.22e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.38 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRD-VQMVFQNpyASLNPRQKIGD 112
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 113 QLAEPLLInTALSREERREKVQQMMRQVGLrpEHYQR-YPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQ 191
Cdd:PRK10070 126 NTAFGMEL-AGINAEERREKALDALRQVGL--ENYAHsYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 192 VLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALL 254
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-239 |
2.41e-34 |
|
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: 125.92 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHyevsrglFKGhaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG0411 1 SDPLLEVRGLTKR-------FGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQ--RRQLRRdvqmVFQNP--YASLNPRQ--------KIGDQLAEPLLINTALSREER--REKVQQMMRQVGLRpEH 146
Cdd:COG0411 71 LPPHRiaRLGIAR----TFQNPrlFPELTVLEnvlvaahaRLGRGLLAALLRLPRARREEReaRERAEELLERVGLA-DR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 147 YQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLV 226
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVV 225
|
250
....*....|....
gi 15599702 227 MYLGRP-AEMGPAD 239
Cdd:COG0411 226 LDFGRViAEGTPAE 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-236 |
2.61e-34 |
|
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: 124.71 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGkTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskDQRRQL-----RRDVQMVFQNpyASLNPR 107
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF----DSRKKInlppqQRKIGLVFQQ--YALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QKIGDQLAEPLlinTALSREERREKVQQMMRQVGLRPEHYqRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVS 187
Cdd:cd03297 90 LNVRENLAFGL---KRKRNREDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599702 188 IQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-245 |
2.89e-34 |
|
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: 125.14 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDqrrqlRRDVQMVFQNpYAsLNPRQK 109
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQN-YA-LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLlINTALSREERREKVQQMMRQVGLrpEH-YQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:cd03299 88 VYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGI--DHlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 189 QAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-245 |
2.97e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 128.28 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRqlrrdVQMVFQNpYA 102
Cdd:PRK10851 13 GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-----VGFVFQH-YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 sLNPRQKIGDQLAEPLlinTALSREER------REKVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:PRK10851 85 -LFRHMTVFDNIAFGL---TVLPRRERpnaaaiKAKVTQLLEMVQL--AHLaDRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-241 |
5.08e-34 |
|
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: 124.65 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 21 FKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNP 100
Cdd:cd03253 8 FAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 ------------YASLNprqkigdqlAEPLLINTALSREERREKVQQMmrqvglrPEHYQ-----RyPHMFSGGQRQRIA 163
Cdd:cd03253 85 vlfndtigynirYGRPD---------ATDEEVIEAAKAAQIHDKIMRF-------PDGYDtivgeR-GLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 164 LARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTT-IVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-241 |
2.07e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.31 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNpyASLNPR 107
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNIAVVFQD--AGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QkIGDQL------AEPLLINTALSRE------ERREKVQQMMrqVGLRPEhyqryphMFSGGQRQRIALARAMMLQPKVL 175
Cdd:PRK13657 424 S-IEDNIrvgrpdATDEEMRAAAERAqahdfiERKPDGYDTV--VGERGR-------QLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 176 VADEPTSALDVSIQAQVlNLFMDLQQQFRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:PRK13657 494 ILDEATSALDVETEAKV-KAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-227 |
3.68e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 123.05 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS 82
Cdd:COG4525 2 SMLTVRHVSVRYP------GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDqrrqlrRDVqmVFQNpyASLNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRI 162
Cdd:COG4525 76 AD------RGV--VFQK--DALLPWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNL--AVVrhVADDVLVM 227
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVM 208
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-316 |
5.72e-33 |
|
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: 117.08 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 234 EMGPADKLYENPLHPYTRALLSATPAIHpDPTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPEL-RLLDQRQ 312
Cdd:TIGR01727 4 ETGPAEEIFKNPLHPYTKALLSAIPTIK-KRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALvEIAEGHR 82
|
....
gi 15599702 313 VACH 316
Cdd:TIGR01727 83 VACH 86
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
6.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.60 E-value: 6.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEVSRglfkghaqvRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSK 83
Cdd:PRK13652 3 LIETRDLCYSYSGSK---------EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLRRDVQMVFQNPyaslnprqkiGDQLAEPLL--------INTALSREERREKVQQMMRQVGLrpEHYQ-RYPHMF 154
Cdd:PRK13652 71 ENIREVRKFVGLVFQNP----------DDQIFSPTVeqdiafgpINLGLDEETVAHRVSSALHMLGL--EELRdRVPHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAE 234
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
250
....*....|.
gi 15599702 235 MGPADKLYENP 245
Cdd:PRK13652 219 YGTVEEIFLQP 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-244 |
7.33e-33 |
|
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: 121.49 E-value: 7.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLaraLTLIE---EPTSGSLKIAGQEVKgaskdqrrqlrrdvqmvfqnpya 102
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLErfyDPTSGEILLDGVDIR----------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNP---RQKIG--DQlaEPLLINT------ALSREER-REKVQQMMRQVGLR------PEHYQRY--PH--MFSGGQRQ 160
Cdd:cd03249 69 DLNLrwlRSQIGlvSQ--EPVLFDGtiaeniRYGKPDAtDEEVEEAAKKANIHdfimslPDGYDTLvgERgsQLSGGQKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQV---LNLFMdlqqQFRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMGP 237
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVqeaLDRAM----KGRTTIV-IAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
....*..
gi 15599702 238 ADKLYEN 244
Cdd:cd03249 221 HDELMAQ 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-245 |
2.75e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.03 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaskD 84
Cdd:PRK11650 4 LKLQAVRKSYD---------GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNpYAsLNPRQKIGDQLAEPLLiNTALSREERREKVQQMMRQVGLRPeHYQRYPHMFSGGQRQRIAL 164
Cdd:PRK11650 70 ELEPADRDIAMVFQN-YA-LYPHMSVRENMAYGLK-IRGMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
.
gi 15599702 245 P 245
Cdd:PRK11650 226 P 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-241 |
3.65e-32 |
|
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: 119.40 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 16 VSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQrRQLRRDVQM 95
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQnpYASLNprqkigDQLA--EPLLINTAL---SREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMML 170
Cdd:cd03265 78 VFQ--DLSVD------DELTgwENLYIHARLygvPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 171 QPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-249 |
4.26e-32 |
|
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: 122.53 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgASKDQRRQL---RRDVQMVFQNpyASLNPRQK 109
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL--FDSRKGIFLppeKRRIGYVFQE--ARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLLINTALSREERREKVQQMMrqvGLRPeHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQ 189
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELL---GIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 190 AQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPY 249
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-243 |
4.93e-32 |
|
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: 119.26 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPYAslnprq 108
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQDVFL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kIGDQLAEplliNTALSR-EERREKVQQMMRQVGLRpEHYQRYPHMF-----------SGGQRQRIALARAMMLQPKVLV 176
Cdd:cd03251 88 -FNDTVAE----NIAYGRpGATREEVEEAARAANAH-EFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 177 ADEPTSALDVS----IQAQVLNLFMDlqqqfRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYE 243
Cdd:cd03251 162 LDEATSALDTEserlVQAALERLMKN-----RTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-236 |
6.64e-32 |
|
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: 118.36 E-value: 6.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 37 LEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDqrrqlRRDVQMVFQ--NPYASLNPRQKIGDQL 114
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQenNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 115 AEPLLINtalsrEERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLN 194
Cdd:cd03298 96 SPGLKLT-----AEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599702 195 LFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
24-262 |
9.35e-32 |
|
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: 121.64 E-value: 9.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 24 HAQVrALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEP--TSGSLKIAGQEVKGASKdqrrqLRRDVQMVFQNpY 101
Cdd:TIGR03258 16 GANT-VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPP-----HKRGLALLFQN-Y 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 AsLNPRQKIGDQLAEPLLINTaLSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:TIGR03258 89 A-LFPHLKVEDNVAFGLRAQK-MPKADIAERVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 182 SALDVSIQAQVLNLFMDLQQQF-RTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSATPAI 260
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245
|
..
gi 15599702 261 HP 262
Cdd:TIGR03258 246 PA 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-250 |
9.66e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.86 E-value: 9.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 16 VSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALT-LIE---EP-TSGSLKIAGQEVkgaSKDQRRQLR 90
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIElypEArVSGEVYLDGQDI---FKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 91 RDVQMVFQ--NPYASLNprqkIGDQLAEPLLIN-TALSREERREKVQQMMRQVGLRPEHYQRY---PHMFSGGQRQRIAL 164
Cdd:PRK14247 82 RRVQMVFQipNPIPNLS----IFENVALGLKLNrLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFrtAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
....*.
gi 15599702 245 PLHPYT 250
Cdd:PRK14247 236 PRHELT 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-243 |
1.90e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPyaslnPRQ 108
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAEPL---LINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK13648 96 FVGSIVKYDVafgLENHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYE 243
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
30-231 |
2.20e-31 |
|
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: 115.78 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQ----LRRDVQMvfqnpyasln 105
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDhvgyLPQDDEL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 prqkIGDQLAEpllintalsreerrekvqqmmrqvglrpehyqrypHMFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:cd03246 88 ----FSGSIAE-----------------------------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRhVADDVLVMYLGR 231
Cdd:cd03246 129 VEGERALNQAIAALKAAGATR-IVIAHRPETLA-SADRILVLEDGR 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-237 |
3.35e-31 |
|
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: 122.60 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHY-EVSRGLfkghaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKI-AGQEVK 79
Cdd:TIGR03269 277 EPIIKVRNVSKRYiSVDRGV------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 GASK---DQRRQLRRDVQMVFQNpYaSLNPRQKIGDQLAEPllINTALSREERREKVQQMMRQVGLRPEHYQ----RYPH 152
Cdd:TIGR03269 351 DMTKpgpDGRGRAKRYIGILHQE-Y-DLYPHRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKAEeildKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRP 232
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*
gi 15599702 233 AEMGP 237
Cdd:TIGR03269 507 VKIGD 511
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-236 |
3.49e-31 |
|
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: 116.50 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrrqLRRDVQMVFQ--NPYASLNPRQKIG 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP-----YQRPVSMLFQenNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 112 DQLAEPLLINTalsreERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQ 191
Cdd:TIGR01277 93 LGLHPGLKLNA-----EQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 192 VLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-212 |
5.50e-31 |
|
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: 115.65 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTrhyeVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgask 83
Cdd:COG4133 2 MLEAENLS----CRRG------ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLRRDVQMVFqnPYASLNPRQKIGDQLAeplLINTALSREERREKVQQMMRQVGLRPeHYQRYPHMFSGGQRQRIA 163
Cdd:COG4133 68 DAREDYRRRLAYLG--HADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599702 164 LARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISH 212
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTH 189
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-216 |
5.96e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 122.53 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:PRK10535 1 MTALLELKDIRRSYP------SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRD-VQMVFQNPY--ASLNPRQKIgdqlaEPLLINTALSREERREKVQQMMRQVGLRPE-HYQryPHMFSG 156
Cdd:PRK10535 75 LDADALAQLRREhFGFIFQRYHllSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLEDRvEYQ--PSQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 157 GQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAV 216
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTV-IIVTHDPQV 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-235 |
7.71e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.07 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEvsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASK 83
Cdd:PRK11629 5 LLQCDNLCKRYQ------EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLR-RDVQMVFQnpYASLNPRQKIGDQLAEPLLINTAlSREERREKVQQMMRQVGLRPEHYQRyPHMFSGGQRQRI 162
Cdd:PRK11629 79 AAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvaddvlvmyLGRPAEM 235
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR---------MSRQLEM 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-251 |
1.25e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.78 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 6 TARDLTRHYEVsRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQ 85
Cdd:PRK11607 12 TRKALTPLLEI-RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 86 RrqlrrDVQMVFQNpYAsLNPRQKIGDQLAEPLLiNTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALA 165
Cdd:PRK11607 91 R-----PINMMFQS-YA-LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 166 RAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEnp 245
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE-- 239
|
....*.
gi 15599702 246 lHPYTR 251
Cdd:PRK11607 240 -HPTTR 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-250 |
1.68e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.91 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQeVKGASKDQRR----QLRRDVQMVFQ--NPYas 103
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDIFQidaiKLRKEVGMVFQqpNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 104 lnPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRY---PHMFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQFrtAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYT 250
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-231 |
2.63e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.98 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPyaslnPRQK 109
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVFQNP-----DNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPL---LINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:PRK13650 95 VGATVEDDVafgLENKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRhVADDVLVMYLGR 231
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-236 |
2.76e-30 |
|
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: 114.49 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqlrrdvQMVFQNpyASLNPRQK 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR--------MVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAepLLINTA---LSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:TIGR01184 71 VRENIA--LAVDRVlpdLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-242 |
3.62e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQR-RQLRRDVQMVFQNPYASL 104
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 nprqkIGDQLAEPLLI---NTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:PRK13646 99 -----FEDTVEREIIFgpkNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 182 SALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLY 242
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-245 |
4.13e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.49 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKI--------AGQEVKGASKDQRR-----QLRRD 92
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHELITNPYSKKiknfkELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 93 VQMVFQNPYASLNPRQKIGDQLAEPllINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQP 172
Cdd:PRK13631 118 VSMVFQFPEYQLFKDTIEKDIMFGP--VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 173 KVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVfISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-239 |
4.18e-30 |
|
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: 119.85 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQ----LRRDVQMvfqnp 100
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhigyLPQDVEL----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 yaslnprqkIGDQLAEplliNTALSREERREKVQQMMRQVG-----LR-PEHYQRYP----HMFSGGQRQRIALARAMML 170
Cdd:COG4618 418 ---------FDGTIAE----NIARFGDADPEKVVAAAKLAGvhemiLRlPDGYDTRIgeggARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 171 QPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVaDDVLVMYLGRPAEMGPAD 239
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATV-VVITHRPSLLAAV-DKLLVLRDGRVQAFGPRD 551
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-231 |
4.66e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 115.23 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQR-RQLRRDVQMVFQNPYASLNP 106
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDiKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 RQKIGDQLAEPLliNTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:PRK13649 101 ETVLKDVAFGPQ--NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTI-VLVTHLMDDVANYADFVYVLEKGK 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
32-225 |
5.71e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.96 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 32 GVSFELEAGKTLAVVGESGCGKSTLARALTLIEEP---TSGSLKIAGQEVKGASKDQRRqlrrdVQMVFQNPYasLNPRQ 108
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-----IGILFQDDL--LFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAepLLINTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDvsi 188
Cdd:COG4136 92 SVGENLA--FALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD--- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599702 189 qaqvlnlfMDLQQQFRtAYVF---ISHNLAV--VRHVADDVL 225
Cdd:COG4136 166 --------AALRAQFR-EFVFeqiRQRGIPAllVTHDEEDAP 198
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-244 |
1.13e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 114.72 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARaLT---LIEEptSGSLKIAGQEVKGASKDQR--RQLRRDVQMVFQNP 100
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQ-LTnglIISE--TGQTIVGDYAIPANLKKIKevKRLRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YASLNPRQKIGDQLAEPllINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PRK13645 100 EYQLFQETIEKDIAFGP--VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-243 |
1.17e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 114.45 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQR-RQLRRDVQMVFQNPYASLNP 106
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEiKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 RQKIGDQLAEPLliNTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:PRK13643 100 ETVLKDVAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 187 SIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMG-PADKLYE 243
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTV-VLVTHLMDDVADYADYVYLLEKGHIISCGtPSDVFQE 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-231 |
1.40e-29 |
|
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: 111.37 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHyevsrglfkghaqvRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:cd03215 2 EPVLEVRGLSVK--------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRqlRRDVQMVfqnpyaslnP--RQKIGDQLAEPLLINTALSReerrekvqqmmrqvglrpehyqryphMFSGGQR 159
Cdd:cd03215 68 SPRDAI--RAGIAYV---------PedRKREGLVLDLSVAENIALSS--------------------------LLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-231 |
1.43e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 113.23 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLkIAGQEVKGAS 82
Cdd:PRK11247 11 TPLLLNAVSKRY--------GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDqrrqlrrDVQMVFQNpyASLNPRQKIGDqlaeplliNTALS-REERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQR 161
Cdd:PRK11247 80 RE-------DTRLMFQD--ARLLPWKKVID--------NVGLGlKGQWRDAALQALAAVGL-ADRANEWPAALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 162 IALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-231 |
1.48e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.28 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 10 LTRHYEVSRGLFKGHaqvRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQL 89
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 90 RRDVQMVFQNPYASLNprQKIGDQLAEPLLINTAlSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMM 169
Cdd:PRK10908 78 RRQIGMIFQDHHLLMD--RTVYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 170 LQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTV-LMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-227 |
1.77e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.64 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEvkgaSKDQRR--QLRRDVQMVFQNPyaslnP 106
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDEENlwDIRNKAGMVFQNP-----D 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 RQKIGDQLAEPLLI---NTALSREERREKVQQMMRQVGLrpEHYQRY-PHMFSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:PRK13633 96 NQIVATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGM--YEYRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 183 ALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVM 227
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-227 |
4.08e-29 |
|
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: 116.62 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNPYAslnprq 108
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQIAWVPQHPFL------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kigdqLAEPLLINTALSREE-RREKVQQMMRQVGL------RPEHYQR----YPHMFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:TIGR02857 408 -----FAGTIAENIRLARPDaSDAEIREALERAGLdefvaaLPQGLDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599702 178 DEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVrHVADDVLVM 227
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQG-RTV-LLVTHRLALA-ALADRIVVL 529
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-241 |
5.43e-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: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRrqLRRDVQMVF 97
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNP--YASLNPRQKIgdQLAEpllinTALSREERREKVQQMmrqVGLRPEHYQRYPHM---FSGGQRQRIALARAMMLQP 172
Cdd:cd03224 82 EGRriFPELTVEENL--LLGA-----YARRRAKRKARLERV---YELFPRLKERRKQLagtLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 173 KVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-241 |
1.01e-28 |
|
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: 116.21 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrRQLRRDVQMVFQNPyaslnpr 107
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDV---QAVRRQLGVVLQNG------- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QKIGDQLAEPLLINTALSREErrekVQQMMRQVGLRpEHYQRYPhM------------FSGGQRQRIALARAMMLQPKVL 175
Cdd:TIGR03797 537 RLMSGSIFENIAGGAPLTLDE----AWEAARMAGLA-EDIRAMP-MgmhtvisegggtLSGGQRQRLLIARALVRKPRIL 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 176 VADEPTSALDVSIQAQVLNLFmdlqQQFRTAYVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:TIGR03797 611 LFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-261 |
1.05e-28 |
|
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: 113.27 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQL-RRDVQMVFQNpyASLNPRQKIG 111
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQE--ARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 112 DQLaeplliNTALSR---EERREKVQQMMRQVGLRPeHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:COG4148 96 GNL------LYGRKRaprAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 189 QAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP-LHPYTR-----ALLSATPAIH 261
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPdLLPLAGgeeagSVLEATVAAH 247
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-241 |
1.63e-28 |
|
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: 109.52 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEVSrglfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgasKD 84
Cdd:cd03263 1 LQIRNLTKTYKKG--------TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNP--YASLNPRQKIgdQLAEPLlinTALSREERREKVQQMMRQVGLRPeHYQRYPHMFSGGQRQRI 162
Cdd:cd03263 69 DRKAARQSLGYCPQFDalFDELTVREHL--RFYARL---KGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG-RSI-ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-245 |
1.87e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.82 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQ---EVKGAskdqrrqlRRDVQ 94
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA--------ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 95 MVFQNpYAsLNPRQKIGDQLAEPLLINTAlSREERREKVQQMMRQVGLrpEHY-QRYPHMFSGGQRQRIALARAMMLQPK 173
Cdd:PRK11000 79 MVFQS-YA-LYPHLSVAENMSFGLKLAGA-KKEEINQRVNQVAEVLQL--AHLlDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 174 VLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
2.98e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLtrHYEVSRGlfkghaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:PRK13636 3 DYILKVEEL--NYNYSDG-------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRrQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLliNTALSREERREKVQQMMRQVGLrpEHYQRYP-HMFSGGQRQ 160
Cdd:PRK13636 74 RKGLM-KLRESVGMVFQDPDNQLFSASVYQDVSFGAV--NLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
29-227 |
4.50e-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: 108.63 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKI----AGQEVKGASKDQRRQLRR-DVQMVFQnpYAS 103
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVrhegAWVDLAQASPREVLEVRRkTIGYVSQ--FLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 104 LNPRQKIGDQLAEPLLINtALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSA 183
Cdd:TIGR02324 101 VIPRVSALEVVAEPLLER-GVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599702 184 LDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:TIGR02324 180 LDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-227 |
4.50e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDqrrqlrRDVqmVFQN----PYAS 103
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE------RGV--VFQNegllPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 104 LNPRQKIGDQLAepllintALSREERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSA 183
Cdd:PRK11248 87 VQDNVAFGLQLA-------GVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599702 184 LDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-242 |
7.22e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.41 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEvsrglfkGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkg 80
Cdd:PRK13642 1 MNKILEVENLVFKYE-------KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 aSKDQRRQLRRDVQMVFQNPyaslnPRQKIGDQLAEPL---LINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGG 157
Cdd:PRK13642 72 -TAENVWNLRRKIGMVFQNP-----DNQFVGATVEDDVafgMENQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 158 QRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGRPAEMGP 237
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA 223
|
....*
gi 15599702 238 ADKLY 242
Cdd:PRK13642 224 PSELF 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-213 |
1.92e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.79 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHyevsrgLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:PRK10584 4 ENIVEVHHLKKS------VGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRQLR-RDVQMVFQN--PYASLNPRQKIgdQLaePLLINTALSREERrEKVQQMMRQVGLrPEHYQRYPHMFSGGQ 158
Cdd:PRK10584 78 DEEARAKLRaKHVGFVFQSfmLIPTLNALENV--EL--PALLRGESSRQSR-NGAKALLEQLGL-GKRLDHLPAQLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 159 RQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHN 213
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-231 |
5.53e-27 |
|
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: 105.06 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 19 GLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDvqmvfq 98
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 99 npyASLNPRQKIGDQlaeplLINTA----LSREERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKV 174
Cdd:cd03269 79 ---RGLYPKMKVIDQ-----LVYLAqlkgLKKEEARRRIDEWLERLELSEYANKRVEEL-SKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTV-ILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-236 |
7.18e-27 |
|
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: 110.68 E-value: 7.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaskdqrrqlrRDVQMvfqnpyASLnpRQK 109
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI------------RDVTQ------ASL--RAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IG----------DQLAEplliNTALSREE-RREKVQQMMRQVGLR------PEHYQRyphM-------FSGGQRQRIALA 165
Cdd:COG5265 434 IGivpqdtvlfnDTIAY----NIAYGRPDaSEEEVEAAARAAQIHdfieslPDGYDT---RvgerglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 166 RAMMLQPKVLVADEPTSALDV----SIQAQvlnlfmdLQQ--QFRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMG 236
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSrterAIQAA-------LREvaRGRTTLV-IAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-241 |
1.08e-26 |
|
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: 105.26 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNpyaSLNPRQ 108
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQVGVVLQE---NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAeplLINTALSREE-----RREKVQQMMRQVglrPEHYQRYPHM----FSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:cd03252 91 SIRDNIA---LADPGMSMERvieaaKLAGAHDFISEL---PEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 180 PTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAG-RTV-IIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
30-244 |
1.11e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.15 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIE--EPTSGSLKIAGQEVKGASKDQRrqLRRDVQMVFQNP------- 100
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDER--ARAGIFLAFQYPveipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 -----YASLNPRQKigdqlaepllinTALSREERREKVQQMMRQVGLRPEHYQRYPHM-FSGGQRQRIALARAMMLQPKV 174
Cdd:COG0396 94 vsnflRTALNARRG------------EELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 175 LVADEPTSALDV-SIQAqVLNLFMDLQQQfRTAYVFISHNLAVVRHV-ADDVLVMYLGRPAEMGP---ADKLYEN 244
Cdd:COG0396 162 AILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGkelALELEEE 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-245 |
1.29e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.84 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrQLRRDVQMVFQNPYAslnprQ 108
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ--GIRKLVGIVFQNPET-----Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAEPLLI---NTALSREERREKVQQMMRQVGLRPEHYqRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK13644 90 FVGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTaYVFISHNLAVVrHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKT-IVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-239 |
1.48e-26 |
|
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: 109.36 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQ----LRRDVQMvFQNP 100
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKhigyLPQDVEL-FPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YAslnprQKIG--DQLAEPllintalsreerrEKVQQMMRQVGLRpEHYQRYPHMF-----------SGGQRQRIALARA 167
Cdd:TIGR01842 408 VA-----ENIArfGENADP-------------EKIIEAAKLAGVH-ELILRLPDGYdtvigpggatlSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 168 MMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVrHVADDVLVMYLGRPAEMGPAD 239
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERD 538
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-251 |
1.54e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEpTSGSLKIAGQ-EVKGASKDQRR----QLRRDVQMVFQNP-- 100
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFFNQNIYERRvnlnRLRRQVSMVHPKPnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 -----YASL---------NPRQKIGDqlaeplLINTALSREERREKVQQMMRQVGLRpehyqryphmFSGGQRQRIALAR 166
Cdd:PRK14258 100 fpmsvYDNVaygvkivgwRPKLEIDD------IVESALKDADLWDEIKHKIHKSALD----------LSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 167 AMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMY-----LGRPAEMGPADKL 241
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKI 243
|
250
....*....|
gi 15599702 242 YENPLHPYTR 251
Cdd:PRK14258 244 FNSPHDSRTR 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-250 |
1.71e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.24 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALT----LIEEPT-SGSLKIAG 75
Cdd:PRK14239 2 TEPILQVSDLSVYY----------NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndLNPEVTiTGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 76 QEVKGASKDQRrQLRRDVQMVFQNPyaslNP-RQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYpH-- 152
Cdd:PRK14239 72 HNIYSPRTDTV-DLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-Hds 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 153 --MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVfiSHNLAVVRHVADDVLVMYLG 230
Cdd:PRK14239 146 alGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|
gi 15599702 231 RPAEMGPADKLYENPLHPYT 250
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKET 243
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-236 |
1.83e-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: 102.78 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfkgHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKd 84
Cdd:cd03247 1 LSINNVSFSYP--------EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 qrrQLRRDVQMVFQNPYaslnprqkigdqlaeplLINTALsreerrekvqqmMRQVGLRpehyqryphmFSGGQRQRIAL 164
Cdd:cd03247 72 ---ALSSLISVLNQRPY-----------------LFDTTL------------RNNLGRR----------FSGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHVaDDVLVMYLGRPAEMG 236
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTL-IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-249 |
2.33e-26 |
|
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: 104.14 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:TIGR03410 1 LEVSNLNVYY--------GQSHI--LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRrqLRRDVQMVFQNpyaslnprQKIGDQL--AEPLLinTALSREERREKvqqmmrqvGLRPEHYQRYPHMF-------- 154
Cdd:TIGR03410 71 ER--ARAGIAYVPQG--------REIFPRLtvEENLL--TGLAALPRRSR--------KIPDEIYELFPVLKemlgrrgg 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 --SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRP 232
Cdd:TIGR03410 131 dlSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
250
....*....|....*..
gi 15599702 233 AEMGPADKLYENPLHPY 249
Cdd:TIGR03410 211 VASGAGDELDEDKVRRY 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-265 |
2.34e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTrhyeVSRGlfkgHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS 82
Cdd:PRK13548 1 AMLEARNLS----VRLG----GRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRRQLRrdvqmvfqnpyASLnpRQKIgdQLAEPLLINT---------ALSREERREKVQQMMRQVGLrpEHY-QRYPH 152
Cdd:PRK13548 71 PAELARRR-----------AVL--PQHS--SLSFPFTVEEvvamgraphGLSRAEDDALVAAALAQVDL--AHLaGRDYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 153 MFSGGQRQRIALARAMM------LQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLV 226
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15599702 227 MYLGRPAEMG-PADKLYENPLhpytRALLSATPAIHPDPT 265
Cdd:PRK13548 214 LHQGRLVADGtPAEVLTPETL----RRVYGADVLVQPHPE 249
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-239 |
2.67e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTrhyeVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:COG4559 2 LEAENLS----VRLG------GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRrdvqmvfqnpyASLnpRQKIgdQLAEPL---------LINTALSREERREKVQQMMRQVGLrpEHY--QRYPHM 153
Cdd:COG4559 72 ELARRR-----------AVL--PQHS--SLAFPFtveevvalgRAPHGSSAAQDRQIVREALALVGL--AHLagRSYQTL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 154 fSGGQRQRIALARAM-------MLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLV 226
Cdd:COG4559 135 -SGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILL 212
|
250
....*....|...
gi 15599702 227 MYLGRPAEMGPAD 239
Cdd:COG4559 213 LHQGRLVAQGTPE 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-231 |
3.29e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPYASLNPR 107
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDPDDQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QKIGDQLAEPllINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVS 187
Cdd:PRK13647 96 TVWDDVAFGP--VNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599702 188 IQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTV-IVATHDVDLAAEWADQVIVLKEGR 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-231 |
4.52e-26 |
|
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: 102.66 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTlAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskDQRRQLRRDVQMVFQNPyaSLNPR 107
Cdd:cd03264 14 RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRRRIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QKIGDQLAEPLLINTALSREERREkVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVS 187
Cdd:cd03264 87 FTVREFLDYIAWLKGIPSKEVKAR-VDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 188 IQAQVLNLFMDLQQqfrTAYVFIS-HNLAVVRHVADDVLVMYLGR 231
Cdd:cd03264 165 ERIRFRNLLSELGE---DRIVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-245 |
4.66e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.52 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:COG0410 1 MPMLEVENLHAGY--------GGIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRQL--------RRdvqmVFQN---------PYASLNPRQKIGDQLAE-----PLLintalsrEERRekvqqmmRQ 139
Cdd:COG0410 71 PPHRIARLgigyvpegRR----IFPSltveenlllGAYARRDRAEVRADLERvyelfPRL-------KERR-------RQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 140 VG--LrpehyqryphmfSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVV 217
Cdd:COG0410 133 RAgtL------------SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFA 199
|
250 260
....*....|....*....|....*...
gi 15599702 218 RHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:COG0410 200 LEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-245 |
9.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 9.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLAR---ALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPyasln 105
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKlinGLLLPDDNPNSKITVDGITL---TAKTVWDIREKVGIVFQNP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIGDQLAEPL---LINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:PRK13640 94 DNQFVGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 183 ALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-236 |
1.25e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.03 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskDQR-RQLRRDVQMVFQNPYAslnpr 107
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR----DYTlASLRNQVALVSQNVHL----- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 qkIGDQLAEplliNTALSREER--REKVQQMMRqVGLRPEHYQRYPH-----------MFSGGQRQRIALARAMMLQPKV 174
Cdd:PRK11176 429 --FNDTIAN----NIAYARTEQysREQIEEAAR-MAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 175 LVADEPTSALDV----SIQAQvlnlfMDLQQQFRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMG 236
Cdd:PRK11176 502 LILDEATSALDTeserAIQAA-----LDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
29-247 |
1.42e-25 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 106.71 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNP---YASLN 105
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLD---PAELRARMALVPQDPvlfAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIGDQLAEPLLINTALSREERREKVQQMmrqvglrPEHYQRY----PHMFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:TIGR02204 432 ENIRYGRPDATDEEVEAAARAAHAHEFISAL-------PEGYDTYlgerGVTLSGGQRQRIAIARAILKDAPILLLDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 182 SALDvSIQAQVLNLFMDLQQQFRTAYVfISHNLAVVRHvADDVLVMYLGRPAEMGPADKLY-ENPLH 247
Cdd:TIGR02204 505 SALD-AESEQLVQQALETLMKGRTTLI-IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIaKGGLY 568
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-245 |
3.00e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPYA-SLNPRQ 108
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEPVLfSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAE-PLLINTALSREERREKVQQMMRQ-----VGlrpEHYQRyphmFSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:TIGR00958 574 NIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNgydteVG---EKGSQ----LSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 183 ALDVSIQAQVLNlfmDLQQQFRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:TIGR00958 647 ALDAECEQLLQE---SRSRASRTV-LLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-241 |
3.88e-25 |
|
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: 105.57 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 11 TRHYEVSRGLFK--------GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS 82
Cdd:TIGR02203 321 TRAIERARGDVEfrnvtfryPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 kdqRRQLRRDVQMVFQNPYAslnprqkIGDQLAEplliNTALSREER--REKVQQMMRQVGLRpEHYQRYPHMF------ 154
Cdd:TIGR02203 401 ---LASLRRQVALVSQDVVL-------FNDTIAN----NIAYGRTEQadRAEIERALAAAYAQ-DFVDKLPLGLdtpige 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 -----SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVfISHNLAVVRHvADDVLVMYL 229
Cdd:TIGR02203 466 ngvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLV-IAHRLSTIEK-ADRIVVMDD 542
|
250
....*....|..
gi 15599702 230 GRPAEMGPADKL 241
Cdd:TIGR02203 543 GRIVERGTHNEL 554
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-250 |
3.98e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.10 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRR---QLRRDVQMVFQN 99
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 100 PyaslNP-RQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRY---PHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:PRK14271 110 P----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQqfRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYT 250
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-231 |
4.29e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG 80
Cdd:COG3845 2 MPPALELRGITKRF----------GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 AS-KDQRrqlRRDVQMVFQNPyaslnprqkigdQLAEPL--LINTALSREER----------REKVQQMMRQVGLR--PE 145
Cdd:COG3845 72 RSpRDAI---ALGIGMVHQHF------------MLVPNLtvAENIVLGLEPTkggrldrkaaRARIRELSERYGLDvdPD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 146 hyqRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDvsiQAQVLNLFMDLqQQFR---TAYVFISHNLAVVRHVAD 222
Cdd:COG3845 137 ---AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT---PQEADELFEIL-RRLAaegKSIIFITHKLREVMAIAD 209
|
....*....
gi 15599702 223 DVLVMYLGR 231
Cdd:COG3845 210 RVTVLRRGK 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-231 |
4.31e-25 |
|
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: 99.98 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRqlrrdvqmvf 97
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 qnpYASLNPRQKIGDQL-AEPLLINTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLV 176
Cdd:cd03268 74 ---IGALIEAPGFYPNLtARENLRLLARLLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 177 ADEPTSALDVSIQAQVLNLFMDLQQQFRTayVFI-SHNLAVVRHVADDVLVMYLGR 231
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGIT--VLIsSHLLSEIQKVADRIGIINKGK 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-264 |
8.22e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrRQLRRDVQMVFQNPYASL 104
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 NPRqkiGDQLAE----PLLINTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PRK09536 91 EFD---VRQVVEmgrtPHRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQFRTAYVFIsHNLAVVRHVADDVLVMYLGRPAEMG-PADKLYENPLhpytRALLSATPA 259
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGpPADVLTADTL----RAAFDARTA 241
|
....*
gi 15599702 260 IHPDP 264
Cdd:PRK09536 242 VGTDP 246
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-214 |
8.44e-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: 104.36 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:TIGR02868 335 LELRDLSAGYP---------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QrrqLRRDVQMVFQNPYAslnprqkigdqLAEPLLINTALSREE-RREKVQQMMRQVGLRpEHYQRYPH----------- 152
Cdd:TIGR02868 406 E---VRRRVSVCAQDAHL-----------FDTTVRENLRLARPDaTDEELWAALERVGLA-DWLRALPDgldtvlgegga 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTayVFISHNL 214
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHHL 530
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-298 |
1.33e-24 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 94.39 E-value: 1.33e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 234 EMGPADKLYENPLHPYTRALLSATPAIHPdPTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERC 298
Cdd:pfam08352 2 EEGPTDDILENPLHPYTRALLNSVPRLDP-PKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-240 |
1.50e-24 |
|
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: 104.18 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 12 RHYEVSRGLFKGHAQVR------------ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVk 79
Cdd:TIGR03375 451 GTRFLHRPRLQGEIEFRnvsfaypgqetpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 gaskdqrRQ-----LRRDVQMVFQNP---YASLnpRQKIgdQLAEPLLINTALSREERREKVQQMMRQvglrpeHYQRYP 151
Cdd:TIGR03375 530 -------RQidpadLRRNIGYVPQDPrlfYGTL--RDNI--ALGAPYADDEEILRAAELAGVTEFVRR------HPDGLD 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 152 HM-------FSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQvlnlFMDLQQQF---RTaYVFISHNLAVVRHVa 221
Cdd:TIGR03375 593 MQigergrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER----FKDRLKRWlagKT-LVLVTHRTSLLDLV- 666
|
250
....*....|....*....
gi 15599702 222 DDVLVMYLGRPAEMGPADK 240
Cdd:TIGR03375 667 DRIIVMDNGRIVADGPKDQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-237 |
5.30e-24 |
|
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: 97.56 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPY------- 101
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ASLNPRQKIGDqlAEpllINTALSREERREKVQQMMRQVGLRPEHYQRYphmFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:cd03244 96 SNLDPFGEYSD--EE---LWQALERVGLKEFVESLPGGLDTVVEEGGEN---LSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 182 SALDVSIQAQVLNLfmdLQQQFRTAYVF-ISHNLAVVRHvADDVLVMYLGRPAEMGP 237
Cdd:cd03244 168 ASVDPETDALIQKT---IREAFKDCTVLtIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-236 |
6.35e-24 |
|
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: 96.47 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTrhYEVSRGLFKGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALT--LIEEPTSGSLKIAGQEVKga 81
Cdd:cd03213 3 TLSFRNLT--VTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 skdqRRQLRRDVQMVFQNP--YASLNPRqkigdqlaEPLLINTALSreerrekvqqmmrqvGLrpehyqryphmfSGGQR 159
Cdd:cd03213 77 ----KRSFRKIIGYVPQDDilHPTLTVR--------ETLMFAAKLR---------------GL------------SGGER 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-247 |
1.17e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEV------------SRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTS 68
Cdd:COG1134 1 MSSMIEVENVSKSYRLyhepsrslkellLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 69 GSLKIAGqevkgaskdqrrqlrR-----DVQMVFQNpyaSLNPRQKIgdqlaeplLINTAL---SREERREKVQQ----- 135
Cdd:COG1134 81 GRVEVNG---------------RvsallELGAGFHP---ELTGRENI--------YLNGRLlglSRKEIDEKFDEivefa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 136 -----MMRQVGlrpeHYqryphmfSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFI 210
Cdd:COG1134 135 elgdfIDQPVK----TY-------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTV-IFV 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15599702 211 SHNLAVVRHVADDVLVMYLGRPAEMGPAD---KLYENPLH 247
Cdd:COG1134 203 SHSMGAVRRLCDRAIWLEKGRLVMDGDPEeviAAYEALLA 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-264 |
1.35e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrRQLRRDVQMVFQ---- 98
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQhhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 99 --------------NPYASLNPRqkigdqlaepllintaLSREErREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIAL 164
Cdd:PRK11231 88 pegitvrelvaygrSPWLSLWGR----------------LSAED-NARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMG-PADKLYE 243
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTV-VTVLHDLNQASRYCDHLVVLANGHVMAQGtPEEVMTP 228
|
250 260
....*....|....*....|.
gi 15599702 244 NPLhpytRALLSATPAIHPDP 264
Cdd:PRK11231 229 GLL----RTVFDVEAEIHPEP 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-255 |
1.75e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYevsrGLFkghaqvRALNGVSFELEAGKTLAVVGESGCGKSTLARALT----LIEE-PTSGSLKIAGQ 76
Cdd:PRK14243 8 ETVLRTENLNVYY----GSF------LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlndLIPGfRVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 77 EVKGASKDQRrQLRRDVQMVFQNPY-------------ASLNPRQKIGDQLAEPLLINTALSREerrekVQQMMRQVGLR 143
Cdd:PRK14243 78 NLYAPDVDPV-EVRRRIGMVFQKPNpfpksiydniaygARINGYKGDMDELVERSLRQAALWDE-----VKDKLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 144 pehyqryphmFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFrtAYVFISHNLAVVRHVADD 223
Cdd:PRK14243 152 ----------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599702 224 VLVM---------YLGRPAEMGPADKLYENPLHPYTRALLS 255
Cdd:PRK14243 220 TAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-226 |
3.75e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYEvSRGLFKGhaqvralngVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIaGQEVKGAS 82
Cdd:COG0488 314 KVLELEGLSKSYG-DKTLLDD---------LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRRqlrrdvqmvfqnpyASLNPRQKIGDQLAEpllintaLSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRI 162
Cdd:COG0488 383 FDQHQ--------------EELDPDKTVLDELRD-------GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDV-SIQAqvLNlfmDLQQQFRTAYVFISHNLAVVRHVADDVLV 226
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIeTLEA--LE---EALDDFPGTVLLVSHDRYFLDRVATRILE 501
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-214 |
5.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.69 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEVsrglfKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:PRK13651 3 IKVKNIVKIFNK-----KLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QR---------------------RQLRRDVQMVFQnpYASLnprqkigdQLAEPLL--------INTALSREERREKVQQ 135
Cdd:PRK13651 78 KEkekvleklviqktrfkkikkiKEIRRRVGVVFQ--FAEY--------QLFEQTIekdiifgpVSMGVSKEEAKKRAAK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 136 MMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNL 214
Cdd:PRK13651 148 YIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTI-ILVTHDL 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-231 |
1.42e-22 |
|
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: 93.94 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 8 RDLTRHYEVS----------RGLFKG-HAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGq 76
Cdd:cd03267 4 SNLSKSYRVYskepgligslKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 77 EVKGaskDQRRQLRRDVQMVFQnpyaslnprQKigDQL------AEPLLINTALSR------EERREKVQQMMRqvgLRP 144
Cdd:cd03267 83 LVPW---KRRKKFLRRIGVVFG---------QK--TQLwwdlpvIDSFYLLAAIYDlpparfKKRLDELSELLD---LEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 145 EHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDV 224
Cdd:cd03267 146 LLDTPVRQL-SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRV 224
|
....*..
gi 15599702 225 LVMYLGR 231
Cdd:cd03267 225 LVIDKGR 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-236 |
1.53e-22 |
|
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: 93.25 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPY------ 101
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPTlfsgti 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 -ASLNPRQKIGDQlaeplLINTALSREERREKvqqmmrqvglrpehyqryphmFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:cd03369 99 rSNLDPFDEYSDE-----EIYGALRVSEGGLN---------------------LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 181 TSALDVS----IQAQVLNLFMDlqqqfrTAYVFISHNLavvRHVA--DDVLVMYLGRPAEMG 236
Cdd:cd03369 153 TASIDYAtdalIQKTIREEFTN------STILTIAHRL---RTIIdyDKILVMDAGEVKEYD 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-241 |
1.82e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.43 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLrrDVQMVF 97
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--GIYLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNP--YASLNPRQKIGDQLAEPllintalsrEERREKVQQMMRQVGLrpehyQRYPHMFSG----GQRQRIALARAMMLQ 171
Cdd:PRK15439 93 QEPllFPNLSVKENILFGLPKR---------QASMQKMKQLLAALGC-----QLDLDSSAGslevADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 172 PKVLVADEPTSALdvsIQAQVLNLFMDLQ--QQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:PRK15439 159 SRILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-231 |
2.24e-22 |
|
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: 93.30 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGqevKGASKDQRRQLRRDVQMVFQNPY---ASLNP 106
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYEHKYLHSKVSLVGQEPVlfaRSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 RQKIGDQLAEPLLINTALSREERREKVQQMmrQVGLRPEHYQRyPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:cd03248 107 NIAYGLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 187 SIQAQVLNLFMDLQQqfRTAYVFISHNLAVVRHvADDVLVMYLGR 231
Cdd:cd03248 184 ESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-214 |
2.60e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.00 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQR-RQLRRdvqmVFQNPYASL 104
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaKYIGR----VFQDPMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 NPRQKIgdqlAEPLLIntALSR-----------EERREKVQQMMRQVGLRPEHyqrypHM------FSGGQRQRIALARA 167
Cdd:COG1101 94 APSMTI----EENLAL--AYRRgkrrglrrgltKKRRELFRELLATLGLGLEN-----RLdtkvglLSGGQRQALSLLMA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599702 168 MMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNL 214
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-231 |
2.85e-22 |
|
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: 92.65 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNP---Y 101
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRNIGYVPQDVtlfY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ASLnpRQKIgdQLAEPLLINTALSREERREKVQQMMR--------QVGLRPEHyqryphmFSGGQRQRIALARAMMLQPK 173
Cdd:cd03245 92 GTL--RDNI--TLGAPLADDERILRAAELAGVTDFVNkhpngldlQIGERGRG-------LSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 174 VLVADEPTSALDVSIQAQvlnLFMDLQQQFRT-AYVFISHNLAVVRhVADDVLVMYLGR 231
Cdd:cd03245 161 ILLLDEPTSAMDMNSEER---LKERLRQLLGDkTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-241 |
4.94e-22 |
|
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: 96.73 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPYAS----- 103
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFINYLPQEPYIFsgsil 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 104 ----LNPRQKIGDQLaepllINTALSREERREKVQQMmrQVGLRPEhYQRYPHMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:TIGR01193 566 enllLGAKENVSQDE-----IWAACEIAEIKDDIENM--PLGYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 180 PTSALDVSIQAQVLNLFMDLQQQfrtAYVFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKL 241
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDEL 695
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-236 |
6.94e-22 |
|
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: 91.83 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEVSRGLF------------KGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLK 72
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 73 IAGQEVkgaskdqrrqLRRDVQMVFQNpyaSLNPRQKIgdqlaeplLINTAL---SREERREKVQ--QMMRQVGlrpEHY 147
Cdd:cd03220 81 VRGRVS----------SLLGLGGGFNP---ELTGRENI--------YLNGRLlglSRKEIDEKIDeiIEFSELG---DFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 148 QRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVM 227
Cdd:cd03220 137 DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTV-ILVSHDPSSIKRLCDRALVL 215
|
....*....
gi 15599702 228 YLGRPAEMG 236
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-245 |
7.38e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 7.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQ--RRQLRRDVQMV--FQNPYASL 104
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMGVVRTFQHVrlFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 N----PRQKIGDQLAEPLLINTALSREERR--EKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVAD 178
Cdd:PRK11300 100 NllvaQHQQLKTGLFSGLLKTPAFRRAESEalDRAATWLERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 179 EPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-231 |
8.15e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.48 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTrhyevsrglFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:COG3845 255 EVVLEVENLS---------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRQLRrdvqmvfqnpyASLNP--RQK---IGDQ-LAEPLLINTA----------LSREERREKVQQMMRQVGLRPE 145
Cdd:COG3845 326 SPRERRRLG-----------VAYIPedRLGrglVPDMsVAENLILGRYrrppfsrggfLDRKAIRAFAEELIEEFDVRTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 146 HYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVL 225
Cdd:COG3845 395 GPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIA 473
|
....*.
gi 15599702 226 VMYLGR 231
Cdd:COG3845 474 VMYEGR 479
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
30-241 |
8.31e-22 |
|
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: 95.96 E-value: 8.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNpyaSLNPRQK 109
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW---LRRQMGVVLQE---NVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAeplLINTALSREErrekVQQMMRQVGLRpEHYQRYPHMF-----------SGGQRQRIALARAMMLQPKVLVAD 178
Cdd:TIGR01846 547 IRDNIA---LCNPGAPFEH----VIHAAKLAGAH-DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 179 EPTSALDVSIQAQVLNlFMDLQQQFRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:TIGR01846 619 EATSALDYESEALIMR-NMREICRGRTV-IIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-227 |
8.37e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQlrrDVQMVFQNPyaSLNPrQK 109
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSYCAQTP--TLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLLIntalsREER--REKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVS 187
Cdd:PRK10247 97 VYDNLIFPWQI-----RNQQpdPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599702 188 IQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvADDVLVM 227
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-241 |
8.83e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.68 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALtLIEEPTSGSLKIAGQEVKGASKDQ-RRQLrrdvQMVFQNP---YASLnpRQ 108
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNAL-LGFLPYQGSLKINGIELRELDPESwRKHL----SWVGQNPqlpHGTL--RD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KI--GDQLAEPLLINTALSREERREKVQQMMR----QVGlrpEHYQRyphmFSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:PRK11174 442 NVllGNPDASDEQLQQALENAWVSEFLPLLPQgldtPIG---DQAAG----LSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 183 ALDVSIQAQVLNLFMDLQQQfrTAYVFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKL 241
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-212 |
1.02e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLkiagqevkgaskdqrrQLRRDVQMVF--QNPY---ASL 104
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------------ARPAGARVLFlpQRPYlplGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 npRqkigDQLAEPLLiNTALSREErrekVQQMMRQVGL-----RPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:COG4178 443 --R----EALLYPAT-AEAFSDAE----LREALEAVGLghlaeRLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|...
gi 15599702 180 PTSALDVSIQAQVLNLFmdLQQQFRTAYVFISH 212
Cdd:COG4178 512 ATSALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-236 |
1.26e-21 |
|
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: 90.89 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEVSRGLFKghaqvrALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskD 84
Cdd:cd03266 2 ITADALTKRFRDVKKTVQ------AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQMVFQNP--YASLNPRQKIG--DQLaepllinTALSREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQ 160
Cdd:cd03266 72 EPAEARRRLGFVSDSTglYDRLTARENLEyfAGL-------YGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 161 RIALARAMMLQPKVLVADEPTSALDVsIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-247 |
1.28e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEVS----------RGLFKG-HAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLK 72
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalKGLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 73 IAGQE-VKgaskdQRRQLRRDVQMVF-QnpyaslnpRQkigdQL------AEPLLINTA---LSREERREKVQQMMRQVG 141
Cdd:COG4586 81 VLGYVpFK-----RRKEFARRIGVVFgQ--------RS----QLwwdlpaIDSFRLLKAiyrIPDAEYKKRLDELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 142 LRPEHYQ--RyphMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRH 219
Cdd:COG4586 144 LGELLDTpvR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEA 220
|
250 260
....*....|....*....|....*...
gi 15599702 220 VADDVLVMYLGRpaemgpadKLYENPLH 247
Cdd:COG4586 221 LCDRVIVIDHGR--------IIYDGSLE 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-236 |
3.60e-21 |
|
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: 90.02 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 27 VRALNGVSFELEAGKTLAVVGESGCGKSTLARALT-LIEEP--TSGSLKIAGQEVKgaskdqRRQLRRDVQMVFQNPY-- 101
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgRVEGGgtTSGQILFNGQPRK------PDQFQKCVAYVRQDDIll 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ASLNPRQKIgdqLAEPLLINTALSREERREKV--QQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:cd03234 94 PGLTVRETL---TYTAILRLPRKSSDAIRKKRveDVLLRDLALTRIGGNLVKGI-SGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 180 PTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
30-222 |
6.22e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAG--------QEVKGaskDQRRQLRRDVQMVFQNPY 101
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQEPPL---DDDLTVLDTVLDGDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ASLNPRQKIGDQLAEPLLINTALSR-EERRE---------KVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQ 171
Cdd:COG0488 91 ALEAELEELEAKLAEPDEDLERLAElQEEFEalggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 172 PKVLVADEPTSALDV-SIQ--AQVLnlfmdlqQQFRTAYVFISHN---L-AVVRHVAD 222
Cdd:COG0488 171 PDLLLLDEPTNHLDLeSIEwlEEFL-------KNYPGTVLVVSHDryfLdRVATRILE 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-244 |
6.92e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHyevsrglFKGhaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEePT---SGSLKIAGQE 77
Cdd:PRK13549 2 MEYLLEMKNITKT-------FGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 78 VKGAS-KDQRRQ----LRRDVQMVfqnPYASLNPRQKIGDQLAEPLLINTAlsreERREKVQQMMRQVGLRPEHYQRYPH 152
Cdd:PRK13549 71 LQASNiRDTERAgiaiIHQELALV---KELSVLENIFLGNEITPGGIMDYD----AMYLRAQKLLAQLKLDINPATPVGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 153 mFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLGRP 232
Cdd:PRK13549 144 -LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
250
....*....|..
gi 15599702 233 AEMGPADKLYEN 244
Cdd:PRK13549 222 IGTRPAAGMTED 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-241 |
1.33e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSK 83
Cdd:COG4152 1 MLELKGLTKRF----------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQL------RrdvqmvfqnpyaSLNPRQKIGDQL---AEpLlinTALSREERREKVQQMMRQVGLrPEHYQRYPHMF 154
Cdd:COG4152 68 EDRRRIgylpeeR------------GLYPKMKVGEQLvylAR-L---KGLSKAEAKRRADEWLERLGL-GDRANKKVEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMMLQPKVLVADEPTSALD-VSIqaqvlNLFMDLQQQFR---TAYVFISHNLAVVRHVADDVLVMYLG 230
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNV-----ELLKDVIRELAakgTTVIFSSHQMELVEELCDRIVIINKG 205
|
250
....*....|.
gi 15599702 231 RPAEMGPADKL 241
Cdd:COG4152 206 RKVLSGSVDEI 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-231 |
1.63e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRhyevsRGLFKGhaqvralngVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKga 81
Cdd:COG1129 254 EVVLEVEGLSV-----GGVVRD---------VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 skdqrrqlrrdvqmvFQNPYASLnpRQKIG----DQLAEPLLI------NTAL------------SREERREKVQQMMRQ 139
Cdd:COG1129 318 ---------------IRSPRDAI--RAGIAyvpeDRKGEGLVLdlsireNITLasldrlsrggllDRRRERALAEEYIKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 140 VGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRH 219
Cdd:COG1129 381 LRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLG 459
|
250
....*....|..
gi 15599702 220 VADDVLVMYLGR 231
Cdd:COG1129 460 LSDRILVMREGR 471
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-244 |
3.05e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.81 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLtrHYEVsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIE--EPTSGSLKIAGQEVKGAS 82
Cdd:cd03217 1 LEIKDL--HVSV--------GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRrqLRRDVQMVFQNPyaslnprqkigdqlaepllintalsreerrekvqqmMRQVGLRPEHYQRYPHM-FSGGQRQR 161
Cdd:cd03217 71 PEER--ARLGIFLAFQYP------------------------------------PEIPGVKNADFLRYVNEgFSGGEKKR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 162 IALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHV-ADDVLVMYLGRPAEMGP--- 237
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDkel 191
|
....*..
gi 15599702 238 ADKLYEN 244
Cdd:cd03217 192 ALEIEKK 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-227 |
3.21e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 19 GLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskdqrrqlRRDVQMVFQ 98
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN----------KLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 99 NPYASLNPRQKIGDQLA--EPLLINTALSRE----------ERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALAR 166
Cdd:PRK09700 80 LGIGIIYQELSVIDELTvlENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANL-SISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 167 AMMLQPKVLVADEPTSALdvsIQAQVLNLFMdLQQQFR---TAYVFISHNLAVVRHVADDVLVM 227
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFL-IMNQLRkegTAIVYISHKLAEIRRICDRYTVM 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
30-227 |
7.22e-20 |
|
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: 84.04 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKiagqevkgaskdqrrqlrrdvqmvfqnpyasLNPRQK 109
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------------------WGSTVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IG--DQLaepllintalsreerrekvqqmmrqvglrpehyqryphmfSGGQRQRIALARAMMLQPKVLVADEPTSALDV- 186
Cdd:cd03221 65 IGyfEQL----------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLe 104
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599702 187 SIQAqvLNLFMdlqQQFRTAYVFISHNLAVVRHVADDVLVM 227
Cdd:cd03221 105 SIEA--LEEAL---KEYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-270 |
8.37e-20 |
|
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: 89.50 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEE--PTSGSLKIAGQEVKGASKdqRRQLRRDVQM 95
Cdd:TIGR02633 5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNI--RDTERAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQN----PYASLNPRQKIGDQLAEPLLIntaLSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQ 171
Cdd:TIGR02633 83 IHQEltlvPELSVAENIFLGNEITLPGGR---MAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 172 PKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVV-------------RHVA---------DDVLVMYL 229
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVkavcdticvirdgQHVAtkdmstmseDDIITMMV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599702 230 GRpaEMgpaDKLYENPLHPYTRALLSATPAIHPDPTKPKIR 270
Cdd:TIGR02633 239 GR--EI---TSLYPHEPHEIGDVILEARNLTCWDVINPHRK 274
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-257 |
1.05e-19 |
|
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: 86.29 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTrhyeVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLaraLTLI---EEPTSG-SLKIAGQE 77
Cdd:COG1119 1 DPLLELRNVT----VRRG------GKTILDDISWTVKPGEHWAILGPNGAGKSTL---LSLItgdLPPTYGnDVRLFGER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 78 VKG------------ASKDQRRQLRRDV---QMVFQNPYASLNPRQKIGDqlaepllintalsreERREKVQQMMRQVGL 142
Cdd:COG1119 68 RGGedvwelrkriglVSPALQLRFPRDEtvlDVVLSGFFDSIGLYREPTD---------------EQRERARELLELLGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 143 rpEHY--QRYPHMfSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNL----AV 216
Cdd:COG1119 133 --AHLadRPFGTL-SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeeipPG 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599702 217 VRHvaddVLVMYLGRPAEMGPADKLyenplhpYTRALLSAT 257
Cdd:COG1119 210 ITH----VLLLKDGRVVAAGPKEEV-------LTSENLSEA 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-231 |
1.58e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNG-----VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRrqLRRDVQMVFQNp 100
Cdd:PRK15439 270 TVEDLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQR--LARGLVYLPED- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 yaslnpRQKIGDQLAEPLLINTA----------LSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMML 170
Cdd:PRK15439 347 ------RQSSGLYLDAPLAWNVCalthnrrgfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 171 QPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-241 |
1.98e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEP---TSGSLKIAGQEVkgaskdQRRQLRRDVQMVFQNpyaSLNp 106
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI------DAKEMRAISAYVQQD---DLF- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 rqkIGDQLAEPLLINTA-------LSREERREKVQQMMRQVGLRPEHYQR-----YPHMFSGGQRQRIALARAMMLQPKV 174
Cdd:TIGR00955 111 ---IPTLTVREHLMFQAhlrmprrVTKKEKRERVDEVLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-241 |
3.36e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQrrqLRRDVQMVFQNPYAslnprq 108
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQAISVVSQRVHL------ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kIGDQLAEPLLINTALSREErreKVQQMMRQVGL------------------RPehyqryphmFSGGQRQRIALARAMML 170
Cdd:PRK11160 426 -FSATLRDNLLLAAPNASDE---ALIEVLQQVGLeklleddkglnawlgeggRQ---------LSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 171 QPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAyVFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKL 241
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQN-KTV-LMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-231 |
5.92e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEvkgaskdqrrqlrrdvqMVF 97
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----------------MRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNPYASLNPRQKIGDQ---------LAEPLL----------INTALSREERREKVQQMmrQVGLRPEHYQRYphmFSGGQ 158
Cdd:PRK11288 71 ASTTAALAAGVAIIYQelhlvpemtVAENLYlgqlphkggiVNRRLLNYEAREQLEHL--GVDIDPDTPLKY---LSIGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 159 RQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-231 |
8.16e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgASKDQRRQLRRDVQMVFQNPYASLNpRQK 109
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQIF-YTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLLiNTALSREERREKVQQMMRQVGlrPEHYQRYP-HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:PRK13638 95 IDSDIAFSLR-NLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599702 189 QAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
35-235 |
8.77e-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: 83.36 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 35 FELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD-----QRRQLRRDVQMVFQnpYASLNPRQK 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHigyvpQRHEFAWDFPISVA--HTVMSGRTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLLINTAlsreerreKVQQMMRQVGLrpEHYQRYP-HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:TIGR03771 79 HIGWLRRPCVADFA--------AVRDALRRVGL--TELADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599702 189 QAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVL-----VMYLGRPAEM 235
Cdd:TIGR03771 149 QELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVllngrVIADGTPQQL 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-201 |
9.51e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.29 E-value: 9.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYEvsrglfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALT--LIEEPTSGS-LKIAGQE 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFN----------QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglITGDKSAGShIELLGRT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 78 VKGASKDQR--RQLRRDVQMVFQNpyASLNPRQKIGDQLAEPLLINTALSR-------EERREKVQQMMRQVGLRPEHYQ 148
Cdd:PRK09984 71 VQREGRLARdiRKSRANTGYIFQQ--FNLVNRLSVLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 149 RYPHMfSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQ 201
Cdd:PRK09984 149 RVSTL-SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQ 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
34-212 |
1.42e-18 |
|
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: 81.43 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEvkgaskdqrrqlrrDVQMVFQNPYAslnPRQKIGDQ 113
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------------DLLFLPQRPYL---PLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 114 LAepllintalsreerrekvqqmmrqvglrpehyqrYP--HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQ 191
Cdd:cd03223 84 LI----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 15599702 192 VLNLFmdlqQQFRTAYVFISH 212
Cdd:cd03223 130 LYQLL----KELGITVISVGH 146
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
30-251 |
1.50e-18 |
|
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: 86.15 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEvkgASKDQRRQLRRDVQMVFQNpyASLNpRQK 109
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP---REEIPREVLANSVAMVDQD--IFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAeplLINTALSREERREKVQ--QMMRQVGLRPEHYQrypHM-------FSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:TIGR03796 569 VRDNLT---LWDPTIPDADLVRACKdaAIHDVITSRPGGYD---AElaegganLSGGQRQRLEIARALVRNPSILILDEA 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 181 TSALDVSIQAQVLnlfmdlqQQFR---TAYVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYENPlHPYTR 251
Cdd:TIGR03796 643 TSALDPETEKIID-------DNLRrrgCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVG-GAYAR 707
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
26-225 |
3.20e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 26 QVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQeVKGASKDQRRQLRRDVQMVFQNpYASLN 105
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-LRIGYVPQKLYLDTTLPLTVNR-FLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIGDqlaepllINTALSREERREKVQQMMRQVglrpehyqryphmfSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK09544 94 PGTKKED-------ILPALKRVQAGHLIDAPMQKL--------------SGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVL 225
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-196 |
1.63e-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: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTrhyeVSRGlfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQevkgASKD 84
Cdd:TIGR01189 1 LAARNLA----CSRG------ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT----PLAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLRRDVQmvfqnpYASLNPRQKIGDQLAEPLLINTALSREERREkVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIAL 164
Cdd:TIGR01189 67 QRDEPHENIL------YLGHLPGLKPELSALENLHFWAAIHGGAQRT-IEDALAAVGLT-GFEDLPAAQLSAGQQRRLAL 138
|
170 180 190
....*....|....*....|....*....|..
gi 15599702 165 ARAMMLQPKVLVADEPTSALDVSIQAQVLNLF 196
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-245 |
2.08e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 24 HAQVRALNGVSFELEAGKTLAVVGESGCGKSTLaraLTLIE---EPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNP 100
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTL---LSLIQrhfDVSEGDIRFHDIPL---TKLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YAslnprqkIGDQLAEplliNTALSR-EERREKVQQMMRQVG-----LR-PEHYQ----RYPHMFSGGQRQRIALARAMM 169
Cdd:PRK10789 399 FL-------FSDTVAN----NIALGRpDATQQEIEHVARLASvhddiLRlPQGYDtevgERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 170 LQPKVLVADEPTSALDVSIQAQVLNlfmDLQQQFRTAYVFIS-HNLAVVRHvADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILH---NLRQWGEGRTVIISaHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-227 |
2.12e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGqEVKGASKDQRRQL--------RRDVQ 94
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-GARVAYVPQRSEVpdslpltvRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 95 MVFQNPYASLNPrqkigdqlaepllintaLSREERREkVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMMLQPKV 174
Cdd:NF040873 80 MGRWARRGLWRR-----------------LTRDDRAA-VDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHvADDVLVM 227
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATV-VVVTHDLELVRR-ADPCVLL 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-245 |
2.31e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNpyASLNPRQKIGD 112
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 113 QLAEPLLINTALSREERREKVQQMMRQVGLRPEHyQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQV 192
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 193 LNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-231 |
5.64e-17 |
|
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: 77.89 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALtLIE-EPTSGSLKIAGQevkgaskdqrrqlrrdVQMVFQNPY---ASL 104
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS----------------IAYVSQEPWiqnGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 npRQKIgdQLAEPLlintalsREERREKVqqmMRQVGLRPEhYQRYPH-----------MFSGGQRQRIALARAMMLQPK 173
Cdd:cd03250 83 --RENI--LFGKPF-------DEERYEKV---IKACALEPD-LEILPDgdlteigekgiNLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 174 VLVADEPTSALDVSIQAQVL-NLFMDLQQQFRTAyVFISHNLAVVRHvADDVLVMYLGR 231
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTR-ILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
44-236 |
6.51e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.30 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 44 AVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqRRQLRRDVQMVFQNPYAslnprqkigdqLAEPLLINTA 123
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS---HSVLRQGVAMVQQDPVV-----------LADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 124 LSREERREKVQQMMRQVGLrPEHYQRYP-----------HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQV 192
Cdd:PRK10790 437 LGRDISEEQVWQALETVQL-AELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599702 193 LNLFMDLQQQfrTAYVFISHNLAVVRHvADDVLVMYLGRPAEMG 236
Cdd:PRK10790 516 QQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-243 |
4.00e-16 |
|
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: 78.69 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 21 FKGhaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIE--EPTSGSL--------------------------- 71
Cdd:TIGR03269 10 FDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 72 -KIAGQEVK--GASKDQRRQLRRDVQMVFQNPYAsLNPRQKIGDQLAEPLLiNTALSREERREKVQQMMRQVGLrpEHyq 148
Cdd:TIGR03269 87 gTLEPEEVDfwNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLIEMVQL--SH-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 149 RYPHM---FSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVL 225
Cdd:TIGR03269 161 RITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 15599702 226 VMYLGRPAEMGPADKLYE 243
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-261 |
4.12e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 44 AVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD------QRRqlrrdVQMVFQNpyASLNPRQKI-GDqlae 116
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppeKRR-----IGYVFQD--ARLFPHYKVrGN---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 117 pLLINTALSREERREKVQQMMrqvGLRPeHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLF 196
Cdd:PRK11144 97 -LRYGMAKSMVAQFDKIVALL---GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 197 MDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENP-LHPYTR-----ALLSATPAIH 261
Cdd:PRK11144 172 ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSaMRPWLPkeeqsSILKVTVLEH 242
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-239 |
5.21e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAqvrALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrrqlrrdvqmvfQNPYA 102
Cdd:PRK15056 19 GHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--------------KNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRQKIgdQLAEPLLINTAL-------------SREERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRIALARAMM 169
Cdd:PRK15056 82 YVPQSEEV--DWSFPVLVEDVVmmgryghmgwlrrAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 170 LQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVfISHNLAVVRHVAdDVLVMYLGRPAEMGPAD 239
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFC-DYTVMVKGTVLASGPTE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-245 |
1.10e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIagQEVKGASKDQRRQLRRDVQMVFQNP------------ 100
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQDPllfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 -----------------------YASLNPRQKIGDQLAEPL--LINTALSRE--ERREKVQQMMRQ-------------- 139
Cdd:PTZ00265 482 yslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLndMSNTTDSNEliEMRKNYQTIKDSevvdvskkvlihdf 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 140 VGLRPEHYQRY----PHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLA 215
Cdd:PTZ00265 562 VSALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
250 260 270
....*....|....*....|....*....|
gi 15599702 216 VVRHvADDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PTZ00265 642 TIRY-ANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-259 |
1.90e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPYA------- 102
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI---SKFGLMDLRKVLGIIPQAPVLfsgtvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRQKIGD-QLAEpllintALSREERREKVQQmmRQVGLRPEHYQRYPHmFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:PLN03130 1332 NLDPFNEHNDaDLWE------SLERAHLKDVIRR--NSLGLDAEVSEAGEN-FSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 182 SALDVSIQAQVLNlfmDLQQQFRT-AYVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSATPA 259
Cdd:PLN03130 1403 AAVDVRTDALIQK---TIREEFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTGAA 1477
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-231 |
2.04e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.75 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 27 VRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEePT---SGSLKIAGQEVKgaSKDQRRQLRRDVQMVFQN---- 99
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCR--FKDIRDSEALGIVIIHQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 100 PYASL-------NPRQKIGdqlaeplLINtalsREERREKVQQMMRQVGLRpEHyqryPHMFSG----GQRQRIALARAM 168
Cdd:NF040905 91 PYLSIaeniflgNERAKRG-------VID----WNETNRRARELLAKVGLD-ES----PDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 169 MLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITS-IIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-241 |
3.26e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG-ASKDQRRQLRRDVQmvfQNPYASlnprq 108
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQ---QLPAAE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kiGDQLAEPLLI-----NTALSR--EERREKVQQMMRQVGLRPeHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:PRK10575 99 --GMTVRELVAIgrypwHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 182 SALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-227 |
4.31e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 27 VRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaskdqrrqlrrdvqmvFQNPYASlnp 106
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-----------------FNGPKSS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 rQKIG-----------DQL--AEplliNTALSRE-----------ERREKVQQMMRQVGLRpEHYQRYPHMFSGGQRQRI 162
Cdd:PRK10762 77 -QEAGigiihqelnliPQLtiAE----NIFLGREfvnrfgridwkKMYAEADKLLARLNLR-FSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADDVLVM 227
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRLKEIFEICDDVTVF 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-259 |
5.15e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPYA------- 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV---AKFGLTDLRRVLSIIPQSPVLfsgtvrf 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRQKIGD-QLAEpllintALSREERREKVQQmmRQVGLRPEHYQRYPHmFSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:PLN03232 1329 NIDPFSEHNDaDLWE------ALERAHIKDVIDR--NPFGLDAEVSEGGEN-FSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 182 SALDVSIQAQVLNlfmDLQQQFRT-AYVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSATPA 259
Cdd:PLN03232 1400 ASVDVRTDSLIQR---TIREEFKScTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-196 |
9.54e-15 |
|
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: 71.76 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgasKDQRRQLRRDVQMvfqnpyaslnprqk 109
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLY-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAepllINTALSREER---------REKVQQMMRQVGLRP-EHyqRYPHMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:cd03231 78 LGHAPG----IKTTLSVLENlrfwhadhsDEQVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170
....*....|....*..
gi 15599702 180 PTSALDVSIQAQVLNLF 196
Cdd:cd03231 152 PTTALDKAGVARFAEAM 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-231 |
1.18e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRGlfkghaqVRALNGVSFELEAGKTLAVVGESGCGKSTLARAL-TLIEEPTSGSLKIAGQEVKg 80
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPH-------IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVK- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 aSKDQRRQLRRDVQMVFQNpyaslnpRQKIG----------------DQLAEPLLINTALSREERREKVQQMmrQVglrp 144
Cdd:PRK13549 329 -IRNPQQAIAQGIAMVPED-------RKRDGivpvmgvgknitlaalDRFTGGSRIDDAAELKTILESIQRL--KV---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 145 ehyqRYPHMF------SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVR 218
Cdd:PRK13549 395 ----KTASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVL 469
|
250
....*....|...
gi 15599702 219 HVADDVLVMYLGR 231
Cdd:PRK13549 470 GLSDRVLVMHEGK 482
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-214 |
1.27e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG-ASKDQRRQLRRDVQMVFQNPY 101
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ASLNPRQKIGDQLAEPLLINTalsREERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRW---RKEDEEAVTKAMQATGITHLADQSVDTL-SGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190
....*....|....*....|....*....|...
gi 15599702 182 SALDVSIQAQVLNLFMDLQQQFRTAYVFISHNL 214
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-198 |
1.66e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTrhyeVSRG---LFKGhaqvralngVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKg 80
Cdd:PRK13538 1 MLEARNLA----CERDeriLFSG---------LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 askDQRRQLRRDvqMVFqnpyaslnprqkIGDQLA--------EPLLINTALSREERREKVQQMMRQVGLRpeHYQRYP- 151
Cdd:PRK13538 67 ---RQRDEYHQD--LLY------------LGHQPGikteltalENLRFYQRLHGPGDDEALWEALAQVGLA--GFEDVPv 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599702 152 HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMD 198
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-246 |
2.58e-14 |
|
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: 71.03 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRqlRRDVQMVF 97
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--RLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QNP--YASLNPRQKIgdqLAepLLINTALSREERREKVQQMMRQVGLrpEHYQRYPHMF-SGGQRQRIALARAMMLQPKV 174
Cdd:cd03218 82 QEAsiFRKLTVEENI---LA--VLEIRGLSKKEREEKLEELLEEFHI--THLRKSKASSlSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 175 LVADEPTSALD---VS-IQAQVLNLfmdlqqQFRTAYVFIS-HNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPL 246
Cdd:cd03218 155 LLLDEPFAGVDpiaVQdIQKIIKIL------KDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-231 |
2.74e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSRglfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARAL-TLIEEPTSGSLKIAGQEVkg 80
Cdd:TIGR02633 255 DVILEARNLTCWDVINP-------HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 ASKDQRRQLRRDVQMVFQNpyaslNPRQKIGDQLAEPLLINTA----------LSREERREKVQQMMRQVGLRPEHYQRY 150
Cdd:TIGR02633 326 DIRNPAQAIRAGIAMVPED-----RKRHGIVPILGVGKNITLSvlksfcfkmrIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 151 PHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfRTAYVFISHNLAVVRHVADDVLVMYLG 230
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
.
gi 15599702 231 R 231
Cdd:TIGR02633 480 K 480
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-185 |
1.35e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASkdqrRQLRRDVQMVF 97
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 98 QnpYASLNPRQKIgdqlAEPLLINT---ALSREERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKV 174
Cdd:PRK13537 87 Q--FDNLDPDFTV----RENLLVFGryfGLSAAAARALVPPLLEFAKLENKADAKVGEL-SGGMKRRLTLARALVNDPDV 159
|
170
....*....|.
gi 15599702 175 LVADEPTSALD 185
Cdd:PRK13537 160 LVLDEPTTGLD 170
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-234 |
2.03e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTlieeptsgslkiagqevkgaskdqRRQLRRDVQMVFQNPYASLNPR 107
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA------------------------GALKGTPVAGCVDVPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 QKIGDQLAEPLLINTALsreerrekvqQMMRQVGLR-PEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:COG2401 100 ASLIDAIGRKGDFKDAV----------ELLNAVGLSdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599702 187 SiQAQVLNL-FMDLQQQFRTAYVFISHNLAVVRHVADDVLVM--YLGRPAE 234
Cdd:COG2401 170 Q-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPEE 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-196 |
2.14e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTrhyeVSRG---LFKGhaqvralngVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkg 80
Cdd:PRK13539 2 MLEGEDLA----CVRGgrvLFSG---------LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 81 askdqrRQLRRDVQMVFQNPYASLNPRQKIGDQLA--------EPLLINTALSReerrekvqqmmrqVGLRPEHYQRYpH 152
Cdd:PRK13539 67 ------DDPDVAEACHYLGHRNAMKPALTVAENLEfwaaflggEELDIAAALEA-------------VGLAPLAHLPF-G 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLF 196
Cdd:PRK13539 127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-245 |
2.28e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkGASKdqRRQLRRDVQMVFQNPYA-SLNPRQ 108
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI-GAYG--LRELRRQFSMIPQDPVLfDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIgdqlaEPLLintalsrEERREKVQQMMRQVGLRpEH-----------YQRYPHMFSGGQRQRIALARAMMLQ-PKVLV 176
Cdd:PTZ00243 1403 NV-----DPFL-------EASSAEVWAALELVGLR-ERvasesegidsrVLEGGSNYSVGQRQLMCMARALLKKgSGFIL 1469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 177 ADEPTS----ALDVSIQAQVLNLFmdlqqqfrTAY--VFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKLYENP 245
Cdd:PTZ00243 1470 MDEATAnidpALDRQIQATVMSAF--------SAYtvITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-185 |
2.30e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYevsrGLFKghaqvrALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgA 81
Cdd:NF033858 264 EPAIEARGLTMRF----GDFT------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--D 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDqrRQLRRDVQMVFQ--NPYASLNPRQkigdqlaeplliNTAL-------SREERREKVQQMMRQVGLRpEHYQRYPH 152
Cdd:NF033858 332 AGD--IATRRRVGYMSQafSLYGELTVRQ------------NLELharlfhlPAAEIAARVAEMLERFDLA-DVADALPD 396
|
170 180 190
....*....|....*....|....*....|...
gi 15599702 153 MFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:NF033858 397 SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-226 |
2.34e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKG-ASKDQRRQLRRDVQMVFQNPYA-SLNPRQKI 110
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNdMTNEQDYQGDEEQNVGMKNVNEfSLTKEGGS 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 111 GDQLA--------------------------------EPLLINTAL------SREE-RREKVQQMMRQVGLR------PE 145
Cdd:PTZ00265 1267 GEDSTvfknsgkilldgvdicdynlkdlrnlfsivsqEPMLFNMSIyenikfGKEDaTREDVKRACKFAAIDefieslPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 146 HYQR----YPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHvA 221
Cdd:PTZ00265 1347 KYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
....*
gi 15599702 222 DDVLV 226
Cdd:PTZ00265 1426 DKIVV 1430
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-246 |
3.10e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.13 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYevsrglfkGHAQVraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:COG1137 1 MMTLEAENLVKSY--------GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQR---------------RQLRrdvqmVFQNPYASLnprqkigdQLAEpllintaLSREERREKVQQMMRQVGLrpEH 146
Cdd:COG1137 71 PMHKRarlgigylpqeasifRKLT-----VEDNILAVL--------ELRK-------LSKKEREERLEELLEEFGI--TH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 147 YQRYPHM-FSGGQRQRIALARAMMLQPKVLVADEPTSALD---VS-IQAQVLNLfmdlqqQFRTAYVFIS-HNlavVRH- 219
Cdd:COG1137 129 LRKSKAYsLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL------KERGIGVLITdHN---VREt 199
|
250 260
....*....|....*....|....*....
gi 15599702 220 --VADDVLVMYLGRPAEMGPADKLYENPL 246
Cdd:COG1137 200 lgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-241 |
3.89e-13 |
|
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: 70.36 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQevkgaskdqrrqlrrdVQMVFQNPYASlnprqk 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQQAWIQ------ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 iGDQLAEPLLINTALsrEERRekVQQMMRQVGLRPEhYQRYPH-----------MFSGGQRQRIALARAMMLQPKVLVAD 178
Cdd:TIGR00957 712 -NDSLRENILFGKAL--NEKY--YQQVLEACALLPD-LEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 179 EPTSALDVSIQAQVLNLFMD----LQQQFRtayVFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKL 241
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-231 |
8.23e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALtlieeptSGSLK---IAGQEVKGASKDQRRQLRRdVQMVFQNP--YASL 104
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILANNRKPTKQILKR-TGFVTQDDilYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 NPRQKIgdQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMF----SGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PLN03211 156 TVRETL--VFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-239 |
1.64e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 24 HAQV---RALNGVSFELEAGKTLAVVGESGCGKSTLARALTliEEP----TSGSLKIAGQEVKGASKDQRRQLrrDVQMV 96
Cdd:CHL00131 14 HASVnenEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEERAHL--GIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 97 FQNPY------------ASLNPRQK-IGDQLAEPL----LINTALSReerrekvqqmmrqVGLRPEHYQRYPHM-FSGGQ 158
Cdd:CHL00131 90 FQYPIeipgvsnadflrLAYNSKRKfQGLPELDPLefleIINEKLKL-------------VGMDPSFLSRNVNEgFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 159 RQRIALARAMMLQPKVLVADEPTSALDVS---IQAQVLNLFMDLQQqfrtAYVFISHNLAVVRHVADD-VLVMYLGRPAE 234
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKPDyVHVMQNGKIIK 232
|
....*
gi 15599702 235 MGPAD 239
Cdd:CHL00131 233 TGDAE 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-238 |
4.49e-12 |
|
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: 64.74 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 27 VRALNGVSFELEAG-----KTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgASKDQrrQLRRDVQMVFQNPY 101
Cdd:cd03237 7 KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV--SYKPQ--YIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ASLNPRQKIGDQ----LAEPLLINtalsreerrekvQQMMRQVglrPEhyqryphmFSGGQRQRIALARAMMLQPKVLVA 177
Cdd:cd03237 83 SSITKDFYTHPYfkteIAKPLQIE------------QILDREV---PE--------LSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 178 DEPTSALDV---SIQAQVLNLFMDLQQqfRTAYVfISHNLAVVRHVADDVLVmYLGRPAEMGPA 238
Cdd:cd03237 140 DEPSAYLDVeqrLMASKVIRRFAENNE--KTAFV-VEHDIIMIDYLADRLIV-FEGEPSVNGVA 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-227 |
6.02e-12 |
|
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: 64.27 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 15 EVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQ-EVKGASKDQRRQLRRDV 93
Cdd:cd03290 2 QVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 94 QMVFQNPYAsLNPRQKIGDQLAEPLlintalsreeRREKVQQMMRQVGLRPEhYQRYPH-----------MFSGGQRQRI 162
Cdd:cd03290 82 AYAAQKPWL-LNATVEENITFGSPF----------NKQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSI-----QAQVLNLfmdLQQQFRTAyVFISHNLAVVRHvADDVLVM 227
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKF---LQDDKRTL-VLVTHKLQYLPH-ADWIIAM 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-185 |
6.56e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.33 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLaraLTLI---EEPTSGSLKIAGQEVKGASKdqrRQLRRDVQ 94
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL---LSMIsrlLPPDSGEVLVDGLDVATTPS---RELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 95 MVFQNPyaSLNPRQKIGDqlaeplLIntALSR---------EERREKVQQMMRQVGLRP-EHyqRYPHMFSGGQRQRiAL 164
Cdd:COG4604 79 ILRQEN--HINSRLTVRE------LV--AFGRfpyskgrltAEDREIIDEAIAYLDLEDlAD--RYLDELSGGQRQR-AF 145
|
170 180
....*....|....*....|...
gi 15599702 165 ArAMML--QPKVLVADEPTSALD 185
Cdd:COG4604 146 I-AMVLaqDTDYVLLDEPLNNLD 167
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-208 |
7.58e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 1 METVLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARalTLIEEP--TSGSLKIAGQEV 78
Cdd:PRK11614 2 EKVMLSFDKVSAHY----------GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLG--TLCGDPraTSGRIVFDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 79 KGASkdQRRQLRRDVQMVFQNpyASLNPRQKIGDQLAEPLLIntalsrEERREKVQQMMRQVGLRPEHYQRYPH---MFS 155
Cdd:PRK11614 70 TDWQ--TAKIMREAVAIVPEG--RRVFSRMTVEENLAMGGFF------AERDQFQERIKWVYELFPRLHERRIQragTMS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 156 GGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYV 208
Cdd:PRK11614 140 GGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-225 |
1.09e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEvSRGLFKGhaqvralngVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIA-----GQEVK 79
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKN---------LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenaniGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 GASKD------------QRRQLRRDVQMVfqnpyaslnpRQKIGDQLaepllintaLSREERREKVQqmmrqvglrpehy 147
Cdd:PRK15064 390 DHAYDfendltlfdwmsQWRQEGDDEQAV----------RGTLGRLL---------FSQDDIKKSVK------------- 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 148 qryphMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV-SIQAqvLNLFMDlqqQFRTAYVFISHNLAVVRHVADDVL 225
Cdd:PRK15064 438 -----VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNMALE---KYEGTLIFVSHDREFVSSLATRII 506
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-231 |
2.24e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.94 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTL-ARALTLIeePTSGSLKIAGQEVKGASKDQRRQLR-----RDV---QM-VFQn 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLlARMAGLL--PGQGEILLNGRPLSDWSAAELARHRaylsqQQSppfAMpVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 100 pYASLNPRQKIGDQLAEPLLintalsreerrekvQQMMRQVGLRPEhYQRYPHMFSGGQRQRIALArAMMLQ-------- 171
Cdd:COG4138 89 -YLALHQPAGASSEAVEQLL--------------AQLAEALGLEDK-LSRPLTQLSGGEWQRVRLA-AVLLQvwptinpe 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599702 172 PKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLA-VVRHvADDVLVMYLGR 231
Cdd:COG4138 152 GQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITV-VMSSHDLNhTLRH-ADRVWLLKQGK 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-185 |
2.65e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgasKDQRRQLRrdvQMVFQNPYASLNPRQk 109
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---KDLCTYQK---QLCFVGHRSGINPYL- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 110 igdQLAEPLLINTALSREERreKVQQMMRQVGLrpEHYQRYP-HMFSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK13540 90 ---TLRENCLYDIHFSPGAV--GITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-202 |
3.23e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 16 VSRGLFKGHaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLrrdVQM 95
Cdd:PRK10938 6 ISQGTFRLS-DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQ-NPYASLNPRQK-IGDQLAEplLINTALSREERrekVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPK 173
Cdd:PRK10938 82 EWQrNNTDMLSPGEDdTGRTTAE--IIQDEVKDPAR---CEQLAQQFGITALLDRRFKYL-STGETRKTLLCQALMSEPD 155
|
170 180
....*....|....*....|....*....
gi 15599702 174 VLVADEPTSALDVSIQAQVLNLFMDLQQQ 202
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-212 |
4.12e-11 |
|
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: 63.61 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLkiagqevkgaSKDQRRQLRrdvqMVFQNPYASLNprqK 109
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL----------TKPAKGKLF----YVPQRPYMTLG---T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEPLLINTALSREERREKVQQMM----------RQVGLrpEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDLEQILdnvqlthileREGGW--SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 15599702 180 PTSALDVSIQAQVLNLFmdlqQQFRTAYVFISH 212
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-231 |
4.35e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.12 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 16 VSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPT---SGSLKIAGQEVKGASKDQRRQL--- 89
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIiyv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 90 -RRDVQMvfqnpyASLNPRQkigdqlaeplLINTALsreerREKVQQMMRQVglrpehyqryphmfSGGQRQRIALARAM 168
Cdd:cd03233 89 sEEDVHF------PTLTVRE----------TLDFAL-----RCKGNEFVRGI--------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 169 MLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVR--HVADDVLVMYLGR 231
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTT-TFVSLYQASDEiyDLFDKVLVLYEGR 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-186 |
4.74e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.42 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYEvSRGLFkghaqvralNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIaGQEVKGASK 83
Cdd:TIGR03719 322 VIEAENLTKAFG-DKLLI---------DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQLRRDVQMVFQ-----NPYASLNPRQkigdqlaepllINTA--LSREERREKVQQmmRQVGlrpehyqryphMFSG 156
Cdd:TIGR03719 391 DQSRDALDPNKTVWEeisggLDIIKLGKRE-----------IPSRayVGRFNFKGSDQQ--KKVG-----------QLSG 446
|
170 180 190
....*....|....*....|....*....|
gi 15599702 157 GQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-231 |
5.12e-11 |
|
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: 60.08 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 40 GKTLAVVGESGCGKSTLARALTLIEEPTSGSLkiagqevkgaskdqrrqlrrdvqmvfqnpyaslnprqkigdqlaepLL 119
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------------IY 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 120 INTALSREERREKvqqmmrqvgLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVL-----N 194
Cdd:smart00382 36 IDGEDILEEVLDQ---------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelR 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599702 195 LFMDLQQQFRTAYVFISHNL-----AVVRHVADDVLVMYLGR 231
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-185 |
8.29e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 16 VSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRqlRRDVQM 95
Cdd:PRK10895 5 TAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNpyASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLrpEHYQ-RYPHMFSGGQRQRIALARAMMLQPKV 174
Cdd:PRK10895 83 LPQE--ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLRdSMGQSLSGGERRRVEIARALAANPKF 158
|
170
....*....|.
gi 15599702 175 LVADEPTSALD 185
Cdd:PRK10895 159 ILLDEPFAGVD 169
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-235 |
1.23e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYevsrglfkgHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKD 84
Cdd:PRK10522 323 LELRNVTFAY---------QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QRRQLrrdVQMVFQNPY---ASLNPrqkiGDQLAEPLLINTALSREERREKVQ-QMMRQVGLRpehyqryphmFSGGQRQ 160
Cdd:PRK10522 394 DYRKL---FSAVFTDFHlfdQLLGP----EGKPANPALVEKWLERLKMAHKLElEDGRISNLK----------LSKGQKK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 161 RIALARAMMLQPKVLVADEptSALDVSIQ------AQVLNLfmdLQQQFRTayVF-ISHNLAVVRHvADDVLVMYLGRPA 233
Cdd:PRK10522 457 RLALLLALAEERDILLLDE--WAADQDPHfrrefyQVLLPL---LQEMGKT--IFaISHDDHYFIH-ADRLLEMRNGQLS 528
|
..
gi 15599702 234 EM 235
Cdd:PRK10522 529 EL 530
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-235 |
1.80e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVSrglfkghaqvraLNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:PRK10982 248 EVILEVRNLTSLRQPS------------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 S------------KDQRRQ--LRRDVQMVFQNPYASLNP-RQKIGdqlaepLLINTALSREerrekVQQMMRQVGLRPEH 146
Cdd:PRK10982 316 NaneainhgfalvTEERRStgIYAYLDIGFNSLISNIRNyKNKVG------LLDNSRMKSD-----TQWVIDSMRVKTPG 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 147 YQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADDVLV 226
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILV 463
|
....*....
gi 15599702 227 MYLGRPAEM 235
Cdd:PRK10982 464 MSNGLVAGI 472
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-240 |
3.13e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEA-------GKTLAVVGESGCGKSTLARALTLIEEPTSGS----LKIA--GQEVKGASKDQRRQLRRDVQMVFQNP 100
Cdd:PRK13409 352 DFSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpeLKISykPQYIKPDYDGTVEDLLRSITDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YasLNPrqkigdQLAEPLLINTALSREERRekvqqmmrqvglrpehyqryphmFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PRK13409 432 Y--YKS------EIIKPLQLERLLDKNVKD-----------------------LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 181 TSALDVS---IQAQVLNLFMDLQQqfRTAYVfISHNLAVVRHVADDVLVmYLGRPAEMGPADK 240
Cdd:PRK13409 481 SAHLDVEqrlAVAKAIRRIAEERE--ATALV-VDHDIYMIDYISDRLMV-FEGEPGKHGHASG 539
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-231 |
3.27e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAS-KDQRRQ---L----RRDVQMVfqnPYASL 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAgimLcpedRKAEGII---PVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 NPRQKI---GDQLAEPLLINTALSREERREKVQQMMRQVglrPEHYQryPHMF-SGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PRK11288 349 ADNINIsarRHHLRAGCLINNRWEAENADRFIRSLNIKT---PSREQ--LIMNlSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599702 181 TSALDVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-185 |
4.42e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.84 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgasKDQRRQLRRDVQMVFQnpYASLNPRQK 109
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 110 IgdqlAEPLLINT---ALSREERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK13536 131 V----RENLLVFGryfGMSTREIEAVIPSLLEFARLESKADARVSDL-SGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-241 |
4.48e-10 |
|
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: 60.73 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPY-------A 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI---AKIGLHDLRFKITIIPQDPVlfsgslrM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRQKIGDQLaepllINTALSREERREKVQQMmrQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPTS 182
Cdd:TIGR00957 1379 NLDPFSQYSDEE-----VWWALELAHLKTFVSAL--PDKLDHECAEGGENL-SVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 183 ALDVS----IQAQVlnlfmdlQQQFRTAYVF-ISHNLAVVRHVAdDVLVMYLGRPAEMG-PADKL 241
Cdd:TIGR00957 1451 AVDLEtdnlIQSTI-------RTQFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFGaPSNLL 1507
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-236 |
5.40e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIE--EPTSGSLKIAGQEVKGASKDQRRQlrRDVQMVFQNPY------ 101
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG--EGIFMAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 102 ------ASLNPRQKIGDQlaEPLlintalSREERREKVQQMMRQVGLRPEHYQRYPHM-FSGGQRQRIALARAMMLQPKV 174
Cdd:PRK09580 95 nqfflqTALNAVRSYRGQ--EPL------DRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADD-VLVMYLGRPAEMG 236
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKPDyVHVLYQGRIVKSG 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-241 |
7.71e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.36 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARAlTLIEEPTSGSLKIAGQEVKGASKDQRRQL--RRDVQM 95
Cdd:NF000106 17 RGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP-AHV*GPDAGRRPWRF*TWCANRRALRRTIg*HRPVR* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNPYASLNPRQKIGDQLAepllintaLSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARAMMLQPKVL 175
Cdd:NF000106 96 GRRESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 176 VADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKL 241
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATV-LLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-236 |
7.77e-10 |
|
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: 58.53 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 40 GKTLAVVGESGCGKSTLARALTLIEEPTSGSLK-----------IAGQEVKgaskDQRRQLRRDVQMVFQNP-YASLNPR 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQ----NYFTKLLEGDVKVIVKPqYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 108 Q---KIGDqlaepllintALSREERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPTSAL 184
Cdd:cd03236 102 AvkgKVGE----------LLKKKDERGKLDELVDQLELRHVLDRNIDQL-SGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599702 185 DVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADDVLVMYlGRPAEMG 236
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-GEPGAYG 220
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-236 |
1.02e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.52 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrrqlrrdvqmvfqnpyASLNpRQ 108
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS------------------SGLN-GQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYpHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:PRK13545 100 LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPV-KTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599702 189 QAQVLNLFMDLQQQFRTAYvFISHNLAVVRHVADDVLVMYLGRPAEMG 236
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-231 |
1.72e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKdqrrqlrrdvQMVFQNPYASLNPRQK 109
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP----------QDGLANGIVYISEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 iGDQL-------------AEPLLINTA--LSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKV 174
Cdd:PRK10762 338 -RDGLvlgmsvkenmsltALRYFSRAGgsLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFmdlqQQFRT---AYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLI----NQFKAeglSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-238 |
1.95e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFELEA-------GKTLAVVGESGCGKSTLARALTLIEEPTSGS----LKIA--GQEVKGASKDQRRQ-LRRDVQMVFQN 99
Cdd:COG1245 353 GFSLEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedLKISykPQYISPDYDGTVEEfLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 100 PYaslnprqkIGDQLAEPLLIntalsreerrEKVqqmmrqvglrpehYQRYPHMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:COG1245 433 SY--------YKTEIIKPLGL----------EKL-------------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 180 PTSALDVS---IQAQVLNLFMDLQQqfRTAYVfISHNLAVVRHVADDVLVmYLGRPAEMGPA 238
Cdd:COG1245 482 PSAHLDVEqrlAVAKAIRRFAENRG--KTAMV-VDHDIYLIDYISDRLMV-FEGEPGVHGHA 539
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-231 |
1.98e-09 |
|
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: 58.87 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 23 GHAQVRALNGVSFEleaGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLrrdvqmvfqnpya 102
Cdd:TIGR01257 942 GRPAVDRLNITFYE---NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSL------------- 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRQKI---GDQLAEPLLINTAL---SREERREKVQQMMRQVGLrpeHYQRYPHM--FSGGQRQRIALARAMMLQPKV 174
Cdd:TIGR01257 1006 GMCPQHNIlfhHLTVAEHILFYAQLkgrSWEEAQLEMEAMLEDTGL---HHKRNEEAqdLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMdlqqQFRTAYVFI--SHNLAVVRHVADDVLVMYLGR 231
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLL----KYRSGRTIImsTHHMDEADLLGDRIAIISQGR 1137
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-225 |
2.40e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTL--------------IEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQM 95
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGDDTTALQCVLNTDIERTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 96 VFQNPYASLnPRQKIGDQLAEplliNTALSREERREKVQQMMRQVGL-------------------RPEHYQRYPHMFSG 156
Cdd:PLN03073 273 VAQQRELEF-ETETGKGKGAN----KDGVDKDAVSQRLEEIYKRLELidaytaearaasilaglsfTPEMQVKATKTFSG 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 157 GQRQRIALARAMMLQPKVLVADEPTSALDVSiqaQVLNLFMDLQQQFRTaYVFISHNLAVVRHVADDVL 225
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLH---AVLWLETYLLKWPKT-FIVVSHAREFLNTVVTDIL 412
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-217 |
3.31e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIaGQEVKGASKDQRRqlrrdvqmvfqnpyASLNPRQK 109
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHR--------------AELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQLAEpllintalsreerreKVQQMMrqVGLRPEHYQRYPHMF--------------SGGQRQRIALARaMMLQP-KV 174
Cdd:PRK11147 400 VMDNLAE---------------GKQEVM--VNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPsNL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599702 175 LVADEPTSALDVsiqaQVLNLFMDLQQQFRTAYVFISHNLAVV 217
Cdd:PRK11147 462 LILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-186 |
3.42e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 3 TVLTARDLTRHYEvSRGLFKGhaqvralngVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIaGQEVKGAS 82
Cdd:PRK11819 323 KVIEAENLSKSFG-DRLLIDD---------LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 83 KDQRRqlrrdvqmvfqnpyASLNPRQKIGDQLAEPLLINTALSRE-ERREKV---------QQmmRQVGlrpehyqryph 152
Cdd:PRK11819 392 VDQSR--------------DALDPNKTVWEEISGGLDIIKVGNREiPSRAYVgrfnfkggdQQ--KKVG----------- 444
|
170 180 190
....*....|....*....|....*....|....*.
gi 15599702 153 MFSGGQRQRIALarAMMLQP--KVLVADEPTSALDV 186
Cdd:PRK11819 445 VLSGGERNRLHL--AKTLKQggNVLLLDEPTNDLDV 478
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-185 |
5.25e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 4 VLTARDLTRHYevsrglfkghAQVRALNGVSFELEAGKTLAVVGESGCGKSTLaraLTLIeeptSGSLKI-AGQ-EVKGA 81
Cdd:NF033858 1 VARLEGVSHRY----------GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL---LSLI----AGARKIqQGRvEVLGG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SKDQRRQlRRDV--------QMVFQNPYASLNPRQKI-------GdqlaepllintaLSREERREKVQQMMRQVGLRPeh 146
Cdd:NF033858 64 DMADARH-RRAVcpriaympQGLGKNLYPTLSVFENLdffgrlfG------------QDAAERRRRIDELLRATGLAP-- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599702 147 yqryphmF--------SGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:NF033858 129 -------FadrpagklSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-240 |
8.06e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQ--VRALNGVSFELEAGKTLAVVGESGCGKSTLARALTlieEPTSGSLKIAGQEVK--GASKDQ-RRQLRRD 92
Cdd:TIGR00956 63 RKLKKFRDTktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA---SNTDGFHIGVEGVITydGITPEEiKKHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 93 VQMVFQN----PYASLNPRQKIGDQLAEPLLINTALSREERREKVQQM-MRQVGLRPEHYQRYPHMF----SGGQRQRIA 163
Cdd:TIGR00956 140 VVYNAETdvhfPHLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvSGGERKRVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 164 LARAMMLQPKVLVADEPTSALDVS----------IQAQVLNL--FMDLQQQFRTAY-VFishnlavvrhvaDDVLVMYLG 230
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSAtalefiralkTSANILDTtpLVAIYQCSQDAYeLF------------DKVIVLYEG 287
|
250
....*....|
gi 15599702 231 RPAEMGPADK 240
Cdd:TIGR00956 288 YQIYFGPADK 297
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-231 |
1.09e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 27 VRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKgaSKDQRRQLRRDVQMVFQnpyaSLNP 106
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--FKSSKEALENGISMVHQ----ELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 -RQKigdqlaePLLINTALSREERRekvqqmmrqvGLRPEH---YQRYPHMF----------------SGGQRQRIALAR 166
Cdd:PRK10982 85 vLQR-------SVMDNMWLGRYPTK----------GMFVDQdkmYRDTKAIFdeldididprakvatlSVSQMQMIEIAK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 167 AMMLQPKVLVADEPTSALDvsiQAQVLNLFMDLQ--QQFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLT---EKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-239 |
1.19e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 29 ALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGqevkgaskdqrrqlrrDVQMVFQNpyASLNPrQ 108
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--AGLSG-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 KIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHmFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKK-YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599702 189 QAQVLNLFMDLQQQFRTAYvFISHNLAVVRHVADDVLVMYLGRPAEMGPAD 239
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIF-FVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-221 |
1.28e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 35 FELEAGKTLAVVGESGCGKSTLaraltlieeptsgsLKIAGQEVkgASKDQRRQLRRD--VQMVFQNPyaslnPRQKIGD 112
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTL--------------MKILNGEV--LLDDGRIIYEQDliVARLQQDP-----PRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 113 ----------QLAEPLLINTALSR---EERREKVQQMMRQVGLRPEHYQRY----------------PHM----FSGGQR 159
Cdd:PRK11147 83 vydfvaegieEQAEYLKRYHDISHlveTDPSEKNLNELAKLQEQLDHHNLWqlenrinevlaqlgldPDAalssLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 160 QRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDlqqqFRTAYVFISHNLAVVRHVA 221
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMA 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-240 |
2.33e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.17 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKST-LARALTLIeePTSGSLKIAGQ---EVKGASKDQRR-----QLRRDVQM-VFQnpYA 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTlLARMAGLL--PGSGSIQFAGQpleAWSAAELARHRaylsqQQTPPFAMpVFQ--YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 slnprqkigdQLAEPLLINTALSREERREKVQQMMRQVGLrpehyQRYPHMFSGGQRQRIALArAMMLQ--------PKV 174
Cdd:PRK03695 91 ----------TLHQPDKTRTEAVASALNEVAEALGLDDKL-----GRSVNQLSGGEWQRVRLA-AVVLQvwpdinpaGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 175 LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVADDVLVMYLGRPAEMGPADK 240
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAV-VMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-237 |
3.32e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 25 AQVRALNGVSFELEAGKTLAVVGESGCGKSTLAraltlieeptsgslkiagQEVKGASKdqRRQLRRDVQMVFQNPYASL 104
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV------------------NEGLYASG--KARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 105 nprqkigDQLAepLLINTALSReerrekvqqmmrqvgLRPEhyqRYPHMFSGGQRQRIALARAMMLQPK--VLVADEPTS 182
Cdd:cd03238 66 -------DQLQ--FLIDVGLGY---------------LTLG---QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 183 ALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHvADDVLvmylgrpaEMGP 237
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIDLGNTV-ILIEHNLDVLSS-ADWII--------DFGP 163
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-241 |
9.67e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.22 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVkgaSKDQRRQLRRDVQMVFQNPYA------- 102
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI---SKLPLHTLRSRLSIILQDPILfsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 103 SLNPRQKIGD-QLAEPLLIntalsreerrEKVQQMMRQV-GLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:cd03288 114 NLDPECKCTDdRLWEALEI----------AQLKNMVKSLpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 181 TSALDVS----IQAQVLNLFMDlqqqfRTAyVFISHNLAVVRHvADDVLVMYLGRPAEMGPADKL 241
Cdd:cd03288 184 TASIDMAteniLQKVVMTAFAD-----RTV-VTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-231 |
1.03e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIA-GQEVKGASKDQRRQLRRDvqmvfqnpyaslnprq 108
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRAD---------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 109 kigdqlAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSI 188
Cdd:PRK10636 392 ------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599702 189 QAQVLNLFMDlqqqFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PRK10636 466 RQALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-233 |
3.68e-07 |
|
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: 51.32 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFEL------EAGKTLAVVGESGCGKSTLARALT--LI-------EEPT--------SGSL------KIAGQEVKGASKD 84
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSgeLKpnlgdydEEPSwdevlkrfRGTElqdyfkKLANGEIKVAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 85 QrrqlrrdvqmvfqnpYASLNPRQKIGDqlaepllINTALSREERREKVQQMMRQVGLRP--EHYQRYphmFSGGQRQRI 162
Cdd:COG1245 167 Q---------------YVDLIPKVFKGT-------VRELLEKVDERGKLDELAEKLGLENilDRDISE---LSGGELQRV 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRtaYVF-ISHNLAVVRHVADDVLVMYlGRPA 233
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK--YVLvVEHDLAILDYLADYVHILY-GEPG 290
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-89 |
3.68e-07 |
|
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: 51.34 E-value: 3.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQL 89
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-235 |
4.45e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHyevsrglfkghaQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGA 81
Cdd:PRK09700 263 ETVFEVRNVTSR------------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 82 SK-DQRR-------QLRRDVQM-----VFQNpyASLNPRQKIGDQLAEPLLINtalSREERR--EKVQQMMrqvGLRPEH 146
Cdd:PRK09700 331 SPlDAVKkgmayitESRRDNGFfpnfsIAQN--MAISRSLKDGGYKGAMGLFH---EVDEQRtaENQRELL---ALKCHS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 147 YQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVfISHNLAVVRHVADDVLV 226
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM-VSSELPEIITVCDRIAV 481
|
....*....
gi 15599702 227 MYLGRPAEM 235
Cdd:PRK09700 482 FCEGRLTQI 490
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-244 |
5.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALtLIEEPT--SGSLKIAGQ--EVKGASKDQRRQLRRDVqmVFQNPYASln 105
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPPrsDASVVIRGTvaYVPQVSWIFNATVRDNI--LFGSPFDP-- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 prqkigdqlaepllintalSREERREKVQQMMRQVGLRP-----EHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:PLN03130 708 -------------------ERYERAIDVTALQHDLDLLPggdltEIGERGVNI-SGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 181 TSALDVSIQAQVLN--LFMDLQQQFRtayVFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PLN03130 768 LSALDAHVGRQVFDkcIKDELRGKTR---VLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-211 |
7.13e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 5 LTARDLTRHYEVSrglfkGHAqvrALNGVSFELEAGKTLAVVGESGCGKSTLARA-LTLIEepTSGSLKIAGQEVKGASK 83
Cdd:cd03289 3 MTVKDLTAKYTEG-----GNA---VLENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLN--TEGDIQIDGVSWNSVPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 84 DQRRQ----LRRDVqMVFQNPY-ASLNPRQKIGDqlaepllintalsreerrEKVQQMMRQVGLRPEhYQRYP------- 151
Cdd:cd03289 73 QKWRKafgvIPQKV-FIFSGTFrKNLDPYGKWSD------------------EEIWKVAEEVGLKSV-IEQFPgqldfvl 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 152 ----HMFSGGQRQRIALARAMMLQPKVLVADEPTSALDvSIQAQVLNlfMDLQQQFRTAYVFIS 211
Cdd:cd03289 133 vdggCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIR--KTLKQAFADCTVILS 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-193 |
8.36e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGqevkgaskdqrrqlrrdvQMVFQNPYASLNPrQK 109
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------------RISFSPQTSWIMP-GT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IGDQlaepllINTALSREERRE----KVQQMMRQVGLRPEHyQRYPHM-----FSGGQRQRIALARAMMLQPKVLVADEP 180
Cdd:TIGR01271 503 IKDN------IIFGLSYDEYRYtsviKACQLEEDIALFPEK-DKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|...
gi 15599702 181 TSALDVSIQAQVL 193
Cdd:TIGR01271 576 FTHLDVVTEKEIF 588
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-241 |
9.40e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALT--LIEEPTSGSLKIAGQ-----EVKGASKDQRRQLRRDVQMVFQNP 100
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdLTGGGAPRGARVTGDvtlngEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YASLNPRQKIGDQLAEPLLINTALSREERrEKVQQMMRQVGLRPeHYQRYPHMFSGGQRQRIALARAM---------MLQ 171
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRDG-EIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 172 PKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISH--NLAvVRHvADDVLVMYLGRPAEMG-PADKL 241
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHdpNLA-ARH-ADRIAMLADGAIVAHGaPADVL 243
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-230 |
2.75e-06 |
|
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: 47.24 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEP--TSGSLKIAGQEVKgaskdqrRQLRRDVQMVFQNPyaSLN 105
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD-------KNFQRSTGYVEQQD--VHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 106 PRQKIgdqlAEPLLINTALSreerrekvqqmmrqvGLRPEhyqryphmfsggQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:cd03232 92 PNLTV----REALRFSALLR---------------GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599702 186 VSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLG 230
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-244 |
3.75e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTlieeptsGSLKIAgqevkgasKDQRRQLRRDVQMVFQNPY---ASLNP 106
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELSHA--------ETSSVVIRGSVAYVPQVSWifnATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 107 RQKIGDQLaEPllintalSREERREKVQQMMRQVGLRPEH-----YQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPT 181
Cdd:PLN03232 698 NILFGSDF-ES-------ERYWRAIDVTALQHDLDLLPGRdlteiGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599702 182 SALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRHVaDDVLVMYLGRPAEMGPADKLYEN 244
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKDELKGKTR-VLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-185 |
4.65e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.77 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 35 FELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGAskDQRRQLrrdvqmvfqnPYASLNPRQKIGDQL 114
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFM----------AYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599702 115 AEPLLINTALSREERREKVQQMMRQVGLrPEHYQRYPHMFSGGQRQRIALARaMMLQPKVL-VADEPTSALD 185
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-185 |
4.76e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 40 GKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIA--------GQEVKgasKDQRRQLRRDVQMVFQNPYASLNPRQKIG 111
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylPQEPQ---LDPTKTVRENVEEGVAEIKDALDRFNEIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 112 DQLAEPLLINTALSREERR--EKVQ-----QMMRQV-----GLR-PEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVAD 178
Cdd:TIGR03719 108 AKYAEPDADFDKLAAEQAElqEIIDaadawDLDSQLeiamdALRcPPWDADVTKL-SGGERRRVALCRLLLSKPDMLLLD 186
|
....*..
gi 15599702 179 EPTSALD 185
Cdd:TIGR03719 187 EPTNHLD 193
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-192 |
6.74e-06 |
|
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: 46.77 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQE---------VKGASKDQrrqlrrdvqMVFQNP 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfssqfswiMPGTIKEN---------IIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 101 YASLNPRQKI-GDQLAEPLLintalsreERREKVQQMMRQVGLrpehyqryphMFSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:cd03291 124 YDEYRYKSVVkACQLEEDIT--------KFPEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|...
gi 15599702 180 PTSALDVSIQAQV 192
Cdd:cd03291 186 PFGYLDVFTEKEI 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-233 |
8.93e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 34 SFEL------EAGKTLAVVGESGCGKSTLARALtlieeptSGSLKIA-GQEVKGASKDQ--RRQLRRDVQMVFQNPYA-S 103
Cdd:PRK13409 87 GFKLyglpipKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlGDYEEEPSWDEvlKRFRGTELQNYFKKLYNgE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 104 LNPRQKIG--DQLAEPLLINT--ALSREERREKVQQMMRQVGLRPEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADE 179
Cdd:PRK13409 160 IKVVHKPQyvDLIPKVFKGKVreLLKKVDERGKLDEVVERLGLENILDRDISEL-SGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599702 180 PTSALDVSIQAQVLNLFMDLQQQfrtAYVF-ISHNLAVVRHVADDVLVMYlGRPA 233
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEG---KYVLvVEHDLAVLDYLADNVHIAY-GEPG 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-240 |
1.68e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.49 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYlGRPAE 234
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEPGV 151
|
....*.
gi 15599702 235 MGPADK 240
Cdd:cd03222 152 YGIASQ 157
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
21-214 |
3.54e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 21 FKGHAqvralNGVSFELEAGKTLaVVGESGCGKSTLARALTL-IEEPTSGSLKIAGQ-----------EVKGASKDQRRQ 88
Cdd:COG0419 10 FRSYR-----DTETIDFDDGLNL-IVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDlinvgseeasvELEFEHGGKRYR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 89 LRRDVQMVFQNPYASLNPRQKI-----GDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRY-----PHMFSGGQ 158
Cdd:COG0419 84 IERRQGEFAEFLEAKPSERKEAlkrllGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 159 RQRIALARAMMlqpkvLVADepTSALDVSIQAQVLNLFMDLQqqfrtayvFISHNL 214
Cdd:COG0419 164 RLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-230 |
5.49e-05 |
|
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: 45.00 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 9 DLTRHYEVSRgLFKGHAQvRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDqrrq 88
Cdd:TIGR01257 1936 DILRLNELTK-VYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 89 lrrdvqmVFQNpyASLNPRQKIGDQL---AEPLLINTALS--REERREKVQQM-MRQVGLRPeHYQRYPHMFSGGQRQRI 162
Cdd:TIGR01257 2010 -------VHQN--MGYCPQFDAIDDLltgREHLYLYARLRgvPAEEIEKVANWsIQSLGLSL-YADRLAGTYSGGNKRKL 2079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599702 163 ALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRtAYVFISHNLAVVRHVADDVLVMYLG 230
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-231 |
1.39e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 33 VSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSlkiagqevkgaskdqrrqlrrdvqmVFQNP---YASLNPRQK 109
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT-------------------------VFRSAkvrMAVFSQHHV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 IG-DQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDV-S 187
Cdd:PLN03073 583 DGlDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdA 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599702 188 IQAQVLNLFMdlqqqFRTAYVFISHNLAVVRHVADDVLVMYLGR 231
Cdd:PLN03073 663 VEALIQGLVL-----FQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-268 |
2.03e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMML---QPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRhVADDVLvmylgr 231
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTV-VIIEHNMHVVK-VADYVL------ 882
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15599702 232 paEMGP----------ADKLYENPLH---PYTRAL---LSATPAIHPDPTKPK 268
Cdd:PRK00635 883 --ELGPeggnlggyllASCSPEELIHlhtPTAKALrpyLSSPQELPYLPDPSP 933
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-252 |
2.72e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAgqevkgaskdqrrqlrRDVQMVFQNPYaslnprqk 109
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQAW-------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 110 igdqlaepllINTALSR-------EERREKVQQMMRQVGLRPEHYQRYPHM----------FSGGQRQRIALARAMMLQP 172
Cdd:PTZ00243 732 ----------IMNATVRgnilffdEEDAARLADAVRVSQLEADLAQLGGGLeteigekgvnLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 173 KVLVADEPTSALDVSIQAQVlnlfmdLQQQFRTAY-----VFISHNLAVVRHvADDVLVMYLGRPAEMGPADKLYENPLH 247
Cdd:PTZ00243 802 DVYLLDDPLSALDAHVGERV------VEECFLGALagktrVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLY 874
|
....*
gi 15599702 248 PYTRA 252
Cdd:PTZ00243 875 ATLAA 879
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-212 |
3.82e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLaraLTLIeeptsgslkiAGQEVKGASKD-----QRR-------QLRRDVQMV- 96
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTL---LSLI----------TGDHPQGYSNDltlfgRRRgsgetiwDIKKHIGYVs 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 97 --FQNPY-ASLNPRQKIGDQLAEPLLINTALSrEERREKVQQMMRQVGLRPEHYQRYPHMFSGGQrQRIAL-ARAMMLQP 172
Cdd:PRK10938 343 ssLHLDYrVSTSVRNVILSGFFDSIGIYQAVS-DRQQKLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLALiVRALVKHP 420
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599702 173 KVLVADEPTSALDvSIQAQVLNLFMD-LQQQFRTAYVFISH 212
Cdd:PRK10938 421 TLLILDEPLQGLD-PLNRQLVRRFVDvLISEGETQLLFVSH 460
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-228 |
4.70e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 28 RALNGVSFELEAGKTlAVVGESGCGKSTLARALTLI-----------------EEPTSGSLKI-----------AGQEVK 79
Cdd:COG3593 12 RSIKDLSIELSDDLT-VLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEIeltfgsllsrlLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 80 GASKDQRRQLRRDVQMVFQNPYASLNprQKIGDQLaEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYP-HMFSGGQ 158
Cdd:COG3593 91 EEDKEELEEALEELNEELKEALKALN--ELLSEYL-KELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPlDRLGSGF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599702 159 RQRI--ALARAMML-----QPKVLVADEPTSALDVSIQAQVLNLFMDLQQQfrTAYVFIS-HNLAVVRHV-ADDVLVMY 228
Cdd:COG3593 168 QRLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEK--PNQVIITtHSPHLLSEVpLENIRRLR 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-186 |
6.25e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 30 LNGVSFELEAGKTLAVVGESGCGKSTLaraLTLIEE-----------PTSGSLKIAGQEVKGASKD----------QRRQ 88
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTL---LALLKNeisadggsytfPGNWQLAWVNQETPALPQPaleyvidgdrEYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 89 LRRDVQMVfqNPYASLNPRQKIGDQLaepllinTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAM 168
Cdd:PRK10636 94 LEAQLHDA--NERNDGHAIATIHGKL-------DAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170
....*....|....*...
gi 15599702 169 MLQPKVLVADEPTSALDV 186
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDL 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
155-185 |
8.95e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 8.95e-04
10 20 30
....*....|....*....|....*....|.
gi 15599702 155 SGGQRQRIALARAMMLQPKVLVADEPTSALD 185
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-237 |
1.14e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAmmLQPKV-----LVADEPTSALDVSIQAQVLNLFMDLQQQFRTAyVFISHNLAVVRhVADDVLvmyl 229
Cdd:TIGR00630 831 SGGEAQRIKLAKE--LSKRStgrtlYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVIEHNLDVIK-TADYII---- 902
|
....*...
gi 15599702 230 grpaEMGP 237
Cdd:TIGR00630 903 ----DLGP 906
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-186 |
1.24e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 2 ETVLTARDLTRHYEVsrglfkgHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARAL------TLIeeptSGSLKIAG 75
Cdd:NF040905 255 EVVFEVKNWTVYHPL-------HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygRNI----SGTVFKDG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 76 QEVKgaskdqrrqlRRDVQMVFQN--PYASLNpRQKIGDQLAEPLLINTALSR----------EERRE-KVQQMMRQvGL 142
Cdd:NF040905 324 KEVD----------VSTVSDAIDAglAYVTED-RKGYGLNLIDDIKRNITLANlgkvsrrgviDENEEiKVAEEYRK-KM 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599702 143 R---PEHYQRYPHMfSGGQRQRIALARAMMLQPKVLVADEPTSALDV 186
Cdd:NF040905 392 NiktPSVFQKVGNL-SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
27-99 |
1.44e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599702 27 VRALNGVSFELEAGKTLaVVGESGCGKSTLARALTLI--EEPTSGSLKIAGQEVKGASK-DQRRQLRRDVQMVFQN 99
Cdd:pfam13476 6 FRSFRDQTIDFSKGLTL-ITGPNGSGKTTILDAIKLAlyGKTSRLKRKSGGGFVKGDIRiGLEGKGKAYVEITFEN 80
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-237 |
3.18e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 155 SGGQRQRIALARAMMLQ---PKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVfISHNLAVVRhVADDVLvmylgr 231
Cdd:cd03271 171 SGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV-IEHNLDVIK-CADWII------ 242
|
....*.
gi 15599702 232 paEMGP 237
Cdd:cd03271 243 --DLGP 246
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
39-78 |
5.43e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 5.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15599702 39 AGKTLAVVGESGCGKSTLARALTlieeptsGSLKIAGQEV 78
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALL-------PELVLATGEI 116
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
18-91 |
5.83e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599702 18 RGLFKGHAQVRALNGVSFELEAGKTLAVV-GESGCGKSTLARALT----------LIEEPTSGSL----KIA---GQEVK 79
Cdd:COG3267 20 RFLFLSPSHREALARLEYALAQGGGFVVLtGEVGTGKTTLLRRLLerlpddvkvaYIPNPQLSPAellrAIAdelGLEPK 99
|
90
....*....|...
gi 15599702 80 GASKDQR-RQLRR 91
Cdd:COG3267 100 GASKADLlRQLQE 112
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-214 |
8.85e-03 |
|
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: 36.57 E-value: 8.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599702 155 SGGQRQRIALARAMML---QPKVLVA-DEPTSALDVSIQAQVLNLFMDLQQQFRTaYVFISHNL 214
Cdd:cd03227 79 SGGEKELSALALILALaslKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLP 141
|
|
| |
